ID Q893I7_CLOTE Unreviewed; 586 AA.
AC Q893I7;
DT 01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2003, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:AAO36355.1};
GN OrderedLocusNames=CTC_01835 {ECO:0000313|EMBL:AAO36355.1};
OS Clostridium tetani (strain Massachusetts / E88).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=212717 {ECO:0000313|EMBL:AAO36355.1, ECO:0000313|Proteomes:UP000001412};
RN [1] {ECO:0000313|EMBL:AAO36355.1, ECO:0000313|Proteomes:UP000001412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Massachusetts / E88 {ECO:0000313|Proteomes:UP000001412};
RX PubMed=12552129; DOI=10.1073/pnas.0335853100;
RA Brueggemann H., Baumer S., Fricke W.F., Wiezer A., Liesegang H., Decker I.,
RA Herzberg C., Martinez-Arias R., Merkl R., Henne A., Gottschalk G.;
RT "The genome sequence of Clostridium tetani, the causative agent of tetanus
RT disease.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:1316-1321(2003).
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; AE015927; AAO36355.1; -; Genomic_DNA.
DR RefSeq; WP_011100015.1; NC_004557.1.
DR AlphaFoldDB; Q893I7; -.
DR STRING; 212717.CTC_01835; -.
DR GeneID; 24253602; -.
DR KEGG; ctc:CTC_01835; -.
DR HOGENOM; CLU_000445_107_19_9; -.
DR OrthoDB; 9810264at2; -.
DR Proteomes; UP000001412; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd06225; HAMP; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR033480; sCache_2.
DR PANTHER; PTHR32089:SF112; HEME-BASED AEROTACTIC TRANSDUCER HEMAT; 1.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR Pfam; PF17200; sCache_2; 1.
DR SMART; SM01049; Cache_2; 1.
DR SMART; SM00304; HAMP; 1.
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 Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001412};
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..36
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 208..227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 231..280
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 299..563
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT COILED 559..586
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 586 AA; 66016 MW; D4589C764E67D2EA CRC64;
MTKHNKGLDK RLFKSYLGIF ILFFISILAV VLVSFIGAKG TLEKLGEEAL KNKINMGIEM
MDMLETQVKN DNLAKEEAQE IFKNKMLNEK GNDGKTRGLN KKLELGIEAY MYAIDSNGIE
KMHPFKEGEN ISNLVDNKGE NVTKLIIKEG KNPENGGLIT FWWKNPDEKQ TRKKVNAVAY
YEPWDWYLNV GCYYEDFYGN IVDTFRNILI VAILILIMSI LLIRLMISKK VEPLNKVIEL
IKKIGEGDLS SKVNINSKDE IGYMASTLNN ALDEIKSMVV SLKETSEKIN EKIKYVNEVT
NTTSETSQNI TKAVEEIACS ATDTTKDMEI SFDAEKDLTD NIALIKDTSL LLQNEAMNAS
KLNSNILNVL KNLEDKSIEN LNLSEETSKN MNILTDKSNT IIKIVNTIEN ISKQINLLAL
NASIESSKAG VAGKGFAVVA QGIKELSEQT EQSTNHINQH VNELMKSILY SEESVNKTKK
SSEIQRDTIK KTQNIFMEVI KFIEEVPKYI ENNVIRIEEV YNKNDTVNSS MDAVLGLMQG
ISSATEEITS SMTEVNKSIL EINDMIDELG INANELNEKS QKFKIK
//
