MCPC_BACSU
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 03-AUG-2022, entry version 129.
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, AND
RP INDUCTION.
RC STRAIN=168;
RX PubMed=9353924; DOI=10.1099/00221287-143-10-3231;
RA Mueller J., Schiel S., Ordal G.W., Saxild H.H.;
RT "Functional and genetic characterization of mcpC, which encodes a third
RT 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., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., 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., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., 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., Sekowska A.,
RA Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
RT "From a consortium sequence to a unified sequence: the Bacillus subtilis
RT 168 reference genome a decade later.";
RL Microbiology 155:1758-1775(2009).
RN [4]
RP FUNCTION IN RESPONSE TO PTS SUBSTRATES.
RX PubMed=9721285; DOI=10.1128/jb.180.17.4475-4480.1998;
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 the
RT phosphoenolpyruvate-dependent phosphotransferase system and the methyl-
RT 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 required for
RT chemotaxis.";
RL J. Biol. Chem. 277:25356-25362(2002).
RN [6]
RP INTERACTION WITH FLOT, AND SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=23651456; DOI=10.1111/mmi.12252;
RA Bach J.N., Bramkamp M.;
RT "Flotillins functionally organize the bacterial membrane.";
RL Mol. Microbiol. 88:1205-1217(2013).
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. All amino acids serve as attractants in B.subtilis, they
CC appear to cause an increase in the turnover methyl groups, leading to
CC methylation of an unidentified acceptor, while repellents have been
CC shown to cause a decrease in methyl group turnover. The methyl groups
CC are added by a methyltransferase and removed by a methylesterase. McpC
CC is required for taxis to cysteine, proline, threonine, glycine, serine,
CC lysine, valine and arginine and for aspartate, glutamine, histidine and
CC glutamate. 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 -!- SUBUNIT: Interacts with FloT. {ECO:0000269|PubMed:23651456}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:23651456};
CC Multi-pass membrane protein {ECO:0000255}. Membrane raft
CC {ECO:0000269|PubMed:23651456}; Multi-pass membrane protein
CC {ECO:0000255}. Note=Present in detergent-resistant membrane (DRM)
CC fractions that may be equivalent to eukaryotic membrane rafts; these
CC rafts include proteins involved in signaling, molecule trafficking and
CC protein secretion. {ECO:0000269|PubMed:23651456}.
CC -!- INDUCTION: Induced by SigD. Expression increases in the late-
CC exponential growth-phase and is maximal during the early-stationary
CC phase. {ECO:0000269|PubMed:9353924}.
CC -!- PTM: Some glutamine residues are deamidated to glutamate by CheD and
CC subsequently methylated. {ECO:0000269|PubMed:12011078,
CC ECO:0000269|PubMed:9353924}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000305}.
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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 RefSeq; WP_003245443.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P54576; -.
DR SMR; P54576; -.
DR STRING; 224308.BSU13950; -.
DR jPOST; P54576; -.
DR PaxDb; P54576; -.
DR PRIDE; P54576; -.
DR EnsemblBacteria; CAB13268; CAB13268; BSU_13950.
DR GeneID; 936206; -.
DR KEGG; bsu:BSU13950; -.
DR PATRIC; fig|224308.179.peg.1521; -.
DR eggNOG; COG0840; Bacteria.
DR InParanoid; P54576; -.
DR OMA; VMSEITH; -.
DR PhylomeDB; P54576; -.
DR BioCyc; BSUB:BSU13950-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0050918; P:positive chemotaxis; IDA:CACAO.
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; 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; Membrane; Methylation; Reference proteome;
KW Transducer; Transmembrane; Transmembrane helix.
FT CHAIN 1..655
FT /note="Methyl-accepting chemotaxis protein McpC"
FT /id="PRO_0000110558"
FT TOPO_DOM 1..8
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 9..29
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 30..276
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 277..297
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 298..655
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 148..225
FT /note="Cache"
FT DOMAIN 298..350
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 369..619
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT CONFLICT 95..96
FT /note="KQ -> NE (in Ref. 1; CAA66052)"
FT /evidence="ECO:0000305"
FT CONFLICT 115..120
FT /note="EMFTYP -> RNVYIS (in Ref. 1; CAA66052)"
FT /evidence="ECO:0000305"
FT CONFLICT 125..135
FT /note="AEDYDPTSRPW -> LRITIQHQDM (in Ref. 1; CAA66052)"
FT /evidence="ECO:0000305"
FT CONFLICT 190
FT /note="M -> L (in Ref. 1; CAA66052)"
FT /evidence="ECO:0000305"
FT CONFLICT 376
FT /note="T -> R (in Ref. 1; CAA66052)"
FT /evidence="ECO:0000305"
FT CONFLICT 438
FT /note="D -> H (in Ref. 1; CAA66052)"
FT /evidence="ECO:0000305"
FT CONFLICT 457
FT /note="V -> E (in Ref. 1; CAA66052)"
FT /evidence="ECO:0000305"
FT CONFLICT 492
FT /note="A -> R (in Ref. 1; CAA66052)"
FT /evidence="ECO:0000305"
FT CONFLICT 645..647
FT /note="ELM -> DVI (in Ref. 1; CAA66052)"
FT /evidence="ECO:0000305"
FT CONFLICT 651
FT /note="A -> R (in Ref. 1; CAA66052)"
FT /evidence="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
