ID F7NY99_9GAMM Unreviewed; 543 AA.
AC F7NY99;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:EGM77152.1};
GN ORFNames=Rhein_2782 {ECO:0000313|EMBL:EGM77152.1};
OS Rheinheimera sp. A13L.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales; Chromatiaceae;
OC Rheinheimera.
OX NCBI_TaxID=506534 {ECO:0000313|EMBL:EGM77152.1, ECO:0000313|Proteomes:UP000004282};
RN [1] {ECO:0000313|EMBL:EGM77152.1, ECO:0000313|Proteomes:UP000004282}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A13L {ECO:0000313|EMBL:EGM77152.1,
RC ECO:0000313|Proteomes:UP000004282};
RX PubMed=21742876; DOI=10.1128/JB.05636-11;
RA Gupta H.K., Gupta R.D., Singh A., Chauhan N.S., Sharma R.;
RT "Genome Sequence of Rheinheimera sp. Strain A13L, Isolated from Pangong
RT Lake, India.";
RL J. Bacteriol. 193:5873-5874(2011).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGM77152.1}.
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DR EMBL; AFHI01000025; EGM77152.1; -; Genomic_DNA.
DR RefSeq; WP_008899624.1; NZ_AFHI01000025.1.
DR AlphaFoldDB; F7NY99; -.
DR STRING; 506534.Rhein_2782; -.
DR eggNOG; COG0840; Bacteria.
DR OrthoDB; 9781845at2; -.
DR Proteomes; UP000004282; 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:InterPro.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd11386; MCP_signal; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR033480; sCache_2.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 1.
DR PANTHER; PTHR32089:SF119; METHYL-ACCEPTING CHEMOTAXIS PROTEIN TLPQ; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR Pfam; PF17200; sCache_2; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM01049; Cache_2; 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.
DR PROSITE; PS50192; T_SNARE; 1.
PE 3: Inferred from homology;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
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..33
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 187..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 211..265
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 270..506
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT DOMAIN 457..519
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
SQ SEQUENCE 543 AA; 58993 MW; 59C88DEE9E1B963A CRC64;
MLRSLSIKTR LFAIVGVAVL GQLLVCWLVL SGLKQSILEE KRLSTLYLSQ VAVALVNNYH
GKVGTGELDE AKAKQLVLAE LKSLRYKEND YYFVIDQQVT MLMHPFRPDL DGKSVADFKD
KQGELLFQNM ADGVADDGSH SVFYNWPKPG ATEEVPKISH VELFKPWGWI VGTGIYIDDV
DASFYEVVLQ LAALVFFVVG LMLALSWYVT RSVVKPMTDV VAAMQDIASG DGDLMVKLSY
DGKDELAALA TAFNLFVGKI RQLITSVGVT SADVNESALD VARISQQISK ESVQQQQETD
MVATAITQMS SAIAEVAQSA EQANHETAQV ETLVEQGMKL MKASVESIHT QSQTIEQSSV
VASSLYTSSQ NISHVLNIIN KLADQTNLLA LNAAIEAARA GEHGRGFSVV ADEVRTLAHQ
TQKSTQEISG IIAELQQGTQ QMTAAVQESK TAAELNINLA VQVQQALTDI ANSITQISDM
NAHIATAAEQ QSAVAGEVDQ NVHTISQLVH QTAGAIKGSD QSTQRLTQLS QDLKDLVKQF
KVQ
//
