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Database: UniProt
Entry: P54576
LinkDB: P54576
Original site: P54576 
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   29-OCT-2014, entry version 99.
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       {ECO:0000269|PubMed:9353924, ECO:0000269|PubMed:9721285}.
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. {ECO:0000269|PubMed:9353924}.
CC   -!- PTM: Some glutamine residues are deamidated to glutamate by CheD
CC       and subsequently methylated. {ECO:0000269|PubMed:12011078,
CC       ECO:0000269|PubMed:9353924}.
CC   -!- SIMILARITY: Contains 1 cache domain. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 HAMP domain. {ECO:0000255|PROSITE-
CC       ProRule:PRU00102}.
CC   -!- SIMILARITY: Contains 1 methyl-accepting transducer domain.
CC       {ECO:0000255|PROSITE-ProRule:PRU00284}.
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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   InParanoid; P54576; -.
DR   KO; K03406; -.
DR   OrthoDB; EOG67HJTT; -.
DR   PhylomeDB; P54576; -.
DR   BioCyc; BSUB:BSU13950-MONOMER; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
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   InterPro; IPR029151; Sensor-like.
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   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; 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. {ECO:0000255}.
FT   TRANSMEM      9     29       Helical. {ECO:0000255}.
FT   TOPO_DOM     30    276       Extracellular. {ECO:0000255}.
FT   TRANSMEM    277    297       Helical. {ECO:0000255}.
FT   TOPO_DOM    298    655       Cytoplasmic. {ECO:0000255}.
FT   DOMAIN      148    225       Cache.
FT   DOMAIN      298    350       HAMP. {ECO:0000255|PROSITE-
FT                                ProRule:PRU00102}.
FT   DOMAIN      369    619       Methyl-accepting transducer.
FT                                {ECO:0000255|PROSITE-ProRule:PRU00284}.
FT   CONFLICT     95     96       KQ -> NE (in Ref. 1; CAA66052).
FT                                {ECO:0000305}.
FT   CONFLICT    115    120       EMFTYP -> RNVYIS (in Ref. 1; CAA66052).
FT                                {ECO:0000305}.
FT   CONFLICT    125    135       AEDYDPTSRPW -> LRITIQHQDM (in Ref. 1;
FT                                CAA66052). {ECO:0000305}.
FT   CONFLICT    190    190       M -> L (in Ref. 1; CAA66052).
FT                                {ECO:0000305}.
FT   CONFLICT    376    376       T -> R (in Ref. 1; CAA66052).
FT                                {ECO:0000305}.
FT   CONFLICT    438    438       D -> H (in Ref. 1; CAA66052).
FT                                {ECO:0000305}.
FT   CONFLICT    457    457       V -> E (in Ref. 1; CAA66052).
FT                                {ECO:0000305}.
FT   CONFLICT    492    492       A -> R (in Ref. 1; CAA66052).
FT                                {ECO:0000305}.
FT   CONFLICT    645    647       ELM -> DVI (in Ref. 1; CAA66052).
FT                                {ECO:0000305}.
FT   CONFLICT    651    651       A -> R (in Ref. 1; CAA66052).
FT                                {ECO:0000305}.
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
//
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