MCPB_BACSU
ID MCPB_BACSU Reviewed; 662 AA.
AC P39215;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Methyl-accepting chemotaxis protein McpB;
DE AltName: Full=H3;
GN Name=mcpB; OrderedLocusNames=BSU31260;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], METHYLATION AT GLN-371; GLN-595; GLU-630
RP AND GLU-637, DEAMIDATION AT GLN-371 AND GLN-595, AND FUNCTION.
RC STRAIN=168 / OI1085;
RX PubMed=8188684; DOI=10.1016/s0021-9258(17)36752-2;
RA Hanlon D.W., Ordal G.W.;
RT "Cloning and characterization of genes encoding methyl-accepting chemotaxis
RT proteins in Bacillus subtilis.";
RL J. Biol. Chem. 269:14038-14046(1994).
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 TO 360; 402 AND 450.
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 METHYLATION AT GLN-371; GLN-595; GLU-630 AND GLU-637, DEAMIDATION AT
RP GLN-371 AND 595, AND MUTAGENESIS OF GLN-371; GLN-595; GLU-630 AND GLU-637.
RX PubMed=10825179; DOI=10.1074/jbc.m004001200;
RA Zimmer M.A., Tiu J., Collins M.A., Ordal G.W.;
RT "Selective methylation changes on the Bacillus subtilis chemotaxis receptor
RT McpB promote adaptation.";
RL J. Biol. Chem. 275:24264-24272(2000).
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. McpB
CC is required for taxis towards asparagine, aspartate, glutamine, and
CC histidine. {ECO:0000269|PubMed:8188684}.
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 -!- PTM: Some glutamine residues are deamidated to glutamate by CheD and
CC subsequently methylated. {ECO:0000269|PubMed:10825179,
CC ECO:0000269|PubMed:12011078, ECO:0000269|PubMed:8188684}.
CC -!- PTM: The demethylation is selective. Gln-371 is demethylated only upon
CC asparagine addition whereas Glu-637 is demethylated only upon
CC asparagine removal. Glu-630 appears indiscriminate and is demethylated
CC upon both addition and removal of asparagine.
CC -!- MISCELLANEOUS: Only chemotaxis towards asparagine is completely
CC deficient in the absence of McpB.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000305}.
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DR EMBL; L29189; AAA20554.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15104.2; -; Genomic_DNA.
DR PIR; A54078; A54078.
DR RefSeq; NP_391004.2; NC_000964.3.
DR RefSeq; WP_003243461.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; P39215; -.
DR SMR; P39215; -.
DR IntAct; P39215; 2.
DR STRING; 224308.BSU31260; -.
DR jPOST; P39215; -.
DR PaxDb; P39215; -.
DR PRIDE; P39215; -.
DR EnsemblBacteria; CAB15104; CAB15104; BSU_31260.
DR GeneID; 937155; -.
DR KEGG; bsu:BSU31260; -.
DR PATRIC; fig|224308.179.peg.3386; -.
DR eggNOG; COG0840; Bacteria.
DR InParanoid; P39215; -.
DR OMA; AHPTMKP; -.
DR PhylomeDB; P39215; -.
DR BioCyc; BSUB:BSU31260-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: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 InterPro; IPR003122; Tar_rcpt_lig-bd.
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 SMART; SM00319; TarH; 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..662
FT /note="Methyl-accepting chemotaxis protein McpB"
FT /id="PRO_0000110557"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..282
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 304..662
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 153..229
FT /note="Cache"
FT DOMAIN 304..356
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 375..611
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT MOD_RES 371
FT /note="Glutamate methyl ester (Gln)"
FT /evidence="ECO:0000269|PubMed:10825179,
FT ECO:0000269|PubMed:8188684"
FT MOD_RES 595
FT /note="Glutamate methyl ester (Gln)"
FT /evidence="ECO:0000305|PubMed:8188684"
FT MOD_RES 630
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000269|PubMed:10825179,
FT ECO:0000269|PubMed:8188684"
FT MOD_RES 637
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000269|PubMed:10825179,
FT ECO:0000269|PubMed:8188684"
FT MUTAGEN 371
FT /note="Q->D: Marked diminution of methanol upon both
FT addition and removal of asparagine. No release of methanol
FT upon asparagine addition but methanol release upon
FT asparagine removal is not affected; when associated with D-
FT 630. Release of methanol upon both asparagine addition and
FT removal; when associated with D-637. No methylation; when
FT associated with D-630 and D-637."
FT /evidence="ECO:0000269|PubMed:10825179"
FT MUTAGEN 595
FT /note="Q->D: Wild-type production of methanol."
FT /evidence="ECO:0000269|PubMed:10825179"
FT MUTAGEN 630
FT /note="E->D: Marked diminution of methanol upon both
FT addition and removal of asparagine; methanol release
FT delayed by about 1 minute compared to wild-type; adapts
FT normally to addition of asparagine but fails to adapt to
FT asparagine removal. No release of methanol upon asparagine
FT addition but methanol release upon asparagine removal is
FT not affected; when associated with D-371. Releases methanol
FT upon asparagine addition but not upon asparagine removal;
FT when associated with D-637. No methylation; when associated
FT with D-371 and D-637."
FT /evidence="ECO:0000269|PubMed:10825179"
FT MUTAGEN 637
FT /note="E->D: Marked diminution of methanol upon both
FT addition and removal of asparagine; fails to adapt to
FT addition of asparagine. Release of methanol upon both
FT asparagine addition and removal; when associated with D-
FT 371. Releases methanol upon asparagine addition but not
FT upon asparagine removal; when associated with D-630. No
FT methylation; when associated with D-371 and D-630."
FT /evidence="ECO:0000269|PubMed:10825179"
FT CONFLICT 360
FT /note="D -> N (in Ref. 1; AAA20554)"
FT /evidence="ECO:0000305"
FT CONFLICT 402
FT /note="E -> R (in Ref. 1; AAA20554)"
FT /evidence="ECO:0000305"
FT CONFLICT 450
FT /note="V -> G (in Ref. 1; AAA20554)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 662 AA; 71901 MW; 2E4ED0EFC31F2983 CRC64;
MKTFINWLKK PSISKKLIVS FIAILIIPIL ILEFSSYRSA SGKLDQEIMG NAKNSVDTFN
TTVTNDLGEK AKAVTFFSES LKRSAFKGKS NQEEIKAKFS QYVSINQGVA RIYGGADNGT
YVQAPKEKLP EGYDPRQRPW YQDAMKAGGE IVVTDPYVAA SDGSMVITIA QELKDGSGVV
AMDITIDKLL EQMKQIKVGK EGYAFIATKN KTYVAHKNHK AGEKLSGDWV AKMYANDSGE
LQYTLNNEDK KMTYTTNELT GWKIAGTMYM DEIKDASKSV LTTGMIVLIA SIVAGGILIL
FIVRSITKPL KRLVQSSKTI SRGDLTETIE IHSKDELGEL GESFNEMGQS LRSLISAIQD
SVNNVAASSE QLTASAGQTS KATEHITMAI EQFSNGNEEQ SEKVESSSHQ LNLMNEGLQQ
VSQTSSDITK ASIQSTEIAG TGEKFVQQTV GQMNSINQSV QQAEAVVKGL EGKSKDITSI
LRVINGIADQ TNLLALNAAI EAARAGESGR GFSVVAEEVR KLAVQSADSA KEIEKLIQEI
VAEIDTSLHM FKEVNQEVQS GLVVTDNTKE SFQSIFSMTN EIAGKLQTMN STVEQLSDRS
QHVSAAVSGI ADVSKESSAS IQDIAASAEE QLASMEEISS SATTLAQMAE ELRDLTKQFK
IE
