ID MCPC_BACSU Reviewed; 655 AA.
AC P54576;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 2.
DT 01-MAY-2013, entry version 92.
DE RecName: Full=Methyl-accepting chemotaxis protein McpC;
GN Name=mcpC; Synonyms=prg71; OrderedLocusNames=BSU13950;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, METHYLATION, EXPRESSION,
RP AND INDUCTION.
RC STRAIN=168;
RX PubMed=9353924;
RA Mueller J., Schiel S., Ordal G.W., Saxild H.H.;
RT "Functional and genetic characterization of mcpC, which encodes a
RT third methyl-accepting chemotaxis protein in Bacillus subtilis.";
RL Microbiology 143:3231-3240(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
RA Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=19383706; DOI=10.1099/mic.0.027839-0;
RA Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G.,
RA Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus
RT subtilis 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP FUNCTION IN RESPONSE TO PTS SUBSTRATES.
RX PubMed=9721285;
RA Garrity L.F., Schiel S.L., Merrill R., Reizer J., Saier M.H. Jr.,
RA Ordal G.W.;
RT "Unique regulation of carbohydrate chemotaxis in Bacillus subtilis by
RT the phosphoenolpyruvate-dependent phosphotransferase system and the
RT methyl-accepting chemotaxis protein McpC.";
RL J. Bacteriol. 180:4475-4480(1998).
RN [5]
RP DEAMIDATION BY CHED.
RX PubMed=12011078; DOI=10.1074/jbc.M201334200;
RA Kristich C.J., Ordal G.W.;
RT "Bacillus subtilis CheD is a chemoreceptor modification enzyme
RT required for chemotaxis.";
RL J. Biol. Chem. 277:25356-25362(2002).
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
CC of methylation. All amino acids serve as attractants in
CC B.subtilis, they appear to cause an increase in the turnover
CC methyl groups, leading to methylation of an unidentified acceptor,
CC while repellents have been shown to cause a decrease in methyl
CC group turnover. The methyl groups are added by a methyltransferase
CC and removed by a methylesterase. McpC is required for taxis to
CC cysteine, proline, threonine, glycine, serine, lysine, valine and
CC arginine and for aspartate, glutamine, histidine and glutamate.
CC Primarily mediates response to positive stimulus of PTS
CC carbohydrates. Greatly influences the duration or magnitude of the
CC response to negative PTS carbohydrate stimulus.
CC -!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
CC -!- INDUCTION: Induced by SigD. Expression increases in the late-
CC exponential growth-phase and is maximal during the early-
CC stationary phase.
CC -!- PTM: Some glutamine residues are deamidated to glutamate by CheD
CC and subsequently methylated.
CC -!- SIMILARITY: Contains 1 cache domain.
CC -!- SIMILARITY: Contains 1 HAMP domain.
CC -!- SIMILARITY: Contains 1 methyl-accepting transducer domain.
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DR EMBL; X97385; CAA66052.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13268.2; -; Genomic_DNA.
DR PIR; A69656; A69656.
DR RefSeq; NP_389278.2; NC_000964.3.
DR ProteinModelPortal; P54576; -.
DR SMR; P54576; 298-350, 357-654.
DR STRING; 224308.BSU13950; -.
DR PaxDb; P54576; -.
DR EnsemblBacteria; CAB13268; CAB13268; BSU13950.
DR GeneID; 936206; -.
DR KEGG; bsu:BSU13950; -.
DR PATRIC; 18974573; VBIBacSub10457_1478.
DR GenoList; BSU13950; -.
DR eggNOG; COG0840; -.
DR HOGENOM; HOG000261838; -.
DR KO; K03406; -.
DR ProtClustDB; CLSK887208; -.
DR BioCyc; BSUB:BSU13950-MONOMER; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004871; F:signal transducer activity; IEA:UniProtKB-KW.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR InterPro; IPR004010; Cache_domain.
DR InterPro; IPR003660; HAMP_linker_domain.
DR InterPro; IPR004089; MCPsignal_dom.
DR Pfam; PF02743; Cache_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00283; MA; 1.
DR PROSITE; PS00538; CHEMOTAXIS_TRANSDUC_1; FALSE_NEG.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Chemotaxis; Complete proteome; Membrane; Methylation;
KW Reference proteome; Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1 655 Methyl-accepting chemotaxis protein McpC.
FT /FTId=PRO_0000110558.
FT TOPO_DOM 1 8 Cytoplasmic (Potential).
FT TRANSMEM 9 29 Helical; (Potential).
FT TOPO_DOM 30 276 Extracellular (Potential).
FT TRANSMEM 277 297 Helical; (Potential).
FT TOPO_DOM 298 655 Cytoplasmic (Potential).
FT DOMAIN 148 225 Cache.
FT DOMAIN 298 350 HAMP.
FT DOMAIN 369 619 Methyl-accepting transducer.
FT CONFLICT 95 96 KQ -> NE (in Ref. 1; CAA66052).
FT CONFLICT 115 120 EMFTYP -> RNVYIS (in Ref. 1; CAA66052).
FT CONFLICT 125 135 AEDYDPTSRPW -> LRITIQHQDM (in Ref. 1;
FT CAA66052).
FT CONFLICT 190 190 M -> L (in Ref. 1; CAA66052).
FT CONFLICT 376 376 T -> R (in Ref. 1; CAA66052).
FT CONFLICT 438 438 D -> H (in Ref. 1; CAA66052).
FT CONFLICT 457 457 V -> E (in Ref. 1; CAA66052).
FT CONFLICT 492 492 A -> R (in Ref. 1; CAA66052).
FT CONFLICT 645 647 ELM -> DVI (in Ref. 1; CAA66052).
FT CONFLICT 651 651 A -> R (in Ref. 1; CAA66052).
SQ SEQUENCE 655 AA; 72031 MW; CD5485BD8D8D693A CRC64;
MFKKLHMKIA VFVSIMLIIT VVLLMLSSYL TLKPMITEDG KNTTQNVTQS LEQNIELQLK
SYAISLSRLA NGELTHTFVT KPSKEASRLF HDDIKQIKDN DDYVAMAYIG TAKKEMFTYP
KADFAEDYDP TSRPWYKLAA ETPDQVVWTE PYKDVVTGDM IVTASKAILD RQKVIGVASY
DLKLSAIQSM VNKQKVPYKG FAFLADASGN LLAHPSNQGK NISKDQTLQT IASEKKGIQD
VNGKMVVYQT IGETGWKVGT QFDTDQLMWI SDKMNRANLW ISLIALIITI ILSYFLAKTI
TGPIQQLIVK TKAVSAGDLT VRAESKSKDE VGILTRDFNL MVENMKEMVE QVRLSSGKVS
DTSEQLTAVA AETNETSGQI AKAIEEVAAG ASEQASEVET INEKSESLST KIRQIAEEAG
GIKERSKSSE DASYKGLDAL GQLLMKSNEA NMETKKVETM LLDLENQTKN IEEVVTAISN
ISDQTNLLAL NASIEAARAG ESGRGFAVVA DEVRKLAEQS ALSTKHISET VKLIQLETKE
ASHAMVEASR MNDEQNSAIH ETGEVLNTIT AEMQSLVQGI DHIYAEIQRM SEEQLAISEA
IQSISAISQE SAAAAEEVNA STDEQLVTLD KVKHSTETLK HASQELMNTI AKFTL
//
