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Methyl-accepting chemotaxis protein McpB (H3)

 MCPB_BACSU              Reviewed;         662 AA.
P39215;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
07-JUL-2009, sequence version 2.
20-JUN-2018, entry version 126.
RecName: Full=Methyl-accepting chemotaxis protein McpB;
AltName: Full=H3;
Name=mcpB; OrderedLocusNames=BSU31260;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], METHYLATION AT GLN-371; GLN-595;
GLU-630 AND GLU-637, DEAMIDATION AT GLN-371 AND GLN-595, AND FUNCTION.
STRAIN=168 / OI1085;
PubMed=8188684;
Hanlon D.W., Ordal G.W.;
"Cloning and characterization of genes encoding methyl-accepting
chemotaxis proteins in Bacillus subtilis.";
J. Biol. Chem. 269:14038-14046(1994).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=168;
PubMed=9384377; DOI=10.1038/36786;
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G.,
Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
Yoshikawa H., Danchin A.;
"The complete genome sequence of the Gram-positive bacterium Bacillus
subtilis.";
Nature 390:249-256(1997).
[3]
SEQUENCE REVISION TO 360; 402 AND 450.
PubMed=19383706; DOI=10.1099/mic.0.027839-0;
Barbe V., Cruveiller S., Kunst F., Lenoble P., Meurice G.,
Sekowska A., Vallenet D., Wang T., Moszer I., Medigue C., Danchin A.;
"From a consortium sequence to a unified sequence: the Bacillus
subtilis 168 reference genome a decade later.";
Microbiology 155:1758-1775(2009).
[4]
METHYLATION AT GLN-371; GLN-595; GLU-630 AND GLU-637, DEAMIDATION AT
GLN-371 AND 595, AND MUTAGENESIS OF GLN-371; GLN-595; GLU-630 AND
GLU-637.
PubMed=10825179; DOI=10.1074/jbc.M004001200;
Zimmer M.A., Tiu J., Collins M.A., Ordal G.W.;
"Selective methylation changes on the Bacillus subtilis chemotaxis
receptor McpB promote adaptation.";
J. Biol. Chem. 275:24264-24272(2000).
[5]
DEAMIDATION BY CHED.
PubMed=12011078; DOI=10.1074/jbc.M201334200;
Kristich C.J., Ordal G.W.;
"Bacillus subtilis CheD is a chemoreceptor modification enzyme
required for chemotaxis.";
J. Biol. Chem. 277:25356-25362(2002).
-!- FUNCTION: Chemotactic-signal transducers respond to changes in the
concentration of attractants and repellents in the environment,
transduce a signal from the outside to the inside of the cell, and
facilitate sensory adaptation through the variation of the level
of methylation. All amino acids serve as attractants in
B.subtilis, they appear to cause an increase in the turnover
methyl groups, leading to methylation of an unidentified acceptor,
while repellents have been shown to cause a decrease in methyl
group turnover. The methyl groups are added by a methyltransferase
and removed by a methylesterase. McpB is required for taxis
towards asparagine, aspartate, glutamine, and histidine.
{ECO:0000269|PubMed:8188684}.
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
-!- PTM: Some glutamine residues are deamidated to glutamate by CheD
and subsequently methylated. {ECO:0000269|PubMed:10825179,
ECO:0000269|PubMed:12011078, ECO:0000269|PubMed:8188684}.
-!- PTM: The demethylation is selective. Gln-371 is demethylated only
upon asparagine addition whereas Glu-637 is demethylated only upon
asparagine removal. Glu-630 appears indiscriminate and is
demethylated upon both addition and removal of asparagine.
-!- MISCELLANEOUS: Only chemotaxis towards asparagine is completely
deficient in the absence of McpB.
-----------------------------------------------------------------------
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EMBL; L29189; AAA20554.1; -; Genomic_DNA.
EMBL; AL009126; CAB15104.2; -; Genomic_DNA.
PIR; A54078; A54078.
RefSeq; NP_391004.2; NC_000964.3.
RefSeq; WP_003243461.1; NZ_JNCM01000033.1.
ProteinModelPortal; P39215; -.
SMR; P39215; -.
IntAct; P39215; 2.
STRING; 224308.Bsubs1_010100016991; -.
PaxDb; P39215; -.
PRIDE; P39215; -.
EnsemblBacteria; CAB15104; CAB15104; BSU31260.
GeneID; 937155; -.
KEGG; bsu:BSU31260; -.
PATRIC; fig|224308.179.peg.3386; -.
eggNOG; ENOG4105C8Q; Bacteria.
eggNOG; COG0840; LUCA.
HOGENOM; HOG000083278; -.
InParanoid; P39215; -.
KO; K03406; -.
OMA; AHPTMKP; -.
PhylomeDB; P39215; -.
BioCyc; BSUB:BSU31260-MONOMER; -.
Proteomes; UP000001570; Chromosome.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
CDD; cd06225; HAMP; 1.
InterPro; IPR033479; dCache_1.
InterPro; IPR003660; HAMP_dom.
InterPro; IPR004089; MCPsignal_dom.
InterPro; IPR029151; Sensor-like_sf.
InterPro; IPR003122; Tar_rcpt_lig-bd.
Pfam; PF02743; dCache_1; 1.
Pfam; PF00672; HAMP; 1.
Pfam; PF00015; MCPsignal; 1.
SMART; SM00304; HAMP; 1.
SMART; SM00283; MA; 1.
SMART; SM00319; TarH; 1.
SUPFAM; SSF103190; SSF103190; 1.
PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
PROSITE; PS50885; HAMP; 1.
1: Evidence at protein level;
Cell membrane; Chemotaxis; Complete proteome; Membrane; Methylation;
Reference proteome; Transducer; Transmembrane; Transmembrane helix.
CHAIN 1 662 Methyl-accepting chemotaxis protein McpB.
/FTId=PRO_0000110557.
TOPO_DOM 1 16 Cytoplasmic. {ECO:0000255}.
TRANSMEM 17 37 Helical. {ECO:0000255}.
TOPO_DOM 38 282 Extracellular. {ECO:0000255}.
TRANSMEM 283 303 Helical. {ECO:0000255}.
TOPO_DOM 304 662 Cytoplasmic. {ECO:0000255}.
DOMAIN 153 229 Cache.
DOMAIN 304 356 HAMP. {ECO:0000255|PROSITE-
ProRule:PRU00102}.
DOMAIN 375 611 Methyl-accepting transducer.
{ECO:0000255|PROSITE-ProRule:PRU00284}.
MOD_RES 371 371 Glutamate methyl ester (Gln).
{ECO:0000269|PubMed:10825179,
ECO:0000269|PubMed:8188684}.
MOD_RES 595 595 Glutamate methyl ester (Gln).
{ECO:0000305|PubMed:8188684}.
MOD_RES 630 630 Glutamate methyl ester (Glu).
{ECO:0000269|PubMed:10825179,
ECO:0000269|PubMed:8188684}.
MOD_RES 637 637 Glutamate methyl ester (Glu).
{ECO:0000269|PubMed:10825179,
ECO:0000269|PubMed:8188684}.
MUTAGEN 371 371 Q->D: Marked diminution of methanol upon
both addition and removal of asparagine.
No release of methanol upon asparagine
addition but methanol release upon
asparagine removal is not affected; when
associated with D-630. Release of
methanol upon both asparagine addition
and removal; when associated with D-637.
No methylation; when associated with D-
630 and D-637.
{ECO:0000269|PubMed:10825179}.
MUTAGEN 595 595 Q->D: Wild-type production of methanol.
{ECO:0000269|PubMed:10825179}.
MUTAGEN 630 630 E->D: Marked diminution of methanol upon
both addition and removal of asparagine;
methanol release delayed by about 1
minute compared to wild-type; adapts
normally to addition of asparagine but
fails to adapt to asparagine removal. No
release of methanol upon asparagine
addition but methanol release upon
asparagine removal is not affected; when
associated with D-371. Releases methanol
upon asparagine addition but not upon
asparagine removal; when associated with
D-637. No methylation; when associated
with D-371 and D-637.
{ECO:0000269|PubMed:10825179}.
MUTAGEN 637 637 E->D: Marked diminution of methanol upon
both addition and removal of asparagine;
fails to adapt to addition of asparagine.
Release of methanol upon both asparagine
addition and removal; when associated
with D-371. Releases methanol upon
asparagine addition but not upon
asparagine removal; when associated with
D-630. No methylation; when associated
with D-371 and D-630.
{ECO:0000269|PubMed:10825179}.
CONFLICT 360 360 D -> N (in Ref. 1; AAA20554).
{ECO:0000305}.
CONFLICT 402 402 E -> R (in Ref. 1; AAA20554).
{ECO:0000305}.
CONFLICT 450 450 V -> G (in Ref. 1; AAA20554).
{ECO:0000305}.
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


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