MCPA_BACSU
ID MCPA_BACSU Reviewed; 661 AA.
AC P39214;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 2.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Methyl-accepting chemotaxis protein McpA;
DE AltName: Full=H1;
GN Name=mcpA; OrderedLocusNames=BSU31240;
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 GLU-370; GLN-594; GLU-629
RP AND GLU-636, DEAMIDATION AT GLN-594, 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 95.
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 PROTEIN SEQUENCE OF 589-595, DEAMIDATION AT GLN-593 AND GLN-594 BY CHED,
RP AND MUTAGENESIS OF GLN-593 AND GLN-594.
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 [5]
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. McpA
CC is required for taxis towards glucose and alpha-methylglucoside.
CC {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: Deamidated by CheD on Gln-593 and Gln-594, producing glutamate
CC residues. The glutamate residues are then methylated. Other additional
CC sites are deamidated and methylated as well.
CC {ECO:0000269|PubMed:12011078, ECO:0000269|PubMed:8188684}.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000305}.
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DR EMBL; L29189; AAA20556.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15102.2; -; Genomic_DNA.
DR PIR; B54078; B54078.
DR RefSeq; NP_391002.2; NC_000964.3.
DR RefSeq; WP_003244077.1; NZ_JNCM01000033.1.
DR AlphaFoldDB; P39214; -.
DR SMR; P39214; -.
DR IntAct; P39214; 23.
DR STRING; 224308.BSU31240; -.
DR jPOST; P39214; -.
DR PaxDb; P39214; -.
DR PRIDE; P39214; -.
DR EnsemblBacteria; CAB15102; CAB15102; BSU_31240.
DR GeneID; 937154; -.
DR KEGG; bsu:BSU31240; -.
DR PATRIC; fig|224308.179.peg.3384; -.
DR eggNOG; COG0840; Bacteria.
DR InParanoid; P39214; -.
DR OMA; QTAKQMQ; -.
DR PhylomeDB; P39214; -.
DR BioCyc; BSUB:BSU31240-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; Direct protein sequencing; Membrane;
KW Methylation; Reference proteome; Transducer; Transmembrane;
KW Transmembrane helix.
FT CHAIN 1..661
FT /note="Methyl-accepting chemotaxis protein McpA"
FT /id="PRO_0000110556"
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..281
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 282..302
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 303..661
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 152..228
FT /note="Cache"
FT DOMAIN 303..355
FT /note="HAMP"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00102"
FT DOMAIN 374..610
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00284"
FT MOD_RES 370
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000305|PubMed:8188684"
FT MOD_RES 593
FT /note="Deamidated glutamine"
FT /evidence="ECO:0000269|PubMed:12011078"
FT MOD_RES 594
FT /note="Deamidated glutamine"
FT /evidence="ECO:0000269|PubMed:12011078"
FT MOD_RES 594
FT /note="Glutamate methyl ester (Gln)"
FT /evidence="ECO:0000269|PubMed:12011078,
FT ECO:0000269|PubMed:8188684"
FT MOD_RES 629
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000305|PubMed:8188684"
FT MOD_RES 636
FT /note="Glutamate methyl ester (Glu)"
FT /evidence="ECO:0000305|PubMed:8188684"
FT MUTAGEN 593
FT /note="Q->A: No CheD modification at Q-593 and Q-594 but
FT modification possible at the unidentified second site; when
FT associated with A-594."
FT /evidence="ECO:0000269|PubMed:12011078"
FT MUTAGEN 594
FT /note="Q->A: No CheD modification at Q-593 and Q-594 but
FT modification possible at the unidentified second site; when
FT associated with A-593."
FT /evidence="ECO:0000269|PubMed:12011078"
FT CONFLICT 95
FT /note="A -> R (in Ref. 1; AAA20556)"
FT /evidence="ECO:0000305"
SQ 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
