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Methyl-accepting chemotaxis protein McpA (H1)

 MCPA_BACSU              Reviewed;         661 AA.
P39214;
01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
07-JUL-2009, sequence version 2.
20-JUN-2018, entry version 125.
RecName: Full=Methyl-accepting chemotaxis protein McpA;
AltName: Full=H1;
Name=mcpA; OrderedLocusNames=BSU31240;
Bacillus subtilis (strain 168).
Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
NCBI_TaxID=224308;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], METHYLATION AT GLU-370; GLN-594;
GLU-629 AND GLU-636, DEAMIDATION AT GLN-594, 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 95.
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]
PROTEIN SEQUENCE OF 589-595, DEAMIDATION AT GLN-593 AND GLN-594 BY
CHED, AND MUTAGENESIS OF GLN-593 AND GLN-594.
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. McpA is required for taxis
towards glucose and alpha-methylglucoside.
{ECO:0000269|PubMed:8188684}.
-!- SUBCELLULAR LOCATION: Cell membrane; Multi-pass membrane protein.
-!- PTM: Deamidated by CheD on Gln-593 and Gln-594, producing
glutamate residues. The glutamate residues are then methylated.
Other additional sites are deamidated and methylated as well.
{ECO:0000269|PubMed:12011078, ECO:0000269|PubMed:8188684}.
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EMBL; L29189; AAA20556.1; -; Genomic_DNA.
EMBL; AL009126; CAB15102.2; -; Genomic_DNA.
PIR; B54078; B54078.
RefSeq; NP_391002.2; NC_000964.3.
RefSeq; WP_003244077.1; NZ_JNCM01000033.1.
ProteinModelPortal; P39214; -.
SMR; P39214; -.
IntAct; P39214; 23.
STRING; 224308.Bsubs1_010100016981; -.
PaxDb; P39214; -.
PRIDE; P39214; -.
EnsemblBacteria; CAB15102; CAB15102; BSU31240.
GeneID; 937154; -.
KEGG; bsu:BSU31240; -.
PATRIC; fig|224308.179.peg.3384; -.
eggNOG; ENOG4105C8Q; Bacteria.
eggNOG; COG0840; LUCA.
HOGENOM; HOG000083278; -.
InParanoid; P39214; -.
KO; K03406; -.
OMA; SYIPSMD; -.
PhylomeDB; P39214; -.
BioCyc; BSUB:BSU31240-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;
Direct protein sequencing; Membrane; Methylation; Reference proteome;
Transducer; Transmembrane; Transmembrane helix.
CHAIN 1 661 Methyl-accepting chemotaxis protein McpA.
/FTId=PRO_0000110556.
TOPO_DOM 1 16 Cytoplasmic. {ECO:0000255}.
TRANSMEM 17 37 Helical. {ECO:0000255}.
TOPO_DOM 38 281 Extracellular. {ECO:0000255}.
TRANSMEM 282 302 Helical. {ECO:0000255}.
TOPO_DOM 303 661 Cytoplasmic. {ECO:0000255}.
DOMAIN 152 228 Cache.
DOMAIN 303 355 HAMP. {ECO:0000255|PROSITE-
ProRule:PRU00102}.
DOMAIN 374 610 Methyl-accepting transducer.
{ECO:0000255|PROSITE-ProRule:PRU00284}.
MOD_RES 370 370 Glutamate methyl ester (Glu).
{ECO:0000305|PubMed:8188684}.
MOD_RES 593 593 Deamidated glutamine.
{ECO:0000269|PubMed:12011078}.
MOD_RES 594 594 Deamidated glutamine.
{ECO:0000269|PubMed:12011078}.
MOD_RES 594 594 Glutamate methyl ester (Gln).
{ECO:0000269|PubMed:12011078,
ECO:0000269|PubMed:8188684}.
MOD_RES 629 629 Glutamate methyl ester (Glu).
{ECO:0000305|PubMed:8188684}.
MOD_RES 636 636 Glutamate methyl ester (Glu).
{ECO:0000305|PubMed:8188684}.
MUTAGEN 593 593 Q->A: No CheD modification at Q-593 and
Q-594 but modification possible at the
unidentified second site; when associated
with A-594.
{ECO:0000269|PubMed:12011078}.
MUTAGEN 594 594 Q->A: No CheD modification at Q-593 and
Q-594 but modification possible at the
unidentified second site; when associated
with A-593.
{ECO:0000269|PubMed:12011078}.
CONFLICT 95 95 A -> R (in Ref. 1; AAA20556).
{ECO:0000305}.
SEQUENCE 661 AA; 72314 MW; E46A09AB33604141 CRC64;
MKKILQLIKQ RSITRKLLVS FLSILIIPVV ILAIFAYQSA SSSLDRQMMG SALENVQQLN
EIINTSIGEK ENSADYFSEW LTKEKYNAKS NASIAEKFSQ YISINKDVES IYTSDTKGHF
TRYPDLPMPS GYNPVERDWY KKAVANKGKV VITDPYKTAS TNTMVVTIAQ QTKDGSGVIA
INMTIENLLK TTKKVNIGTQ GYAFIMTKDK KVVAHPNEQS GTELKGDWLD KMLSADKGDF
QYTMDGDKKK MAFDTNKLTG WKIGGTMYLD EIHEAAQPVL HLALIVLAAA IIIGIIVMTL
IIRSITTPLK QLVGSSKRIS EGDLTETIDI RSKDELGELG KSFNNMASSL RSLIHAIQDS
VDNVAASSEE LTASAAQTSK ATEHITLAIE QFSNGNEKQN ENIETAAEHI YQMNDGLTNM
AQASEVITDS SVQSTEIASE GGKLVHQTVG QMNVIDKSVK EAEQVVRGLE TKSKDITNIL
RVINGIADQT NLLALNAAIE AARAGEYGRG FSVVAEEVRK LAVQSADSAK EIEGLIIEIV
KEINTSLGMF QSVNQEVQTG LDITDKTEMS FKRISEMTNQ IAGELQNMSA TVQQLSASSE
EVSGASEHIA SISKESSAHI QDIAASAEEQ LASMEEISSS AETLSSMAEE LRDMTKRFKI
E


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