ID U5S1I6_9CLOT Unreviewed; 662 AA.
AC U5S1I6;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 2.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:AGY77669.2};
GN ORFNames=CAETHG_3466 {ECO:0000313|EMBL:AGY77669.2};
OS Clostridium autoethanogenum DSM 10061.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1341692 {ECO:0000313|EMBL:AGY77669.2, ECO:0000313|Proteomes:UP000017590};
RN [1] {ECO:0000313|EMBL:AGY77669.2, ECO:0000313|Proteomes:UP000017590}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 10061 {ECO:0000313|EMBL:AGY77669.2};
RX PubMed=24655715; DOI=10.1186/1754-6834-7-40;
RA Brown S.D., Nagaraju S., Utturkar S., De Tissera S., Segovia S.,
RA Mitchell W., Land M.L., Dassanayake A., Kopke M.;
RT "Comparison of single-molecule sequencing and hybrid approaches for
RT finishing the genome of Clostridium autoethanogenum and analysis of CRISPR
RT systems in industrial relevant Clostridia.";
RL Biotechnol. Biofuels 7:40-40(2014).
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; CP006763; AGY77669.2; -; Genomic_DNA.
DR AlphaFoldDB; U5S1I6; -.
DR KEGG; cah:CAETHG_3466; -.
DR PATRIC; fig|1341692.11.peg.3480; -.
DR HOGENOM; CLU_000445_107_19_9; -.
DR Proteomes; UP000017590; 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 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; 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 Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
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 7..27
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 281..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 305..356
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 375..614
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT COILED 516..543
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 662 AA; 72936 MW; F644D5FFFE7204D9 CRC64;
MLKKGKSLQV IAVVGISVIF IALISLVTSI EYMNSKKLIL SSMEKSGKQT VTIHAQNLSS
WIKARLSQVE VIANTQLVSS MNYSEIIPYF KREQKNYNGV FNTIGISDTS GKLIMQNDVT
IDISSEDTFP KVIQGKEIIS DPFKDKQNPS NLIISMECPV KDIKSGKAIG LVSGACLVST
VFKENTNFHI GQTDKVYILS NKGDVLYKQS NDPLNETNLL KSSNSELNGL VKEALSKDSF
LGQFKDKDGT KMLFSARVNG TDWYMLLQVP TKEYTSSLNS LLYLILAVSV LAIIFLIVIL
IILLKKFFDR LLKISLIADE VAEGNLMNSL PESSDELGRI NTTFNKMINN LKNIIIKIRN
VSEVVAESSN SYKEVSLEVV QEGKNIKQSI DNLTSGSKNI AEEIQNITVS VNDVEDKSRK
LAEISAKIDE MIAEAKDKTS DGSKNLHTTV ELLNKMEQKV NISSDVVTEL SEKSKTIANV
TTTITDIAEQ TNLLALNASI EAARAGDQGK GFEVVAEEVR KLAEQSEVAA QEISKEIQEI
QGKITNAVVS MDESINYVGL GIKSTDNILV IFSEIEKEID RIKTMSFNVS EIAKIVLQNN
RKILESVSNT SAMSEEAVAS ALSFQDMVSK QEDIFLNLKG ASEHLDELSA ALSGEIFKFK
VN
//
