ID A0A1G6SDC3_9BURK Unreviewed; 517 AA.
AC A0A1G6SDC3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:SDD14115.1};
GN ORFNames=SAMN05421548_1159 {ECO:0000313|EMBL:SDD14115.1};
OS Paraburkholderia lycopersici.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=416944 {ECO:0000313|EMBL:SDD14115.1, ECO:0000313|Proteomes:UP000198908};
RN [1] {ECO:0000313|Proteomes:UP000198908}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TNe-862 {ECO:0000313|Proteomes:UP000198908};
RA Varghese N., Submissions S.;
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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; FMYQ01000015; SDD14115.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6SDC3; -.
DR STRING; 416944.SAMN05421548_1159; -.
DR OrthoDB; 5298208at2; -.
DR Proteomes; UP000198908; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004888; F:transmembrane signaling receptor activity; IEA:InterPro.
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; 1.20.120.30; Aspartate receptor, ligand-binding domain; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR035440; 4HB_MCP_dom_sf.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR003122; Tar_rcpt_lig-bd.
DR PANTHER; PTHR43531:SF14; METHYL-ACCEPTING CHEMOTAXIS PROTEIN I-RELATED; 1.
DR PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR Pfam; PF02203; TarH; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF47170; Aspartate receptor, ligand-binding domain; 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 Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 186..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 213..265
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 270..499
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT COILED 470..508
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 517 AA; 54936 MW; BDD14DD69B4275C5 CRC64;
MIKNVSIRAR LALAMGFLAA LLVVGGLMGV VGVLMSNGDV KQLYASRLAS SEALSQSNVA
LSRARLWLYR IALDPTSPDV EQETRTAREL LSTSKKAWDA YRALPFSGPE EAQRAADVNG
KFDAFVANGL DLMFSAIATH DAVKIPEVWK SLPPSLFIDV SDGMDSLGAI QVTAAREMFD
AAQARFHWFV GIAVLGIAIA LAAAALAWWS LQRAIGLPLA RAMEHFKAIA DGDLTTDVEV
HSGDEMGQLM SGLDAMQSKL VRTIGAVREG SRSIKTASQE ISAGNLDLSQ RTEEQAASLE
QTAASMDELT STVRQNAENA KQANEVVRST AQLTERGNQA TQEVVQTMRG LSDSSGKIAE
IIGAIEGIAF QTNILSLNAA VEAARAGEQG RGFAVVAGEV RSLAQRSATA SREIRDLITD
SLKRVEAGAR QADSAIGTME AILDSVKSAS SLMSEITSAS EAQSKDIEQV NQAVSEMDRV
TQQNAALVEQ ASAAALSLKE QASQLENAVS IFLVARN
//