ID A0A1I7GK68_9CLOT Unreviewed; 589 AA.
AC A0A1I7GK68;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Methyl-accepting chemotaxis sensory transducer with Cache sensor {ECO:0000313|EMBL:SFU48833.1};
GN ORFNames=SAMN04487886_103911 {ECO:0000313|EMBL:SFU48833.1};
OS Clostridium sp. DSM 8431.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1761781 {ECO:0000313|EMBL:SFU48833.1, ECO:0000313|Proteomes:UP000198524};
RN [1] {ECO:0000313|EMBL:SFU48833.1, ECO:0000313|Proteomes:UP000198524}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 8431 {ECO:0000313|EMBL:SFU48833.1,
RC ECO:0000313|Proteomes:UP000198524};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FPBY01000039; SFU48833.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7GK68; -.
DR OrthoDB; 9810264at2; -.
DR Proteomes; UP000198524; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd18774; PDC2_HK_sensor; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR033480; sCache_2.
DR PANTHER; PTHR32089:SF92; LYSOZYME-LIKE PROTEIN-RELATED; 1.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR Pfam; PF17200; sCache_2; 1.
DR SMART; SM01049; Cache_2; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000198524};
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 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 209..227
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 231..283
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 302..553
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 589 AA; 65564 MW; 78EDAFE4C4230457 CRC64;
MKKLKTKFIR LNIVIVIAVA IATGSLSVIF LNKNNKNTMT NYEEALKDGY DNVIKYQVEN
VISLLNGIYN KQINGQLSED EAKEEAKNLV KSLRYNEDGY FCIYSTDGTL IAHPMFPEQE
GIYRLNEVDK NGVKFIQNII KIAAIDKGGF TEFYYSKPGQ DEAAPKRVYS ELFNPYGWVI
TTGNYIDDID VKLAEKEKDL NATIMNTNIG IVIISFILMS ISTGIAVKFS DKLLKPITGI
KDFAERLAKY DFSKELEIND ETELGKTAEA LNLAQSNIKK LIKKISDCVE DLTSSAEDLS
RLSTDVNNKV DIVSDFTNEI VNNMSDSKHS VDEVHVCINE ITSSVSDLAS KSTDSSGISI
DFKEKSLKLK EKTTSALNNT EGIYNEKEKK ILESIKYGEV VKEVSATVDE ISDIAEETNM
LALNAAIESA RVGEAGRGFA VVSEEVRQLA EQSSSSAESI QETVAKIEHA FMSLSKDSKE
ILDFMSEDVK KQFNEFILSG EYYYENAEKI SSISEDIAAM SEELSASMEE INSMISSMAE
NTEKSTDNSS KILVKVRETS NAMEEVAVTA EKQNVLAKEL NKLIKDFKI
//