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Protein

Methyl-accepting chemotaxis protein McpS

Gene

mcpS

Organism
Pseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Chemotactic-signal transducers respond to changes in the concentration of attractants and repellents in the environment, transduce a signal from the outside to the inside of the cell, and facilitate sensory adaptation through the variation of the level of methylation. McpS is a specific chemoreceptor for 6 tricarboxylic acid (TCA) cycle intermediates (succinate, fumarate, malate, oxaloacetate, citrate and isocitrate), butyrate and acetate. Malate, succinate, fumarate and oxaloacetate cause the strongest chemotactic response.2 Publications

Enzyme regulationi

Binding of citrate to the ligand-binding domain reduces the chemotaxis towards the strong attractants such as malate and succinate. However, in physiologically relevant niches, citrate is mostly complexed with magnesium or calcium ions, and does not bind McpS.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei138Acetate1 Publication1
Binding sitei183Acetate1 Publication1
Binding sitei187Acetate1 Publication1
Binding sitei236Acetate1 Publication1
Binding sitei254Malate/succinate1 Publication1
Binding sitei258Malate1 Publication1

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Transducer

Keywords - Biological processi

Chemotaxis

Names & Taxonomyi

Protein namesi
Recommended name:
Methyl-accepting chemotaxis protein McpS
Gene namesi
Name:mcpS
Ordered Locus Names:PP_4658
OrganismiPseudomonas putida (strain ATCC 47054 / DSM 6125 / NCIMB 11950 / KT2440)
Taxonomic identifieri160488 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000000556 Componenti: Chromosome

Subcellular locationi

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Topological domaini1 – 13CytoplasmicSequence analysisAdd BLAST13
Transmembranei14 – 34HelicalSequence analysisAdd BLAST21
Topological domaini35 – 288PeriplasmicSequence analysisAdd BLAST254
Transmembranei289 – 309HelicalSequence analysisAdd BLAST21
Topological domaini310 – 639CytoplasmicSequence analysisAdd BLAST330

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Membrane

Pathology & Biotechi

Disruption phenotypei

Mutant fails to respond to succinate but responds to toluene.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi60R → A: Abolishes binding of malate, fumarate, oxaloacetate, succinate, isocitrate and butyrate. Decreases binding of citrate. 1 Publication1
Mutagenesisi63R → A: Abolishes binding of malate, fumarate, oxaloacetate, succinate, isocitrate and butyrate. Decreases binding of citrate. 1 Publication1
Mutagenesisi183R → A: Decreases binding of acetate. Does not affect binding of malate. 1 Publication1
Mutagenesisi254R → A: Abolishes binding of malate, fumarate, oxaloacetate, succinate and isocitrate. Decreases binding of citrate. Does not affect binding of butyrate. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004248261 – 639Methyl-accepting chemotaxis protein McpSAdd BLAST639

Post-translational modificationi

Methylated by CheR2.1 Publication

Keywords - PTMi

Methylation

Interactioni

Subunit structurei

Homodimer. Exists as a mixture of monomers and dimers in solution. Ligand binding stabilizes the dimeric form.2 Publications

Protein-protein interaction databases

DIPiDIP-60088N.
STRINGi160488.PP_4658.

Structurei

Secondary structure

1639
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi46 – 68Combined sources23
Turni69 – 71Combined sources3
Helixi73 – 96Combined sources24
Helixi100 – 157Combined sources58
Helixi162 – 191Combined sources30
Helixi195 – 218Combined sources24
Helixi220 – 222Combined sources3
Helixi223 – 276Combined sources54

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YFAX-ray1.80A/B46-283[»]
2YFBX-ray1.90A/B46-283[»]
ProteinModelPortaliQ88E10.
SMRiQ88E10.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini41 – 283HBMPROSITE-ProRule annotationAdd BLAST243
Domaini310 – 362HAMPPROSITE-ProRule annotationAdd BLAST53
Domaini367 – 603Methyl-accepting transducerPROSITE-ProRule annotationAdd BLAST237

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni60 – 65Malate/succinate binding6

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili191 – 245Sequence analysisAdd BLAST55

Sequence similaritiesi

Contains 1 HAMP domain.PROSITE-ProRule annotation
Contains 1 HBM domain.PROSITE-ProRule annotation
Contains 1 methyl-accepting transducer domain.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG4105C8Q. Bacteria.
COG0840. LUCA.
HOGENOMiHOG000222019.
KOiK03406.
OMAiQYMIANG.

Family and domain databases

CDDicd06225. HAMP. 1 hit.
InterProiIPR004090. Chemotax_Me-accpt_rcpt.
IPR003660. HAMP_dom.
IPR032255. HBM.
IPR004089. MCPsignal_dom.
[Graphical view]
PfamiPF00672. HAMP. 1 hit.
PF16591. HBM. 1 hit.
PF00015. MCPsignal. 1 hit.
[Graphical view]
PRINTSiPR00260. CHEMTRNSDUCR.
SMARTiSM00304. HAMP. 2 hits.
SM01358. HBM. 1 hit.
SM00283. MA. 1 hit.
[Graphical view]
PROSITEiPS50111. CHEMOTAXIS_TRANSDUC_2. 1 hit.
PS50885. HAMP. 1 hit.
PS51753. HBM. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q88E10-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNSWFANISV NLKLGLGFGL VLVLTGLLAL TGWTSLGSLI DRSNWMGDIG
60 70 80 90 100
QLNKDLTDLR IARLQYMIAN GDDTAAANTL AKLDAFSKQQ AYLATTFKSP
110 120 130 140 150
ENVKLLGELG DTISAYKLSL NKMRQGYDAT RAARVSMDSS AIRADQAMDA
160 170 180 190 200
LSQEVMARPE ADSVRLAQYQ LISKARQQLL QVRIDVRGYI AENSSANEQA
210 220 230 240 250
ALRQLDAALA DTDNLKRQLP SEDARLQQFE NAVLAYRDAV RQFRDAVANI
260 270 280 290 300
TTSRAEMTVQ GADIVKRSDA LYQIQLERRD IESTQARSLQ AIATLLALLV
310 320 330 340 350
GVLAAVLITR QITRPLQDTL VAVEKIASGD LTQHMRVTRR DELGVLQQGI
360 370 380 390 400
ARMGTTLREL ISGIRDGVTQ IASAAEELSA VTEQTSAGAN SQKVETDQVA
410 420 430 440 450
TAMHEMAATV QEVARNAEQA SHAATGADDE ARAGDRVVGE AIGQIERLAE
460 470 480 490 500
DMHRSTEAMN LLQQESQKIG SVMDVIKSVA EQTNLLALNA AIEAARAGEA
510 520 530 540 550
GRGFAVVADE VRGLAQRTQK STEEIEELIA SLQHGTQQVA NAMQGSRALT
560 570 580 590 600
DSSVELARKA GSSLESITST VSSIQSMNQQ IAAAAEQQSA VAEEISRSIL
610 620 630
NVRDVSEQTA AASDETAASS VELARLGGQL QTLVSQFRV
Length:639
Mass (Da):68,764
Last modified:June 1, 2003 - v1
Checksum:i827C3ADD979A87DB
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE015451 Genomic DNA. Translation: AAN70231.1.
RefSeqiNP_746767.1. NC_002947.4.
WP_010955314.1. NC_002947.4.

Genome annotation databases

GeneIDi1042609.
KEGGippu:PP_4658.
PATRICi19948058. VBIPsePut30601_4966.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE015451 Genomic DNA. Translation: AAN70231.1.
RefSeqiNP_746767.1. NC_002947.4.
WP_010955314.1. NC_002947.4.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2YFAX-ray1.80A/B46-283[»]
2YFBX-ray1.90A/B46-283[»]
ProteinModelPortaliQ88E10.
SMRiQ88E10.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

DIPiDIP-60088N.
STRINGi160488.PP_4658.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi1042609.
KEGGippu:PP_4658.
PATRICi19948058. VBIPsePut30601_4966.

Phylogenomic databases

eggNOGiENOG4105C8Q. Bacteria.
COG0840. LUCA.
HOGENOMiHOG000222019.
KOiK03406.
OMAiQYMIANG.

Family and domain databases

CDDicd06225. HAMP. 1 hit.
InterProiIPR004090. Chemotax_Me-accpt_rcpt.
IPR003660. HAMP_dom.
IPR032255. HBM.
IPR004089. MCPsignal_dom.
[Graphical view]
PfamiPF00672. HAMP. 1 hit.
PF16591. HBM. 1 hit.
PF00015. MCPsignal. 1 hit.
[Graphical view]
PRINTSiPR00260. CHEMTRNSDUCR.
SMARTiSM00304. HAMP. 2 hits.
SM01358. HBM. 1 hit.
SM00283. MA. 1 hit.
[Graphical view]
PROSITEiPS50111. CHEMOTAXIS_TRANSDUC_2. 1 hit.
PS50885. HAMP. 1 hit.
PS51753. HBM. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiMCPS_PSEPK
AccessioniPrimary (citable) accession number: Q88E10
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 22, 2014
Last sequence update: June 1, 2003
Last modified: November 2, 2016
This is version 82 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.