ID A0A1X7FDD6_9PROT Unreviewed; 562 AA.
AC A0A1X7FDD6;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 21.
DE SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:SMF50360.1};
GN ORFNames=SAMN02982917_2568 {ECO:0000313|EMBL:SMF50360.1};
OS Azospirillum oryzae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=286727 {ECO:0000313|EMBL:SMF50360.1, ECO:0000313|Proteomes:UP000192936};
RN [1] {ECO:0000313|EMBL:SMF50360.1, ECO:0000313|Proteomes:UP000192936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A2P {ECO:0000313|EMBL:SMF50360.1,
RC ECO:0000313|Proteomes:UP000192936};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (APR-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- SIMILARITY: Belongs to the methyl-accepting chemotaxis (MCP) protein
CC family. {ECO:0000256|ARBA:ARBA00029447}.
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DR EMBL; FXAK01000005; SMF50360.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X7FDD6; -.
DR STRING; 286727.SAMN02982917_2568; -.
DR OrthoDB; 8482111at2; -.
DR Proteomes; UP000192936; 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; cd19410; HK9-like_sensor; 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 InterPro; IPR007891; CHASE3.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
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; PF05227; CHASE3; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
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 Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Transducer {ECO:0000256|ARBA:ARBA00023224, ECO:0000256|PROSITE-
KW ProRule:PRU00284}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 193..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..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"
FT COILED 256..283
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 562 AA; 58732 MW; 23A0D37059781DEB CRC64;
MFILANLSIS KKISGAFASM VAIALAVAFS SYSKLSFIET SSGWTTHTYE VLEEVSRILG
SVVNQETGVR GYLIAGDDKF LEPYREGQRR YAESLAKAKR LTADNPTQQA RFAEVDHFYR
TWLTTVVEKE IELMAKPETR EQARALEASG AGKSAIDGLR GIIAEIDKME RDLLIKRAVD
QAEAFSTSYT VNFAGGGAMI ILAMAAGIVL SRGIATPIRG MTAVMGRLAA GDNGVQIEGQ
ERRDEIGAMA KAVEVFKRNA IENARLEAEQ EQLKAKAEAD RKASMAALAR SFEASVKGVV
ESVATASGNM QSVATTMVGT AEQTSHQASA SAAAAEQTSA NVQTVAAATE EMSASLLEIS
KQVSTSSQIS AQAVKDAERT NDTVAGLANA AQKIGEVVTL IQSIAGQTNL LALNATIEAA
RAGDAGKGFA VVASEVKNLA TQTARATDEI AAQIATMQAV TTEAVDAIKG IGATITQMSG
IATAIASAVE EQNAATGEIS RNVTQAASGT MEVSTNVIEV QKAASLSGSM AGQVLDAAGE
LSREARTLSS AVDEFLRGVR AA
//
