SitesBLAST
Comparing WP_104485187.1 NCBI__GCF_002936955.1:WP_104485187.1 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)
P02911 Lysine/arginine/ornithine-binding periplasmic protein; LAO-binding protein from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 4 papers)
40% identity, 99% coverage: 3:256/257 of query aligns to 1:259/260 of P02911
- D33 (≠ E32) binding L-arginine; binding L-lysine; binding L-ornithine; mutation to A: Decreases arginine and histidine binding affinity.
- Y36 (= Y35) mutation to A: Shows a drastic decrease in arginine and histidine binding affinity.
- D52 (= D51) mutation to A: Shows a drastic decrease in arginine and histidine binding affinity.
- C60 (= C59) modified: Disulfide link with 67
- C67 (= C66) modified: Disulfide link with 60
- F74 (≠ W73) mutation to A: Shows a drastic decrease in arginine and histidine binding affinity.
- S91 (≠ A90) binding L-arginine; binding L-ornithine; mutation to A: Has no effect on the arginine and histidine binding affinity.
- S92 (= S91) binding L-arginine; binding L-lysine; binding L-ornithine; mutation to A: Decreases arginine and histidine binding affinity.
- S94 (= S93) binding L-arginine; binding L-lysine; binding L-ornithine; mutation to A: Decreases arginine and histidine binding affinity.
- R99 (= R98) binding L-arginine; binding L-lysine; binding L-ornithine; mutation to A: Shows a drastic decrease in arginine and histidine binding affinity.
- L139 (≠ Q138) mutation to K: Changes ligand specificity. Can bind glutamine. Still able to bind basic amino acids, however, with 1000-fold less affinity for arginine.; mutation to Q: Does not affect ligand preference.
- T143 (= T142) binding L-arginine; binding L-lysine; binding L-ornithine
- D183 (≠ N180) binding L-arginine; binding L-ornithine; mutation to A: Shows a drastic decrease in arginine and histidine binding affinity.
5owfA Structure of a lao-binding protein mutant with glutamine (see paper)
42% identity, 89% coverage: 27:256/257 of query aligns to 3:234/235 of 5owfA
1lstA Three-dimensional structures of the periplasmic lysine-, arginine-, ornithine-binding protein with and without a ligand (see paper)
42% identity, 89% coverage: 27:256/257 of query aligns to 6:237/238 of 1lstA
1lahE Structural bases for multiple ligand specificity of the periplasmic lysine-, arginine-, ornithine-binding protein (see paper)
42% identity, 89% coverage: 27:256/257 of query aligns to 6:237/238 of 1lahE
1lagE Structural bases for multiple ligand specificity of the periplasmic lysine-, arginine-, ornithine-binding protein (see paper)
42% identity, 89% coverage: 27:256/257 of query aligns to 6:237/238 of 1lagE
- binding histidine: Y14 (= Y35), F52 (≠ W73), S69 (≠ A90), S70 (= S91), L71 (≠ M92), S72 (= S93), R77 (= R98), L117 (≠ Q138), S120 (= S141), Q122 (≠ H143), D161 (≠ N180)
1lafE Structural bases for multiple ligand specificity of the periplasmic lysine-, arginine-, ornithine-binding protein (see paper)
42% identity, 89% coverage: 27:256/257 of query aligns to 6:237/238 of 1lafE
- binding arginine: D11 (≠ E32), Y14 (= Y35), F52 (≠ W73), S69 (≠ A90), S70 (= S91), S72 (= S93), R77 (= R98), L117 (≠ Q138), S120 (= S141), T121 (= T142), Q122 (≠ H143), D161 (≠ N180)
P02910 Histidine-binding periplasmic protein; HBP from Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720) (see 2 papers)
40% identity, 91% coverage: 25:257/257 of query aligns to 26:260/260 of P02910
- E40 (≠ S39) mutation to K: Decrease in ATPase-inducing activity and histidine transport; when associated with K-47.
- K42 (≠ T41) mutation to E: Increases ATPase-inducing activity and histidine transport; when associated with K-47.
- E47 (= E46) mutation to K: Decrease in ATPase-inducing activity and histidine transport; when associated with K-40. Increases ATPase-inducing activity and histidine transport; when associated with E-42.
- D171 (= D168) mutation D->A,N: Strong decrease in ATPase-inducing activity and histidine transport.
- R176 (= R173) mutation R->D,S: Strong decrease in ATPase-inducing activity and histidine transport.
- D178 (= D175) mutation to A: Slight decrease in ATPase-inducing activity and histidine transport.
Sites not aligning to the query:
1hslA Refined 1.89 angstroms structure of the histidine-binding protein complexed with histidine and its relationship with many other active transport(slash)chemosensory receptors (see paper)
40% identity, 91% coverage: 25:257/257 of query aligns to 4:238/238 of 1hslA
P0AEU0 Histidine-binding periplasmic protein; HBP from Escherichia coli (strain K12) (see 3 papers)
39% identity, 91% coverage: 25:257/257 of query aligns to 26:260/260 of P0AEU0
- C60 (= C59) modified: Disulfide link with 67
- C67 (= C66) modified: Disulfide link with 60
- S91 (≠ A90) binding L-histidine
- S92 (= S91) binding L-histidine
- S94 (= S93) binding L-histidine
- R99 (= R98) binding L-histidine
- T143 (= T142) binding L-histidine
- D183 (≠ N180) binding L-histidine
Sites not aligning to the query:
3tqlA Structure of the amino acid abc transporter, periplasmic amino acid- binding protein from coxiella burnetii. (see paper)
45% identity, 87% coverage: 27:250/257 of query aligns to 4:225/225 of 3tqlA
2y7iA Structural basis for high arginine specificity in salmonella typhimurium periplasmic binding protein stm4351. (see paper)
37% identity, 88% coverage: 25:250/257 of query aligns to 6:227/228 of 2y7iA
- binding arginine: Y16 (= Y35), E20 (≠ S39), F54 (≠ W73), A71 (= A90), G72 (≠ S91), D74 (≠ S93), R79 (= R98), E118 (≠ Q138), T121 (≠ S141), T122 (= T142), D160 (≠ N180)
- binding zinc ion: H9 (≠ R28), D23 (≠ T42), D25 (≠ E44), D55 (= D74), D67 (= D86), D140 (≠ G160)
5orgA Structure of the periplasmic binding protein (pbp) occj from a. Tumefaciens b6 in complex with octopine. (see paper)
37% identity, 89% coverage: 25:254/257 of query aligns to 4:254/257 of 5orgA
- binding octopine: E11 (= E32), Y14 (= Y35), W52 (= W73), A69 (= A90), A70 (≠ S91), M71 (= M92), S72 (= S93), R77 (= R98), N92 (≠ S113), Q140 (= Q138), T143 (≠ S141), T144 (= T142), N183 (= N180)
4zv2A An ancestral arginine-binding protein bound to glutamine (see paper)
38% identity, 87% coverage: 27:250/257 of query aligns to 6:223/225 of 4zv2A
4zv1A An ancestral arginine-binding protein bound to arginine (see paper)
37% identity, 87% coverage: 27:250/257 of query aligns to 6:225/226 of 4zv1A
- binding arginine: E11 (= E32), F14 (≠ Y35), F52 (≠ W73), A69 (= A90), G70 (≠ S91), M71 (= M92), T72 (≠ S93), R77 (= R98), Q117 (= Q138), S120 (= S141), T121 (= T142), D161 (≠ N180)
5itoA Structure of the periplasmic binding protein m117n-noct from a. Tumefaciens in complex with octopine (see paper)
31% identity, 90% coverage: 23:253/257 of query aligns to 1:252/255 of 5itoA
- binding octopine: E10 (= E32), Y13 (= Y35), W51 (= W73), A68 (= A90), A69 (≠ S91), G71 (≠ S93), R76 (= R98), Q139 (= Q138), T142 (≠ S141), S143 (≠ T142), H144 (= H143), S181 (≠ N180)
5ovzA High resolution structure of the pbp noct in complex with nopaline (see paper)
31% identity, 90% coverage: 23:253/257 of query aligns to 1:252/259 of 5ovzA
- binding N-[(1S)-4-carbamimidamido-1-carboxybutyl]-D-glutamic acid: E10 (= E32), Y13 (= Y35), W51 (= W73), A68 (= A90), A69 (≠ S91), G71 (≠ S93), R76 (= R98), M91 (≠ S113), Q139 (= Q138), T142 (≠ S141), S143 (≠ T142), H144 (= H143), S181 (≠ N180), V213 (= V214)
5otcA Structure of the periplasmic binding protein (pbp) noct from agrobacterium tumefaciens c58 in complex with noroctopinic acid. (see paper)
31% identity, 89% coverage: 24:253/257 of query aligns to 1:251/256 of 5otcA
- binding (2~{S})-5-azanyl-2-(2-hydroxy-2-oxoethylamino)pentanoic acid: E9 (= E32), Y12 (= Y35), W50 (= W73), A68 (≠ S91), G70 (≠ S93), R75 (= R98), Q138 (= Q138), T141 (≠ S141), S142 (≠ T142), H143 (= H143), S180 (≠ N180)
5otaA Structure of the periplasmic binding protein (pbp) noct from agrobacterium tumefaciens c58 in complex with octopinic acid (see paper)
31% identity, 89% coverage: 24:253/257 of query aligns to 1:251/254 of 5otaA
- binding (2~{S})-5-azanyl-2-[[(2~{R})-1-oxidanyl-1-oxidanylidene-propan-2-yl]amino]pentanoic acid: E9 (= E32), Y12 (= Y35), W50 (= W73), A68 (≠ S91), G70 (≠ S93), R75 (= R98), M90 (≠ S113), Q138 (= Q138), T141 (≠ S141), S142 (≠ T142), H143 (= H143), S180 (≠ N180)
5ot9A Structure of the periplasmic binding protein (pbp) noct from a.Tumefaciens c58 in complex with histopine. (see paper)
31% identity, 89% coverage: 24:253/257 of query aligns to 1:251/254 of 5ot9A