ID A0A0D8I7G9_9CLOT Unreviewed; 729 AA.
AC A0A0D8I7G9;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:AKL97152.1};
GN ORFNames=CACET_c37240 {ECO:0000313|EMBL:AKL97152.1}, TZ02_13475
GN {ECO:0000313|EMBL:KJF26193.1};
OS Clostridium aceticum.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=84022 {ECO:0000313|EMBL:AKL97152.1, ECO:0000313|Proteomes:UP000035704};
RN [1] {ECO:0000313|EMBL:AKL97152.1, ECO:0000313|Proteomes:UP000035704}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1496 {ECO:0000313|EMBL:AKL97152.1,
RC ECO:0000313|Proteomes:UP000035704};
RA Poehlein A., Schiel-Bengelsdorf B., Gottschalk G., Duerre P., Daniel R.;
RT "Genome sequence of Clostridium aceticum DSM 1496.";
RL Submitted (OCT-2014) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KJF26193.1, ECO:0000313|Proteomes:UP000032372}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 1496 {ECO:0000313|EMBL:KJF26193.1,
RC ECO:0000313|Proteomes:UP000032372};
RA Song Y., Hwang S., Cho B.-K.;
RT "Draft genome sequence of Clostridium aceticum DSM 1496, a potential
RT butanol broducer through syngas fermentation.";
RL Submitted (FEB-2015) to the EMBL/GenBank/DDBJ databases.
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; CP009687; AKL97152.1; -; Genomic_DNA.
DR EMBL; JYHU01000016; KJF26193.1; -; Genomic_DNA.
DR RefSeq; WP_044825498.1; NZ_JYHU01000016.1.
DR AlphaFoldDB; A0A0D8I7G9; -.
DR STRING; 84022.CACET_c37240; -.
DR KEGG; cace:CACET_c37240; -.
DR PATRIC; fig|84022.5.peg.973; -.
DR OrthoDB; 243053at2; -.
DR Proteomes; UP000032372; Unassembled WGS sequence.
DR Proteomes; UP000035704; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0006935; P:chemotaxis; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd18773; PDC1_HK_sensor; 1.
DR CDD; cd12912; PDC2_MCP_like; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR033479; dCache_1.
DR InterPro; IPR003660; HAMP_dom.
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; PF02743; dCache_1; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 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 Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000035704};
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 301..319
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 321..373
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 392..628
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 680..700
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 729 AA; 81883 MW; 4710A3E74AD51BD6 CRC64;
MKFKIATKLM AVFLILCTLP TFVLGTYAYR ASFKALQEGE VQKYNILLQG IVGNTRTTLQ
DTEFLLKNLS ANASFTHVLE SYNQGREVED EIALKESNQI LRKIYVDSMG YYESIFIVGL
DGNIVVDSLG RTGYSLGIED LQFAKDAMTK KGFIMSDVYL SSLSQTGVKI PTLSMAYPIM
HQTGQVLGAI AITFDFANFD RVVRNTEIGE AGYGFIINTK GEMLSHPDAK MLMEEGEDAI
SLSILEHIAQ EQTYGFQQIS IEGNRWSYFY HWVPSTDWVI AFTLPEKEYL SVAQEIRNNT
LLIILIAVMM AIGLSTVFVR RQFIRYINEM VKVMKKIAEG DFTIFAHCNS KDEFEDLSNS
INGMVTSQRQ VLEKLSTTTR NLHEAEEQML ETSDYAEHYM EEIAATAQQF LSTAEESRNV
VCNIQQAIYG VTKQAEEVEN MSVDAVAEGV KARQSIKAGL EATEKAVEGI VEIDHAIEMT
VKDVLTLVED SKKIRQFVDY IKKIAKDTNL LALNASIEAA RAGQEGRGFA VVAQEVRKLS
EQSNETAIEI TAVVADILNK VQDVRNKIHY AQQQSIEGKK ASNYAKQSFN TIYQSIEAVG
EMTSKNNEAA KKQVLGIEAV NEYMKKIEEM IYYTVEGAKQ IAEGTQQQSN TMHNITHVSN
ELRDMATELT SIVSCFKISD EEKEESSVDE DQGLSNESVE RLQEELELEI IPSTMEEIDE
EKLEEEKIA
//
