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MCPH_PSEPK
ID   MCPH_PSEPK              Reviewed;         645 AA.
AC   Q88R14;
DT   30-NOV-2016, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Methyl-accepting chemotaxis protein McpH {ECO:0000305};
GN   Name=mcpH {ECO:0000303|PubMed:26355499};
GN   OrderedLocusNames=PP_0320 {ECO:0000312|EMBL:AAN65951.1};
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=26355499; DOI=10.1111/mmi.13215;
RA   Fernandez M., Morel B., Corral-Lugo A., Krell T.;
RT   "Identification of a chemoreceptor that specifically mediates chemotaxis
RT   toward metabolizable purine derivatives.";
RL   Mol. Microbiol. 99:34-42(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. McpH is a chemoreceptor that binds and responds
CC       exclusively to intermediates of the purine degradation pathway.
CC       {ECO:0000269|PubMed:26355499, ECO:0000305}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Mutation abolishes chemotaxis toward xanthine,
CC       guanine and adenine. {ECO:0000269|PubMed:26355499}.
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000305}.
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DR   EMBL; AE015451; AAN65951.1; -; Genomic_DNA.
DR   RefSeq; NP_742487.1; NC_002947.4.
DR   RefSeq; WP_010951680.1; NC_002947.4.
DR   AlphaFoldDB; Q88R14; -.
DR   SMR; Q88R14; -.
DR   STRING; 160488.PP_0320; -.
DR   EnsemblBacteria; AAN65951; AAN65951; PP_0320.
DR   KEGG; ppu:PP_0320; -.
DR   PATRIC; fig|160488.4.peg.346; -.
DR   eggNOG; COG0840; Bacteria.
DR   HOGENOM; CLU_000445_107_19_6; -.
DR   OMA; MMSEIAE; -.
DR   PhylomeDB; Q88R14; -.
DR   BioCyc; PPUT160488:G1G01-353-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   Pfam; PF02743; dCache_1; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF00015; MCPsignal; 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..645
FT                   /note="Methyl-accepting chemotaxis protein McpH"
FT                   /id="PRO_0000438506"
FT   TRANSMEM        15..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        291..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          51..276
FT                   /note="Cache"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          314..368
FT                   /note="HAMP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT   DOMAIN          373..609
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
SQ   SEQUENCE   645 AA;  69825 MW;  8561D8B29DB162B8 CRC64;
     MRIWRKSIQL QLITSMGAAL LASILVVVII FTVALNRLTD RYLVDTALPA SIEAIRNDIE
     RMLGQPLVAA ADIAGNTLLR DWLAAGEDPA QAPQFIEYLT AAKQRNHAFT TLFASTETGH
     YYNENGLDRT LSRSNPKDKW FYGYIDSGAE RFINIDIDGA TGELALFIDY RVEKEGKLVG
     VAGMGLRMTE LSKLIHDFSF GEHGKVFLVR NDGLIQVHPD AAFSGKRQLA EQLGADAAKG
     VMTGGESLRS SRFSRDGERY LALGLPLRDL NWTLVAEVPE SEIYAQMHQA VWLTSLIGGA
     VALVSLLLVV LLARGLVRPI RRVTAALVQI GSGAGDLSHR LDDSRQDELG DLARGFNRFL
     DSQRSLIGEV LSTSERLRRA VEQVTQVVDN TAERSGRQQE MTEMVATAVH EMGLTVQDIA
     RNAGDAAQAS QSARDEALQA REVVQRSIRG IEGMSGDIGK AADAVSQLAD EVASVDEVLA
     VIRSISEQTN LLALNAAIEA ARAGEMGRGF AVVADEVRTL ARRTQLSTDE VQQMIQRLKL
     GAGSAVSSMQ AGQQATGSGV ESSQRTGASL SAITDQVEHI SDMNHQVATA TEEQSAVTEE
     INRTVQGISD LARETAAEVQ GCREECQALR GLADDLARQM GGFRL
 
 
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