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Database: UniProt
Entry: Q739Q2_BACC1
LinkDB: Q739Q2_BACC1
Original site: Q739Q2_BACC1 
ID   Q739Q2_BACC1            Unreviewed;       660 AA.
AC   Q739Q2;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   27-MAR-2024, entry version 104.
DE   SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:AAS41009.1};
GN   OrderedLocusNames=BCE_2088 {ECO:0000313|EMBL:AAS41009.1};
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=222523 {ECO:0000313|EMBL:AAS41009.1, ECO:0000313|Proteomes:UP000002527};
RN   [1] {ECO:0000313|EMBL:AAS41009.1, ECO:0000313|Proteomes:UP000002527}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248 {ECO:0000313|Proteomes:UP000002527};
RX   PubMed=14960714; DOI=10.1093/nar/gkh258;
RA   Rasko D.A., Ravel J., Okstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA   Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.,
RA   Nelson W.C., Kolsto A.-B., Fraser C.M., Read T.D.;
RT   "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT   adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL   Nucleic Acids Res. 32:977-988(2004).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000256|ARBA:ARBA00029447}.
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DR   EMBL; AE017194; AAS41009.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q739Q2; -.
DR   KEGG; bca:BCE_2088; -.
DR   HOGENOM; CLU_000445_107_19_9; -.
DR   Proteomes; UP000002527; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd11386; MCP_signal; 1.
DR   CDD; cd12913; PDC1_MCP_like; 1.
DR   CDD; cd12912; PDC2_MCP_like; 1.
DR   Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
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   PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   PANTHER; PTHR32089:SF114; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   Pfam; PF02743; dCache_1; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   SMART; SM00304; HAMP; 2.
DR   SMART; SM00283; MA; 1.
DR   SMART; SM00319; TarH; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR   SUPFAM; SSF103190; Sensory domain-like; 1.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR   PROSITE; PS50885; HAMP; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Methylation {ECO:0000256|ARBA:ARBA00022481};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW   ProRule:PRU00284};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        279..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          303..355
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          374..624
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   REGION          425..445
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   660 AA;  71751 MW;  1DFA42C011E17E1D CRC64;
     MGRLLNWFRD MKVAKKLLIS FFVILIAAVS IIGGMSYQTA KKNFESQITS SAHDNIKILD
     NLINQMIEAK FNDVNNFARV IQGNMYQGDN QEELRKILSQ YINLNKDVEQ VYVAGNDKKF
     VQEPNIQMAA DYDPTERSWY KDAVAKQGGI VITEPYKAKG NGHIVVTIAK QAEDKNGVVA
     VDLSLDNLLK TTKLINIGKK GYAFILDGKQ KIIAHPQEKS GEKAADSWAK KIYEDNHGAF
     SYTYDGSEKQ MVFATNVKTG WKIGGTMYSN EVIEAAQPVF YNMLIVMFIS LVIGGALIYF
     VTLSITKPLK RLVVTSKEIS EGDLTQTIDI HSNDEIGQLA KGFNEMTDAL RTLIGRINTS
     AGHVAAASEE LTASVRQASE ATEQITMAMD EISSGATTQT TSVENGAMLL FDVTEGIQHV
     ANSSSSISTA SAHTREKAEN GGKLVGKTVN QMQSIAESVS QSDEVIQLLN NKSKQIGDIL
     EVIQNIADQT NLLALNAAIE AARAGEHGRG FAIVADEVRK LAEKSSVSSS EISKLICEIQ
     DDMSKTVKSM GHVNEEVQSG LVIANETKQN FTEILQSTNE IANQIKTMVE TANGMSKGAN
     EVSISVGQIA MTAQNNATST QNVAASAEEQ LASIEEISSA AGTLSQMAEE LQGLIERFKV
//
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