MCPA_PSEPK
ID MCPA_PSEPK Reviewed; 643 AA.
AC Q88KP1;
DT 30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 100.
DE RecName: Full=Methyl-accepting chemotaxis protein McpA {ECO:0000305};
GN Name=mcpA {ECO:0000303|PubMed:26662997};
GN Synonyms=pctB {ECO:0000312|EMBL:AAN67862.1};
GN OrderedLocusNames=PP_2249 {ECO:0000312|EMBL:AAN67862.1};
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=26662997; DOI=10.1111/1462-2920.13170;
RA Corral-Lugo A., de la Torre J., Matilla M.A., Fernandez M., Morel B.,
RA Espinosa-Urgel M., Krell T.;
RT "Assessment of the contribution of chemoreceptor-based signaling to biofilm
RT formation.";
RL Environ. Microbiol. 18:3355-3372(2016).
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. McpA is a chemoreceptor that binds to 12 different L-amino
CC acids and mediates chemotaxis toward these amino acids.
CC {ECO:0000269|PubMed:26662997, ECO:0000305}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Mutant shows different biofilm kinetics, reaching
CC maximal biofilm formation earlier than wild type. Mutation does not
CC affect the capacity to colonize the plant root.
CC {ECO:0000269|PubMed:26662997}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000305}.
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DR EMBL; AE015451; AAN67862.1; -; Genomic_DNA.
DR RefSeq; NP_744398.1; NC_002947.4.
DR AlphaFoldDB; Q88KP1; -.
DR SMR; Q88KP1; -.
DR STRING; 160488.PP_2249; -.
DR EnsemblBacteria; AAN67862; AAN67862; PP_2249.
DR KEGG; ppu:PP_2249; -.
DR PATRIC; fig|160488.4.peg.2374; -.
DR eggNOG; COG0840; Bacteria.
DR HOGENOM; CLU_000445_107_19_6; -.
DR OMA; QTAKQMQ; -.
DR PhylomeDB; Q88KP1; -.
DR BioCyc; PPUT160488:G1G01-2395-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:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR InterPro; IPR033479; dCache_1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR029151; Sensor-like_sf.
DR Pfam; PF02743; dCache_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR SMART; SM00304; HAMP; 2.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF103190; SSF103190; 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..643
FT /note="Methyl-accepting chemotaxis protein McpA"
FT /id="PRO_0000438504"
FT TRANSMEM 24..44
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 293..313
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DOMAIN 49..273
FT /note="Cache"
FT /evidence="ECO:0000255"
FT DOMAIN 312..366
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 371..607
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
SQ SEQUENCE 643 AA; 68646 MW; 20F207694AD29914 CRC64;
MSALRPPLIG SRSRNMNLKF RHKILLSACG VVVLAFALFT LYNDYLQRNT IRQNIEASVQ
QSGALTASSV QNWMSGRILV LENLAQDIGQ QGAGDTLAGL IEQPSYTRNF LFTYLGQANG
EFTQRPDAQM PAGYDPRQRP WYGAAANAGQ TVLTAPYQGA VGGLMVTIAT PVKSKRNGEL
IGVVGGDVTL DTLVEIINSV DFGGIGHAFL ADANGQVIVS PNKDQVMKNL KDIYPGSNLR
VAAGMQDVTL DGQDRIISFA PVAGLPSAQW YIGLSIDRDK AYAALSQFRT SAIIAMLIAV
AAIAGLLGLL IPVLMSPLTT MGRAMRDIAE GEGDLTRRLA VQNKDEFGEL ATSFNRFVER
IHASISEVSS ATRLVHDLSE KVVSASNASI IGSEEQSMRT NSVAAAINEL GAATQEIARN
AADASQHASG ASEQAHGGRE VVEEAISAMT ALSQRISESC AQIETLNAST DEIGKILDVI
KGISQQTNLL ALNAAIEAAR AGEAGRGFAV VADEVRNLAH RTQESAEEIH RMITSLQVGS
REAVHTMNTS QVSSEQTVQV ANQAGERLAS VTQRIGEIDG MNQSVATATE EQTAVVESLN
LDITQINALN QQGVENLNET LRHCDQLAQQ AGRLKQLVGS FRI
