ID A0A239ES99_9PROT Unreviewed; 562 AA.
AC A0A239ES99;
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:SNS47630.1};
GN ORFNames=SAMN05880556_105143 {ECO:0000313|EMBL:SNS47630.1};
OS Azospirillum sp. RU38E.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=1907313 {ECO:0000313|EMBL:SNS47630.1, ECO:0000313|Proteomes:UP000198368};
RN [1] {ECO:0000313|EMBL:SNS47630.1, ECO:0000313|Proteomes:UP000198368}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU38E {ECO:0000313|EMBL:SNS47630.1,
RC ECO:0000313|Proteomes:UP000198368};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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; FZOI01000005; SNS47630.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239ES99; -.
DR OrthoDB; 7260004at2; -.
DR Proteomes; UP000198368; 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; 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; 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:UP000198368};
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 189..212
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 213..266
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 299..542
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"
SQ SEQUENCE 562 AA; 60075 MW; 796C27033B77204A CRC64;
MLSNLKISHR LLLFVPVLAV ALILAVGSGL STLRTTLVQD RQQELIQILT IVRGIAQNWH
DREQSGEMTR EQAQKGAGDD IRKLRFGNGE YIYINNYDGV TVVHAKRDFE GKNRMGFKTA
DGVETVRLGV EAAKKGGGFF TYNFSRPGVN GGEAVNVPKL SYSLGFEPWQ WALGTGVYID
DIDETFNAIL VKMLLLAAAI LLTGSAVAVL LARSIARPLT MMTDRMGQLA DGDLAVEIPL
LSDRNEMGRL AQALDVFKRN GLRAQELTRA QQAEQEAKER RQVAVEKSLA DFQDKAAHIV
GNLVDASEKV RNHSSGLASM AQQSRGLIDG VNQAASETTS NVQMIASAAE ELAAAVGEVN
QQVTRSTDIA ERAVHEAGQT SATMGGLAEA AQNIGSIIQV ISDIASQTNL LALNATIEAA
RAGEAGKGFA VVASEVKTLA SQTTKATDEI QSYVTGIQRE THRAVEAIDN IARVVNDMRT
IATGIASAME QQGATTADIA RNINQAAMGT QQVSANVVGV AGAAEQTAQS ANSLNGASED
LRRDAETLNT EITSFFNRLR AI
//
