ID A0A1G6XEE6_9PROT Unreviewed; 661 AA.
AC A0A1G6XEE6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:SDD76432.1};
GN ORFNames=SAMN05421720_101470 {ECO:0000313|EMBL:SDD76432.1};
OS Rhodospira trueperi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Rhodospirillaceae; Rhodospira.
OX NCBI_TaxID=69960 {ECO:0000313|EMBL:SDD76432.1, ECO:0000313|Proteomes:UP000199412};
RN [1] {ECO:0000313|EMBL:SDD76432.1, ECO:0000313|Proteomes:UP000199412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700224 {ECO:0000313|EMBL:SDD76432.1,
RC ECO:0000313|Proteomes:UP000199412};
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; FNAP01000001; SDD76432.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G6XEE6; -.
DR STRING; 69960.SAMN05421720_101470; -.
DR OrthoDB; 7260004at2; -.
DR Proteomes; UP000199412; 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 Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 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:SF112; HEME-BASED AEROTACTIC TRANSDUCER HEMAT; 1.
DR PANTHER; PTHR32089; METHYL-ACCEPTING CHEMOTAXIS PROTEIN MCPB; 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 Reference proteome {ECO:0000313|Proteomes:UP000199412};
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..34
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 212..265
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 306..528
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT DOMAIN 458..520
FT /note="T-SNARE coiled-coil homology"
FT /evidence="ECO:0000259|PROSITE:PS50192"
FT REGION 504..538
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 504..524
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 661 AA; 70791 MW; F9486D5307991A71 CRC64;
MSLENIRVSR KIWFPTIIAA LGLLAVVAFA AMLVRAEILS ERVGRVQSVA ESAVSIIAGF
HSRVEAGEID METAQTLAKN AIRDMRYNGG AEYVFVYDYE GVNRVMGPRP EWEGTNKLDL
TDSDGKRLIA ELIAAARAGG GSVSYRFPRG GSDVPEPKVS WAEPFEPWRW MVGTGVYVSD
VDAAAVNKAL RLSGVAALVL AVAAGVALVI IRGITRPLLN LTKTMTALAR GELEAIVPDQ
NRHDEVGEMA HAVQVFKENA QEVQRLQTEQ TTQARRNERR VKGEMLALTN ALDEEVRSAI
SIVMQQSDAM HEAALEMAQS VAQTEQGAGA AATASRNASD SVDAVAAAAE EMASSIAEIG
HQVTNAAAVA HRAVEEAETT NQRIGGLAEA ANQIGDVVNM ISDIAQQTNL LALNATIEAA
RAGEAGKGFA VVANEVKTLA NQTAKATEDI GNQIASMQSA TDQAVHAIQA ISTVIEQLNE
TTTAISTAVE QQSAATKEIS QNAQQAAHNT QDASENIDRV SDSSETTGGH AREVKDSSGE
VRNHIRYMQK ALERIVRSTS DEDRENNILR TVNVAVTLDL GDGNAVPCLL NEIAFSGVAT
LDRVLKQERG QEFRMTLPDL GNVTGTIVAH TNLSTHVRLE IPENQTASLR AVVSRREKAR
T
//
