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Database: UniProt
Entry: Q898Y9_CLOTE
LinkDB: Q898Y9_CLOTE
Original site: Q898Y9_CLOTE 
ID   Q898Y9_CLOTE            Unreviewed;       639 AA.
AC   Q898Y9;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:AAO34940.1};
GN   OrderedLocusNames=CTC_00297 {ECO:0000313|EMBL:AAO34940.1};
OS   Clostridium tetani (strain Massachusetts / E88).
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=212717 {ECO:0000313|EMBL:AAO34940.1, ECO:0000313|Proteomes:UP000001412};
RN   [1] {ECO:0000313|EMBL:AAO34940.1, 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   -!- SIMILARITY: Belongs to the phosphate/phosphite/phosphonate binding
CC       protein family. {ECO:0000256|ARBA:ARBA00007162}.
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DR   EMBL; AE015927; AAO34940.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q898Y9; -.
DR   STRING; 212717.CTC_00297; -.
DR   KEGG; ctc:CTC_00297; -.
DR   HOGENOM; CLU_030791_0_0_9; -.
DR   OrthoDB; 9781943at2; -.
DR   Proteomes; UP000001412; Chromosome.
DR   GO; GO:0043190; C:ATP-binding cassette (ABC) transporter complex; IEA:InterPro.
DR   GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; IEA:InterPro.
DR   CDD; cd01071; PBP2_PhnD_like; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   InterPro; IPR005770; PhnD.
DR   NCBIfam; TIGR01098; 3A0109s03R; 1.
DR   PANTHER; PTHR35841; PHOSPHONATES-BINDING PERIPLASMIC PROTEIN; 1.
DR   PANTHER; PTHR35841:SF1; PHOSPHONATES-BINDING PERIPLASMIC PROTEIN; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   Pfam; PF12974; Phosphonate-bd; 1.
DR   SMART; SM00283; MA; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR   SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
PE   3: Inferred from homology;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001412};
KW   Signal {ECO:0000256|ARBA:ARBA00022729};
KW   Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        18..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        44..62
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          105..341
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   639 AA;  72893 MW;  FB0B831ADE9BA693 CRC64;
     MIYKQYLKWG EIPLDKKILS FIISGSLIFN LVIYFLVNNK GLIILLEIMF ILFIIFIIFT
     NYENKQNVIS EKYNDFKEAK DKENYEKIFE SWQTLSFDIH QLLWMYRDSM KTLTKVINIS
     RDIQFNTEQS TWNVENINSS VEELITISEV LNNNVIVMED SYNESFDVLK NSKDTISGIT
     KYLLELDKDV KEVSIINNKF RHSSNRINDF ILDIEYISNQ TNLLSLNASI EAARAGEAGK
     GFSIVAKEIK NLSKGTNEVV VKIKDIVKEI ILDVDKSTVS MDKCLNKISG TQNIVNESSQ
     LIEKLESVSE GIIRSIERLK EASLEQMTAS NNIGEAISSI AISEENNYIT VAKSIEIISE
     QERKNNNILS ICNKLEDTAH DIQYVTTQLK KDNEIIFGIN PFTSPQNIKE IYVPILERVC
     KNIGYKAKII IVKNYEDLGD RIKEKVIDIG WFSPFAYVKA HANIGVVPLV TPKVNGKVTY
     KGYIIAKKNS EINKIEDLRG RNFSYVDKES ASGYLYARYL IKKEKLDPDN LFKEVQFKGG
     HHSVIESVLS GEADGGATYS EAIESAKNEG MPIEDIVIIK EFSNIPKDVI ASRSDMDKDL
     IQKVKKAFLE FNCLEEIKSP VEGFIETEDI KYNVIREIV
//
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