ID B1L1P0_CLOBM Unreviewed; 690 AA.
AC B1L1P0;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 83.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:ACA56353.1};
GN OrderedLocusNames=CLK_1004 {ECO:0000313|EMBL:ACA56353.1};
OS Clostridium botulinum (strain Loch Maree / Type A3).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=498214 {ECO:0000313|EMBL:ACA56353.1, ECO:0000313|Proteomes:UP000000722};
RN [1] {ECO:0000313|EMBL:ACA56353.1, ECO:0000313|Proteomes:UP000000722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Loch Maree / Type A3 {ECO:0000313|Proteomes:UP000000722};
RX PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-A4
RT and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT plasmids.";
RL PLoS ONE 2:E1271-E1271(2007).
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; CP000962; ACA56353.1; -; Genomic_DNA.
DR RefSeq; WP_012344234.1; NC_010520.1.
DR AlphaFoldDB; B1L1P0; -.
DR KEGG; cbl:CLK_1004; -.
DR HOGENOM; CLU_000445_107_19_9; -.
DR Proteomes; UP000000722; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; 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 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 PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR PANTHER; PTHR32089; 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; 1.
DR SMART; SM00283; MA; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 306..328
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 330..385
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 404..654
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 643..663
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 566..597
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 690 AA; 76844 MW; 843596AF64D0E24E CRC64;
MKKNSSIKNK LIISFVSLIL VSLVLLGSIV YTKVYNQTKE DYAQSIEKQI TQVDTSFNNY
IVAFEENIDM FSKGLNNLDK QVTSYVDKKY QSNEIPMTPL KNGSFEASLY KEFENFTKTH
DGIETLSISS ESNGGYMQYP AISRKKGYDP RTRDWYNEAK KNKDKVSFTD VYKTSSGSMV
MSVINPVKDL NSNFKGVMTF DINLKKLSEM SKNTKVGENG YFIVTDEKGT IIASGKDESL
VSKSIKELKV ENLNDLSKYK NSSFSTKMGN GKEYFINVKK SSNEKLGWYY ISFVEKAELT
RSANSIGLIT LIFTIMFSIV AVLVCIFISN KISQPIKYAA EHIKEMGKGN FTIPIEEKYF
KLEDEIGDII KSLDRMQNSI KSMLGKVKES SEVVSEEGEK LLSASEEMTG SSSEVSNAIH
DVAVGISNQA GELVKATTTI SSFGERLDMV VGELSSISEN SVSINLVAND SNKKMVNMIV
SVKNIEEFFK VFLNVISKLD NNVGQISEMT NLINSISEQT NLLALNAAIE AARAGESGKG
FAVVADEIRK LAERSKESSE SINKLVENID KDKKDIINNT EKMKEELDSQ SKTIEETIDV
FKNIIEAIED IVPKIQNVNS SAYSINEEKD EVLSKMEGSS AISEEISASS EEISASSEEM
HNCSKDVSIS AEKLSEMTRA MNEEVNKFKI
//
