Comparing WP_101442772.1 NCBI__GCF_002846395.1:WP_101442772.1 to proteins with known functional sites using BLASTp with E ≤ 0.001.
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Found 20 (the maximum) hits to proteins with known functional sites (download)
P75831 Macrolide export ATP-binding/permease protein MacB; EC 7.6.2.- from Escherichia coli (strain K12) (see paper)
44% identity, 100% coverage: 1:231/231 of query aligns to 1:232/648 of P75831
1f3oA Crystal structure of mj0796 atp-binding cassette (see paper)
43% identity, 96% coverage: 4:225/231 of query aligns to 1:228/232 of 1f3oA
P75957 Lipoprotein-releasing system ATP-binding protein LolD; EC 7.6.2.- from Escherichia coli (strain K12) (see paper)
45% identity, 95% coverage: 4:223/231 of query aligns to 5:226/233 of P75957
7mdyC Lolcde nucleotide-bound
45% identity, 95% coverage: 4:223/231 of query aligns to 2:223/226 of 7mdyC
7arlD Lolcde in complex with lipoprotein and adp (see paper)
45% identity, 95% coverage: 4:222/231 of query aligns to 2:222/222 of 7arlD
1l2tA Dimeric structure of mj0796, a bacterial abc transporter cassette (see paper)
43% identity, 96% coverage: 4:225/231 of query aligns to 1:228/230 of 1l2tA
7v8iD Lolcd(e171q)e with bound amppnp in nanodiscs (see paper)
45% identity, 95% coverage: 4:223/231 of query aligns to 4:225/229 of 7v8iD
5xu1B Structure of a non-canonical abc transporter from streptococcus pneumoniae r6 (see paper)
44% identity, 96% coverage: 4:224/231 of query aligns to 3:224/226 of 5xu1B
5ws4A Crystal structure of tripartite-type abc transporter macb from acinetobacter baumannii (see paper)
44% identity, 95% coverage: 4:223/231 of query aligns to 4:224/650 of 5ws4A
2pclA Crystal structure of abc transporter with complex (aq_297) from aquifex aeolicus vf5
43% identity, 96% coverage: 2:223/231 of query aligns to 1:219/223 of 2pclA
5lj7A Structure of aggregatibacter actinomycetemcomitans macb bound to atp (p21) (see paper)
42% identity, 96% coverage: 4:225/231 of query aligns to 3:225/592 of 5lj7A
5lilA Structure of aggregatibacter actinomycetemcomitans macb bound to atpys (p21) (see paper)
42% identity, 96% coverage: 4:225/231 of query aligns to 3:225/615 of 5lilA
8g4cB Bceabs atpgs high res tm (see paper)
38% identity, 95% coverage: 4:222/231 of query aligns to 3:223/248 of 8g4cB
7tchB Bceab e169q variant atp-bound conformation (see paper)
38% identity, 95% coverage: 4:222/231 of query aligns to 2:222/245 of 7tchB
P30750 Methionine import ATP-binding protein MetN; EC 7.4.2.11 from Escherichia coli (strain K12) (see 3 papers)
37% identity, 89% coverage: 4:208/231 of query aligns to 1:206/343 of P30750
Sites not aligning to the query:
6cvlD Crystal structure of the escherichia coli atpgs-bound metni methionine abc transporter in complex with its metq binding protein (see paper)
37% identity, 89% coverage: 4:208/231 of query aligns to 2:207/344 of 6cvlD
3tuzC Inward facing conformations of the metni methionine abc transporter: cy5 semet soak crystal form (see paper)
37% identity, 89% coverage: 4:208/231 of query aligns to 2:207/344 of 3tuzC
Sites not aligning to the query:
3tuiC Inward facing conformations of the metni methionine abc transporter: cy5 native crystal form (see paper)
37% identity, 89% coverage: 4:208/231 of query aligns to 2:207/344 of 3tuiC
6z4wA Ftse structure from streptococcus pneumoniae in complex with adp (space group p 1) (see paper)
37% identity, 98% coverage: 3:228/231 of query aligns to 2:225/230 of 6z4wA
A0A0H2ZM82 Cell division ATP-binding protein FtsE from Streptococcus pneumoniae serotype 2 (strain D39 / NCTC 7466) (see paper)
37% identity, 98% coverage: 3:228/231 of query aligns to 2:225/230 of A0A0H2ZM82
>WP_101442772.1 NCBI__GCF_002846395.1:WP_101442772.1
MSTILEINNLKKTYNSGDRHLTVLEGINITLQAGDTCAIVGPSGSGKTTLLGLCAGLDRA
SSGSVVLNGVQLDNLSEDARAQVRNQYVGFIFQNFQLIPTLTALENVMVPLELRGERNVQ
GQAMELLARVGLAERHDHYPTQLSGGEQQRVSLARAFSNRPTILFADEPTGNLDEETGEK
VEKLLFELNREAGTTLVLVTHDLELAEKTQRIIRIKGGHVVSDTKTAESVH
Or try a new SitesBLAST search
SitesBLAST's database includes (1) SwissProt entries with experimentally-supported functional features; and (2) protein structures with bound ligands, from the BioLip database.
Lawrence Berkeley National Laboratory