MCPP_PSEPK
ID MCPP_PSEPK Reviewed; 544 AA.
AC Q88IY8;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 103.
DE RecName: Full=Methyl-accepting chemotaxis protein McpP {ECO:0000305};
GN Name=mcpP {ECO:0000303|PubMed:26048936};
GN OrderedLocusNames=PP_2861 {ECO:0000312|EMBL:AAN68469.1};
OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950
OS / KT2440).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=160488;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x;
RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H.,
RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M.,
RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F.,
RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I.,
RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A.,
RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H.,
RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C.,
RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.;
RT "Complete genome sequence and comparative analysis of the metabolically
RT versatile Pseudomonas putida KT2440.";
RL Environ. Microbiol. 4:799-808(2002).
RN [2]
RP FUNCTION AS A CHEMORECEPTOR, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440;
RX PubMed=26048936; DOI=10.1128/aem.01529-15;
RA Garcia V., Reyes-Darias J.A., Martin-Mora D., Morel B., Matilla M.A.,
RA Krell T.;
RT "Identification of a chemoreceptor for C2 and C3 carboxylic acids.";
RL Appl. Environ. Microbiol. 81:5449-5457(2015).
CC -!- FUNCTION: Chemotactic-signal transducers respond to changes in the
CC concentration of attractants and repellents in the environment,
CC transduce a signal from the outside to the inside of the cell, and
CC facilitate sensory adaptation through the variation of the level of
CC methylation. McpP is a chemoreceptor that responds specifically to some
CC C2 and C3 carboxylic acids. Recognizes acetate, pyruvate, propionate,
CC and L-lactate. {ECO:0000269|PubMed:26048936, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene does not alter motility but
CC largely reduces chemotaxis to acetate, pyruvate, propionate, and L-
CC lactate. {ECO:0000269|PubMed:26048936}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000305}.
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DR EMBL; AE015451; AAN68469.1; -; Genomic_DNA.
DR RefSeq; NP_745005.1; NC_002947.4.
DR RefSeq; WP_010953767.1; NC_002947.4.
DR AlphaFoldDB; Q88IY8; -.
DR SMR; Q88IY8; -.
DR STRING; 160488.PP_2861; -.
DR EnsemblBacteria; AAN68469; AAN68469; PP_2861.
DR KEGG; ppu:PP_2861; -.
DR PATRIC; fig|160488.4.peg.3033; -.
DR eggNOG; COG0840; Bacteria.
DR HOGENOM; CLU_000445_107_21_6; -.
DR OMA; ITHLGEH; -.
DR PhylomeDB; Q88IY8; -.
DR BioCyc; PPUT160488:G1G01-3040-MON; -.
DR Proteomes; UP000000556; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR033480; sCache_2.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR Pfam; PF17200; sCache_2; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM01049; Cache_2; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00283; MA; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Chemotaxis; Membrane; Methylation; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..544
FT /note="Methyl-accepting chemotaxis protein McpP"
FT /id="PRO_0000438507"
FT TRANSMEM 12..32
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 50..70
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 213..267
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 272..508
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
SQ SEQUENCE 544 AA; 58659 MW; 48CB2AF5CE32E975 CRC64;
MNTLRSMSIS RRLWLILVVA VAMLVVLGLL MLRQIHGDLY QAKAEKTRHV VQTAAGVLAY
YQGLEAAGTL SREAAQQQAL QVVRALRYDH DDYFWINDLG PKMIMHPANP KLDDQDLSAI
RDPDGFAVFN EMVALARQQD AGPVNYRWPK PGASEPVAKT SYIQLFKPWG WIIGSGVYVD
DVQAEFARQL RDASLVGVGI ALLMALVVML IARSIARPLQ EAVQAMGNIA SGESDLTRRL
DTHGSDEITH LGEHFNRFNG KLQGVVGQLQ GAAHALAQSA GHVGDNAGAA QQRSAQQSLQ
MDQVATAVNE VTYAVQDVAK TAEQAAGEMR TAQQQVTHGQ QAIHGSLAQI DRLSLTIDEA
VQVIRDLAGH STRIGGVLDV IRSIAEQTNL LALNAAIEAA RAGEQGRGFA VVADEVRLLA
QRTAQSTAEI HTMIEHLQSQ SDAAVKAIDT SSEASRQTVE QAREAGASLD AINQVLNNLT
ALNASIASAT LQQSHVVEEI NRNVLDTAGL SQQTADAARQ SSDAGVALGR LSEELEQLLR
QFRV
