ID   Q899J9_CLOTE            Unreviewed;       617 AA.
AC   Q899J9;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 96.
DE   SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:AAO34825.1};
GN   OrderedLocusNames=CTC_00174 {ECO:0000313|EMBL:AAO34825.1};
OS   Clostridium tetani (strain Massachusetts / E88).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=212717 {ECO:0000313|EMBL:AAO34825.1, ECO:0000313|Proteomes:UP000001412};
RN   [1] {ECO:0000313|EMBL:AAO34825.1, 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).
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DR   EMBL; AE015927; AAO34825.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q899J9; -.
DR   STRING; 212717.CTC_00174; -.
DR   KEGG; ctc:CTC_00174; -.
DR   HOGENOM; CLU_000445_107_18_9; -.
DR   Proteomes; UP000001412; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
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   Gene3D; 3.90.1520.10; H-NOX domain; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR   InterPro; IPR038158; H-NOX_domain_sf.
DR   InterPro; IPR011644; Heme_NO-bd.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   InterPro; IPR024096; NO_sig/Golgi_transp_ligand-bd.
DR   PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR   PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR   Pfam; PF07700; HNOB; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   PRINTS; PR00260; CHEMTRNSDUCR.
DR   SMART; SM00283; MA; 1.
DR   SUPFAM; SSF111126; Ligand-binding domain in the NO signalling and Golgi transport; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001412};
KW   Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW   ProRule:PRU00284}.
FT   DOMAIN          331..588
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   COILED          170..197
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          371..398
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          472..506
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   617 AA;  70056 MW;  67914BCA6D87A12B CRC64;
     MIFDNILINL NTVSNGGNRM KGTIVATWMR TCRKLYNDDV VNKAMSSVGW DSNKIFKPTE
     NVEDSDLKKV IEYIAKSEKL ELGHLWRQIG KDNLVSFYND FPAFFQHENL YSFFNSLFDI
     HVVMTKKFPG AKPPLVTIEP ISSKEAIFYY ESKRGMFDYL LGLIEGSIKY FKEDIEIEEL
     ERTNESLKLK LKFQKNIYLK KEFKFNKLMS FGFVKNLSAK IAISSFIISM ISNLYISEAR
     LYRTGVSSLV QALIIFVICE LLFKPKNFIK RELEKIKDHN YSEKTKIVTK DFFEDIVEII
     NQNKDTVKKD FVSFKGVTDE MNTFVGNINK ISDAMNYTSQ GIAGVVEQVA ETSVSQAQNT
     EKTVFVLNGN IDSLRKIVEN ENNNKIELEC ALDKVNNSYK NVEGTSKNIL DTLDKFQEVK
     EKGQELQNRA EDITSIVSIV AQISEQTNLL ALNASIEAAR AGEQGKGFAV VAEEVRNLAE
     QTKEAVEETN SSLVNFAKEI KNLSDKIDGQ YEVLKNETKN LEIVRNISYE ATTSIQSVAS
     SMIYTINDLN KEAESINNIF GNIESLATIA EENSASSEEV SASVSSYINE IRKLTDNINE
     FKKITESFKA ELCQYKI
//