ID A0A1I5S7F8_9FIRM Unreviewed; 674 AA.
AC A0A1I5S7F8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=Methyl-accepting chemotaxis sensory transducer with Cache sensor {ECO:0000313|EMBL:SFP66738.1};
GN ORFNames=SAMN05444406_10224 {ECO:0000313|EMBL:SFP66738.1};
OS Caldicoprobacter faecalis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Caldicoprobacteraceae;
OC Caldicoprobacter.
OX NCBI_TaxID=937334 {ECO:0000313|EMBL:SFP66738.1, ECO:0000313|Proteomes:UP000198577};
RN [1] {ECO:0000313|EMBL:SFP66738.1, ECO:0000313|Proteomes:UP000198577}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 20678 {ECO:0000313|EMBL:SFP66738.1,
RC ECO:0000313|Proteomes:UP000198577};
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}.
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DR EMBL; FOXR01000002; SFP66738.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I5S7F8; -.
DR STRING; 937334.SAMN05444406_10224; -.
DR OrthoDB; 13222at2; -.
DR Proteomes; UP000198577; Unassembled WGS sequence.
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; cd11386; MCP_signal; 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; 2.
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:UP000198577};
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 270..287
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 293..312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 314..366
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 385..642
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 674 AA; 74115 MW; 6BF21BB545342D1E CRC64;
MIIPISILGY YSRDKAEKAI QQTAAQSTIQ TMEQMSQYLS LVFSTVEEIS MQIFSNKDIQ
DFLLIREDQL TTYDYHQMRQ KVQSVLSNYT MNNKFIDNII LLIDEKRSIA TGNISLSNLN
FEDIKNAEWY KAAIEGNGKI IWRGSHPELD TSATSKTAYC MSGIRAIKHL SSGTIFGVLL
IDVKYEPIMD ILKKANLGSR SEIHLIGPDG HALSSETGEQ INEDESVTTH NITEHDFYQE
IISSEEPAGY KEVTHHGQKW LMIYNRVGET GYTLVGLILN SVLFAATQEI ARTTIMLMVF
ACIFALIVGL YMSNSMGRTI ARIINAAEKV AMGDLTVNPV SRRRDELGVL TRSINSMIAN
MRQLIQQTAA LAHKVVESSS TVASTSQQLS ASSQEIAKAI QEIAQGAAEQ AADAEQGVQK
MDMLAAKINS VSDNARDIHN LSKETMNLTQ QGLDAVDQLE QKARQTTAIT QEILADIDTL
NQHSQAIGKI IKVIDNIADQ TNLLALNAAI EAARAGEMGK GFAVVANEIR KLAEQSMSAT
REITAIIKNT QQQTAQTVKR AKSAEDIVKS QNEAVVTTIS AFKQIAASAE TLVNRVEQII
QGVNEMENDK NQAVLAMQNI SAVSQEAAAS SQEVTASTEE QLSGVEQLAS YAEELNYAAQ
ELMQAISKFK IEQN
//