Searching for up to 100 curated homologs for 6937828 FitnessBrowser__SB2B:6937828 (301 a.a.)
Found high-coverage hits (≥70%) to 56 curated proteins.
You can add additional sequences or change the %identity threshold for inclusion. Once you have selected sequences, you can build an alignment and a tree.
TC 3.A.1.131.1 / P42332 BcrA, component of The 2 or 3 component bacitracin-resistance efflex pump, BcrAB or BcrABC (Podlesek et al., 1995; Bernard et al., 2003) (BcrA is most similar to SpaF (3.A.1.124.2), but BcrB (5-6 TMSs) is only distantly related to other ABC2-type membrane proteins (Wang et al., 2009). BcrC is not sufficiently similar to detect similarity in BLAST searches. BcrC (5TMSs) belongs to the PAP2 phosphatase superfamily and may not be a contituent of the BcrAB transporter. Transcription is regulated by BcrR, a one-component transmembrane signal transduction system from Bacillus licheniformis (see paper)
bcrA / GB|AAA99504.1 bacitracin ABC transporter, ATP-binding protein BcrA from Bacillus licheniformis (see paper)
36% identity, 70% coverage of query (129 bits)
mutF / GI|9802352 mutacin ABC transporter, ATP-binding protein MutF from Streptococcus mutans (see paper)
35% identity, 74% coverage of query (125 bits)
ABCA1_HUMAN / O95477 Phospholipid-transporting ATPase ABCA1; ATP-binding cassette sub-family A member 1; ATP-binding cassette transporter 1; ABC-1; ATP-binding cassette 1; Cholesterol efflux regulatory protein; EC 7.6.2.1 from Homo sapiens (Human) (see 34 papers)
TC 3.A.1.211.14 / O95477 cAMP-dependent and sulfonylurea-sensitive anion transporter, ABCA1 of 2261 aas. Key gatekeeper influencing and possibly catalyzing intracellular phospholipid and cholesterol transport from Homo sapiens
35% identity, 75% coverage of query (123 bits)
TC 3.A.1.211.1 / P41233 The cholesterol/phospholipid flippase, ABC1 (called ABCA1 in humans; Tangier disease proteins; 2261 aas; sp: O95477). An amphipathic helical region of the N-terminal barrel of the phospholipid transfer protein (PLTP) is critical for ABCA1-dependent cholesterol efflux (Oram et al., 2008). PLTP helix 144-163 removes lipid domains formed by ABCA1, stabilizing ABCA1, interacting with phospholipids, and promoting phospholipid transfer by direct interactions with ABCA1. May transport sphingosine-1-phosphate (Kobayashi et al., 2009). May protect from cardiovascular disease and diabetes from Mus musculus (Mouse) (see 7 papers)
Abca1 ATP-binding cassette sub-family A member 1 from Mus musculus (see paper)
35% identity, 75% coverage of query (123 bits)
ABCA1_MOUSE / P41233 Phospholipid-transporting ATPase ABCA1; ATP-binding cassette sub-family A member 1; ATP-binding cassette transporter 1; ABC-1; ATP-binding cassette 1; EC 7.6.2.1 from Mus musculus (Mouse) (see 2 papers)
35% identity, 75% coverage of query (123 bits)
BCRA_ENTFL / Q5WNX0 Bacitracin transport ATP-binding protein BcrA from Enterococcus faecalis (Streptococcus faecalis) (see 2 papers)
35% identity, 71% coverage of query (122 bits)
7tbwA / O95477 The structure of atp-bound abca1 (see paper)
35% identity, 70% coverage of query (121 bits)
FTSE_STRP2 / A0A0H2ZM82 Cell division ATP-binding protein FtsE from Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) (see 3 papers)
FTSE_STRR6 / Q8DQH4 Cell division ATP-binding protein FtsE from Streptococcus pneumoniae (strain ATCC BAA-255 / R6) (see paper)
6z4wA / Q8DQH4 Ftse structure from streptococcus pneumoniae in complex with adp (space group p 1) (see paper)
33% identity, 71% coverage of query (118 bits)
6z67B Ftse structure of streptococcus pneumoniae in complex with amppnp at 2.4 a resolution
33% identity, 71% coverage of query (115 bits)
7tbyA / O95477 The structure of human abca1 in nanodisc (see paper)
34% identity, 70% coverage of query (112 bits)
1oxvD Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus
32% identity, 70% coverage of query (112 bits)
1oxvA Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus
32% identity, 70% coverage of query (112 bits)
GLCV_SACS2 / Q97UY8 Glucose import ATP-binding protein GlcV; EC 7.5.2.- from Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) (Sulfolobus solfataricus) (see 3 papers)
TC 3.A.1.1.13 / Q97UY8 GlcV, component of Glucose, mannose, galactose porter from Sulfolobus solfataricus (see 3 papers)
1oxuA / Q97UY8 Crystal structure of glcv, the abc-atpase of the glucose abc transporter from sulfolobus solfataricus (see paper)
32% identity, 70% coverage of query (112 bits)
7o12B / P19844 Abc transporter nosdfy, amppnp-bound in gdn (see paper)
32% identity, 97% coverage of query (107 bits)
MALK_SALTY / P19566 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see paper)
32% identity, 74% coverage of query (107 bits)
7m1qA / P78363 Human abca4 structure in complex with n-ret-pe (see paper)
31% identity, 75% coverage of query (106 bits)
7o17B Abc transporter nosdfy e154q, atp-bound in lipid nanodisc
32% identity, 97% coverage of query (106 bits)
MalK / b4035 maltose ABC transporter ATP binding subunit (EC 7.5.2.1) from Escherichia coli K-12 substr. MG1655 (see 31 papers)
MalK / P68187 maltose ABC transporter ATP binding subunit (EC 7.5.2.1) from Escherichia coli (strain K12) (see 29 papers)
MALK_ECOLI / P68187 Maltose/maltodextrin import ATP-binding protein MalK; EC 7.5.2.1 from Escherichia coli (strain K12) (see 6 papers)
P68187 ABC-type maltose transporter (subunit 3/3) (EC 7.5.2.1) from Escherichia coli (see paper)
TC 3.A.1.1.1 / P68187 Maltose/maltodextrin import ATP-binding protein MalK aka B4035, component of Maltooligosaccharide porter. The 3-D structure has been reported by Oldham et al. (2007). An altering access mechanism has been suggested for the maltose transporter resulting from rigid-body rotations (Khare et al., 2009). Bordignon et al. (2010) and Schneider et al. (2012) have reviewed the extensive knowledge available on MalEFGK2, its mode of action and its regulatory interactions from Escherichia coli (see 17 papers)
malK / RF|NP_418459 maltose/maltodextrin import ATP-binding protein malK; EC 3.6.3.19 from Escherichia coli K12 (see 18 papers)
31% identity, 74% coverage of query (102 bits)
2awnB / P68187 Crystal structure of the adp-mg-bound e. Coli malk (crystallized with atp-mg) (see paper)
32% identity, 72% coverage of query (102 bits)
1q12A Crystal structure of the atp-bound e. Coli malk
32% identity, 72% coverage of query (102 bits)
3puyA Crystal structure of an outward-facing mbp-maltose transporter complex bound to amp-pnp after crystal soaking of the pretranslocation state
32% identity, 72% coverage of query (102 bits)
3puxA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-bef3
32% identity, 72% coverage of query (102 bits)
3puwA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-alf4
32% identity, 72% coverage of query (102 bits)
3puvA Crystal structure of an outward-facing mbp-maltose transporter complex bound to adp-vo4
32% identity, 72% coverage of query (102 bits)
Build an alignment for 6937828 and 24 homologs with ≥ 30% identity
Or download the sequences
ECSA_BACSU / P55339 ABC-type transporter ATP-binding protein EcsA from Bacillus subtilis (strain 168) (see paper)
TC 3.A.1.143.1 / P55339 ABC-type transporter ATP-binding protein EcsA, component of The exoprotein (including α-amylase) secretion system, EcsAB(C) (Leskelä et al., 1999). Also may play roles in sporulation, competence (Leskelä et al., 1996) and transformation using purified DNA (Takeno et al., 2011). An involvement of EcsC in transport is not established, but it is homologous to the C-terminus of the P-type ATPase, 3.A.3.31.2 from Bacillus subtilis (strain 168) (see 3 papers)
29% identity, 78% coverage of query (99.4 bits)
6z5uK Cryo-em structure of the a. Baumannii mlabdef complex bound to appnhp
33% identity, 74% coverage of query (97.4 bits)
MetN / b0199 L-methionine/D-methionine ABC transporter ATP binding subunit (EC 7.4.2.11) from Escherichia coli K-12 substr. MG1655 (see 4 papers)
MetN / P30750 L-methionine/D-methionine ABC transporter ATP binding subunit (EC 7.4.2.11) from Escherichia coli (strain K12) (see 3 papers)
METN_ECOLI / P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 7 papers)
P30750 ABC-type methionine transporter (subunit 2/2) (EC 7.4.2.11) from Escherichia coli (see 3 papers)
TC 3.A.1.24.1 / P30750 MetN, D-methionine transport ATP-binding protein, component of The L- and D-methionine porter (also transports formyl-L-methionine and other methionine derivatives) (Zhang et al., 2003). The 3.7A structure of MetNI has been solved. An allosteric regulatory mechanism operates at the level of transport activity, so increased intracellular levels of the transported ligand stabilize an inward-facing, ATPase-inactive state of MetNI to inhibit further ligand translocation into the cell from Escherichia coli (see 5 papers)
29% identity, 80% coverage of query (96.7 bits)
3tuzC Inward facing conformations of the metni methionine abc transporter: cy5 semet soak crystal form
29% identity, 80% coverage of query (95.1 bits)
3tuiC Inward facing conformations of the metni methionine abc transporter: cy5 native crystal form
29% identity, 80% coverage of query (95.1 bits)
6cvlD / P30750 Crystal structure of the escherichia coli atpgs-bound metni methionine abc transporter in complex with its metq binding protein (see paper)
29% identity, 80% coverage of query (95.1 bits)
2d62A / O57933 Crystal structure of multiple sugar binding transport atp- binding protein
26% identity, 85% coverage of query (94.0 bits)
LolD / b1117 lipoprotein release complex - ATP binding subunit from Escherichia coli K-12 substr. MG1655 (see 2 papers)
LolD / P75957 lipoprotein release complex - ATP binding subunit from Escherichia coli (strain K12) (see paper)
LOLD_ECOLI / P75957 Lipoprotein-releasing system ATP-binding protein LolD; EC 7.6.2.- from Escherichia coli (strain K12) (see paper)
TC 3.A.1.125.1 / P75957 LolD aka B1117, component of Lipoprotein translocation system (translocates lipoproteins from the inner membrane to periplasmic chaperone, LolA, which transfers the lipoproteins to an outer membrane receptor, LolB, which anchors the lipoprotein to the outer membrane of the Gram-negative bacterial cell envelope) (see 1.B.46; Narita et al., 2003; Ito et al., 2006; Watanabe et al., 2007). The structure of ligand-bound LolCDE has been solved (Ito et al., 2006). LolC and LolE each have 4 TMSs (1+3). Unlike most ATP binding cassette transporters mediating the transmembrane flux of substrates, the LolCDE complex catalyzes the extrusion of lipoproteins anchored to the outer leaflet of the inner membrane. The LolCDE complex is unusual in that it can be purified as a liganded form, which is an intermediate of the lipoprotein release reaction (Taniguchi and Tokuda, 2008). LolCDE has been reconstituted from separated subunits from Escherichia coli (see 5 papers)
lolD / GB|BAA35937.2 lipoprotein releasing system, ATP-binding protein; EC 3.6.3.- from Escherichia coli K12 (see 5 papers)
33% identity, 71% coverage of query (93.2 bits)
7mdyC Lolcde nucleotide-bound
33% identity, 71% coverage of query (93.2 bits)
7v8iD / P75957 Lolcd(e171q)e with bound amppnp in nanodiscs (see paper)
33% identity, 71% coverage of query (91.7 bits)
4hluC / Q9X1Z1 Structure of the ecfa-a' heterodimer bound to adp (see paper)
31% identity, 73% coverage of query (89.0 bits)
8dncA Cryoem structure of the a. Aeolicus wzmwzt transporter bound to the native o antigen and adp
28% identity, 72% coverage of query (87.8 bits)
8dkuA / O67181 Cryoem structure of the a. Aeolicus wzmwzt transporter bound to the native o antigen (see paper)
28% identity, 72% coverage of query (87.8 bits)
ABCAH_MOUSE / E9PX95 ATP-binding cassette sub-family A member 17 from Mus musculus (Mouse) (see 2 papers)
27% identity, 93% coverage of query (83.6 bits)
4zirB Crystal structure of ecfaa' heterodimer bound to amppnp
32% identity, 73% coverage of query (82.4 bits)
sugC / P9WQI3 ABC-type trehalose transporter ATP-binding protein from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
SUGC_MYCTU / P9WQI3 Trehalose import ATP-binding protein SugC; MtbSugC; Nucleotide-binding domain of SugABC transporter; NBD of SugABC transporter; SugABC transporter ATPase SugC; EC 7.5.2.- from Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv) (see 2 papers)
TC 3.A.1.1.31 / O50454 PROBABLE SUGAR-TRANSPORT ATP-BINDING PROTEIN ABC TRANSPORTER SUGC, component of The trehalose-recycling ABC transporter, LpqY-SugA-SugB-SugC (essential for virulence) from Mycobacterium tuberculosis (see 2 papers)
28% identity, 74% coverage of query (81.6 bits)
7zoaB / Q2YQ73 Cryo-em structure of cgt abc transporter in presence of cbg substrate (see paper)
32% identity, 73% coverage of query (78.6 bits)
P63389 Probable ATP-binding protein YheS from Escherichia coli (strain K12)
28% identity, 80% coverage of query (77.8 bits)
YHES_ECOL6 / A0A0H2VBH0 Probable ATP-binding protein YheS from Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC) (see paper)
28% identity, 80% coverage of query (77.8 bits)
YJQ1_SCHPO / Q9USH9 Uncharacterized ABC transporter ATP-binding protein C825.01 from Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast) (see paper)
27% identity, 70% coverage of query (75.1 bits)
SapD / b1291 putrescine ABC exporter ATP binding protein SapD (EC 7.6.2.16) from Escherichia coli K-12 substr. MG1655 (see 5 papers)
SapD / P0AAH4 putrescine ABC exporter ATP binding protein SapD (EC 7.6.2.16) from Escherichia coli (strain K12) (see 5 papers)
SAPD_ECOLI / P0AAH4 Putrescine export system ATP-binding protein SapD from Escherichia coli (strain K12) (see 2 papers)
26% identity, 81% coverage of query (74.3 bits)
8g4cB / O34697 Bceabs atpgs high res tm (see paper)
26% identity, 72% coverage of query (73.6 bits)
7tchB Bceab e169q variant atp-bound conformation
25% identity, 72% coverage of query (72.4 bits)
CFTR / P13569 cystic fibrosis transmembrane conductance regulator (EC 5.6.1.6) from Homo sapiens (see 23 papers)
CFTR_HUMAN / P13569 Cystic fibrosis transmembrane conductance regulator; CFTR; ATP-binding cassette sub-family C member 7; Channel conductance-controlling ATPase; cAMP-dependent chloride channel; EC 5.6.1.6 from Homo sapiens (Human) (see 120 papers)
P13569 adenylate kinase (EC 2.7.4.3); channel-conductance-controlling ATPase (EC 5.6.1.6) from Homo sapiens (see 17 papers)
TC 3.A.1.202.1 / P13569 Cystic fibrosis transmembrane conductance regulator (CFTR) (also called ABCC7); cyclic AMP-dependent chloride channel; also catalyzes nucleotide (ATP-ADP)-dependent glutathione and glutathione-conjugate flux (Kogan et al., 2003) (may also activate inward rectifying K+ channels). The underlying mechanism by which ATP hydrolysis controls channel opening is described by Gadsby et al., 2006. The most common cause of cystic fibrosis (CF) is defective folding of a cystic fibrosis transmembrane conductance regulator (CFTR) mutant lacking Phe508 (DeltaF508)(Riordan, 2008). The DeltaF508 protein appears to be trapped in a prefolded state with incomplete packing of the transmembrane segments, a defect that can be repaired by direct interaction with correctors such as corr-4a, VRT-325, and VRT-532 (Wang et al., 2007). CFTR interacts directly with MRP4 (3.A.1.208.7) to control Cl- secretion (Li et al., 2007). It has intrinsic adenylate kinase activity that may be of functional importance (Randak and Welsh, 2007). The intact CFTR protein mediates ATPase rather than adenylate kinase activity (Ramjeesingh et al., 2008). Regulated by Na+/H+ exchange regulatory cofactors (NHERF; O14745; TC #8.A.24.1.1) (Seidler et al., 2009). Regulated by protein kinase A and C phosphorylation (Csanády et al., 2010). It is also activated by membrane stretch induced by negative pressures (Zhang et al., 2010). TMS6 plays roles in gating and permeation (Bai et al., 2010; 2011). The 3-D structure revealed the probable location of the channel gate (Rosenberg et al., 2011). Conformational changes opening the CFTR chloride channel pore, coupled to ATP-dependent gating, have been studied (Wang and Linsdell, 2012). Alternating access to the transmembrane domain of CFTR has been demonstrated from Homo sapiens (Human) (see 71 papers)
CFTR / RF|NP_000483.3 cystic fibrosis transmembrane conductance regulator from Homo sapiens (see paper)
25% identity, 73% coverage of query (72.0 bits)
5uakA / P13569 Dephosphorylated, atp-free human cystic fibrosis transmembrane conductance regulator (cftr) (see paper)
25% identity, 73% coverage of query (72.0 bits)
7svrA The complex of dephosphorylated human cystic fibrosis transmembrane conductance regulator (cftr) and lumacaftor (vx-809)
25% identity, 73% coverage of query (71.6 bits)
6o2pA Complex of ivacaftor with cystic fibrosis transmembrane conductance regulator (cftr)
25% identity, 73% coverage of query (70.9 bits)
6o1vA Complex of human cystic fibrosis transmembrane conductance regulator (cftr) and glpg1837
25% identity, 73% coverage of query (70.9 bits)
MDR3_HUMAN / P21439 Phosphatidylcholine translocator ABCB4; ATP-binding cassette sub-family B member 4; Multidrug resistance protein 3; P-glycoprotein 3; EC 7.6.2.1 from Homo sapiens (Human) (see 28 papers)
TC 3.A.1.201.3 / P21439 Short chain fatty acid phosphatidylcholine translocase (phospholipid flippase), MDR3; AbcB4; Pgy3 from Homo sapiens (Human) (see 15 papers)
29% identity, 72% coverage of query (70.1 bits)
8j5qD / P9WQJ5 Cryo-em structure of mycobacterium tuberculosis oppabcd in the pre- translocation state (see paper)
28% identity, 70% coverage of query (69.3 bits)
8j5tD Cryo-em structure of mycobacterium tuberculosis oppabcd in the catalytic intermediate state
28% identity, 70% coverage of query (68.2 bits)
8j5sD Cryo-em structure of mycobacterium tuberculosis oppabcd in the pre- catalytic intermediate state
28% identity, 70% coverage of query (68.2 bits)
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Lawrence Berkeley National Laboratory