ID A0A401URG8_9CLOT Unreviewed; 572 AA.
AC A0A401URG8;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 13.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:GCD12139.1};
GN ORFNames=Ctaglu_37620 {ECO:0000313|EMBL:GCD12139.1};
OS Clostridium tagluense.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=360422 {ECO:0000313|EMBL:GCD12139.1, ECO:0000313|Proteomes:UP000287872};
RN [1] {ECO:0000313|EMBL:GCD12139.1, ECO:0000313|Proteomes:UP000287872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A121 {ECO:0000313|EMBL:GCD12139.1,
RC ECO:0000313|Proteomes:UP000287872};
RA Murakami T., Segawa T., Shcherbakova V.A., Mori H., Yoshimura Y.;
RT "Genome sequencing and assembly of Clostridium tagluense strain A121.";
RL Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:GCD12139.1}.
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DR EMBL; BHYK01000027; GCD12139.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A401URG8; -.
DR OrthoDB; 1887545at2; -.
DR Proteomes; UP000287872; 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; 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:UP000287872};
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..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 194..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 214..266
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 271..536
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 572 AA; 63130 MW; 4BB8874B737CEE22 CRC64;
MKFFINLKVK TKLISVFSVV CIFMILIGVQ GIISSSKINE GSKSIYSNGL IPIKDLEEIK
GNINEMRGNM LTIIFERDRT KLDDQIKNMN NLTNEDIKIQ KEYESIPSAS IEEDKTYNEF
KNELVKYREG KVKIIELAKS NSYGEAVKLF NSEMAKTRIT MFEKLGKCIE INQKSATQAN
SDNIAHFNKV RYTILIYTVI AFFIIIFMAY ILSKNIMVPL NRIKELANRL SSYDFSAPIN
ITGKDEFGQT AVALNIAQEN VNSLVKVIME NAQEISASSE ELSATVQELS SKVIIIDEAV
VSIAAGMQES SAASEEISAS VEEVDSSINV LSSKAMEGSN NSYQFKERAT EVKSNSQKAI
NVTQKLYNEK QKNMEKAIED GKVVDSIKVM ADTIGSIATQ TNLLALNAAI EAARAGEQGR
GFAVVADEVR KLAEQSAQAV IKIQETIVKV QGAFKSSIDT GSDILEFINT HVQEQFNAYA
ETGNQYYNDS DFVSKMSEEI AAMSEEITAT VGQVSHAVQN MAESSQSSSG EALTIKESMN
EASQAIEQVA LTAQSQAELA QKLNEIVQQF KI
//
