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Database: UniProt
Entry: A0A0U1KTJ8_9FIRM
LinkDB: A0A0U1KTJ8_9FIRM
Original site: A0A0U1KTJ8_9FIRM 
ID   A0A0U1KTJ8_9FIRM        Unreviewed;       562 AA.
AC   A0A0U1KTJ8;
DT   17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT   17-FEB-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:CQR70717.1};
GN   ORFNames=SpAn4DRAFT_1695 {ECO:0000313|EMBL:CQR70717.1};
OS   Sporomusa ovata.
OC   Bacteria; Bacillota; Negativicutes; Selenomonadales; Sporomusaceae;
OC   Sporomusa.
OX   NCBI_TaxID=2378 {ECO:0000313|EMBL:CQR70717.1, ECO:0000313|Proteomes:UP000049855};
RN   [1] {ECO:0000313|Proteomes:UP000049855}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Nijsse Bart;
RL   Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC       family. {ECO:0000256|ARBA:ARBA00029447}.
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DR   EMBL; CTRP01000003; CQR70717.1; -; Genomic_DNA.
DR   RefSeq; WP_021169440.1; NZ_CTRP01000003.1.
DR   AlphaFoldDB; A0A0U1KTJ8; -.
DR   Proteomes; UP000049855; Unassembled WGS sequence.
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   Gene3D; 6.10.340.10; -; 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   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; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000049855};
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..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        179..202
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          203..257
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          276..533
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
SQ   SEQUENCE   562 AA;  60787 MW;  011DDFF21D02642B CRC64;
     MRITIGTKLI LIAVPILLVS ILVQLFAYFI FTDTSQNMRE SVKNSQIQQR IAKTRLTLEQ
     VVMPANDYLI TGDVTERKNF EELSEQLETN LRELENLSLT PAELTIVQEF RRDWQEIKPD
     AVQILNLANP VGNFAGGDIM ERMDAETERA SGEIDKLDQI YENLAASSYR QAEDNRGKVV
     VGFAINTLVI VLLVVGSGYY AITRIVRPLR EVAGLIEDLG DSGGDLTRRI HSKTGDEMED
     IADATNKLVA STQTMIGKIG QVTTNLYAVT QNVAAQCQVV LLSNEQVTSS IADVAKGSSE
     QAEGSQSLTA QVEVLANAVN ALNSLSEAIS AQELITKNKI EVSNSLLKQV ESAMDEISSQ
     SGSVQLHIAK LENMSGEITQ IVEVITAIAQ QTALLALNAA IEAARAGEQG RGFAVVADEV
     RKLAEQSEQS ASEIAQVVNN IQQEIGTAVT FTVENATAAK KGIEMSNAIC KAITDIQDAV
     NKIGEQLTTV REKIVILDSV ADVTVAATQN ISAVCQQNAA MAQEVSALAE QQSNSLKDVM
     AENQTITAET GVLNNMIHKF TY
//
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