ID B1KZ03_CLOBM Unreviewed; 570 AA.
AC B1KZ03;
DT 29-APR-2008, integrated into UniProtKB/TrEMBL.
DT 29-APR-2008, sequence version 1.
DT 27-MAR-2024, entry version 79.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:ACA54375.1};
GN OrderedLocusNames=CLK_2217 {ECO:0000313|EMBL:ACA54375.1};
OS Clostridium botulinum (strain Loch Maree / Type A3).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=498214 {ECO:0000313|EMBL:ACA54375.1, ECO:0000313|Proteomes:UP000000722};
RN [1] {ECO:0000313|EMBL:ACA54375.1, 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 -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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DR EMBL; CP000962; ACA54375.1; -; Genomic_DNA.
DR RefSeq; WP_012342489.1; NC_010520.1.
DR AlphaFoldDB; B1KZ03; -.
DR KEGG; cbl:CLK_2217; -.
DR HOGENOM; CLU_000445_107_27_9; -.
DR Proteomes; UP000000722; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
DR GO; GO:0006935; P:chemotaxis; IEA:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd19411; MCP2201-like_sensor; 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 InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR024478; HlyB_4HB_MCP.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR047347; YvaQ-like_sensor.
DR PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR Pfam; PF12729; 4HB_MCP_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00304; HAMP; 2.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
DR PROSITE; PS50885; HAMP; 1.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW ProRule:PRU00284}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 190..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 212..264
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 269..520
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 325..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 325..344
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 570 AA; 62866 MW; 47BF0E0BBD56F475 CRC64;
MLKNIKRKVK TQLICAFLIV AVLIVIVGAV GGVALKNVAR YGEKMYSTNL QSVYMITDMN
QNLTEIKSDM LQLIYEKDES KKVELIKNIQ KNKDENSKYL AEYEKLPKTD EENKTFQVFK
GQLNQYRTLR EDVIKLVEAN NYAQAEKQYK EIPKVRDAMF ESISKITEIN LNSAESANND
INSIYTKSNV IIAILSIAGL LMAIFIGLFI ARNIAKPLNK IKDLAERLAN YDFSTSITVT
RGDEFGQTAV ALNTAQENVN GLVKIIMENS QDISASSEEL SATVEELSSK VETIDTAINN
IAASMQESSA ASEEISASVE EVDSSANELS QKAMEGSNNS NQFKERATEV KKNSQKAIEE
SRQIHLEKKK NMEKAVEEGR VVDSIKVMAD TIASIAEQTN LLALNAAIEA ARAGEQGKGF
AVVAEEVRSL AEQSKDAVVS IQETIIKVQN AFKSSIDTGS DILKFINTQV MEQFDAYGET
GGQYYDDSDF VSKMSEEIAA MSEQVTATLG QVSGAVQNMA ISAQKSNEEA DIIKDSMNET
TKAIEQVAET AQSQAELAQN LNEMVHKFKI
//
