Other Characterized Proteins Similar to PA5505

GapMind for catabolism of small carbon sources

Other Characterized Proteins Similar to PA5505

Finding the characterized proteins for PA5505 (L-histidine ABC transporter, substrate-binding component) in L-histidine catabolism

Or see clustering for step PA5505

Or see all steps for L-histidine catabolism

Or cluster curated proteins matching a keyword

Definition of PA5505

Curated sequence Q9HT68: Probable TonB-dependent receptor, component of L-Histidine uptake porter, MetIQN

Fetched 1 sequences

Running ublast to find other characterized proteins with 40% identity and 70% coverage

Found hits to 3 other characterized sequences. (Found 4 hits including self hits.)

Close sequences

(Sequences that are similar to these will not be high-confidence candidates for PA5505.)

METQ_BACSU / O32167 Methionine-binding lipoprotein MetQ from Bacillus subtilis (strain 168)
TC 3.A.1.24.2 / O32167 MetQ (R) (aka YusA), component of The L- and D-methionine porter (also transports methionine sulfoxide from Bacillus subtilis subsp. subtilis str. 168
PFams: Lipoprotein_9
Heteromeric, 274 amino acids: PaperBLAST, CDD, SwissProt::O32167
42% identical to

TC 3.A.1.24.5 / Q9HT68 Probable TonB-dependent receptor, component of L-Histidine uptake porter, MetIQN from Pseudomonas aeruginosa (strain ATCC 15692 / PAO1 / 1C / PRS 101 / LMG 12228)
PFams: Lipoprotein_9
Heteromeric, 260 amino acids: PaperBLAST, CDD

b0197 L-methionine/D-methionine ABC transporter membrane anchored binding protein (EC 7.4.2.11) from Escherichia coli K-12 substr. MG1655
P28635 L-methionine/D-methionine ABC transporter membrane anchored binding protein (EC 7.4.2.11) from Escherichia coli (strain K12)
METQ_ECOLI / P28635 D-methionine-binding lipoprotein MetQ from Escherichia coli (strain K12)
TC 3.A.1.24.1 / P28635 MetQ, D-methionine-binding lipoprotein, 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
GB|ABE05723.1 D-methionine-binding lipoprotein MetQ from Escherichia coli K12
PFams: Lipoprotein_9
Heteromeric, 271 amino acids: PaperBLAST, CDD, CharProtDB::CH_008911
46% identical to

b3661 lipoprotein-28 from Escherichia coli K-12 substr. MG1655
PFams: Lipoprotein_9
272 amino acids: PaperBLAST, CDD, ecocyc::EG10657-MONOMER
40% identical to