ID G1XY30_9PROT Unreviewed; 562 AA.
AC G1XY30;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE SubName: Full=Methyl-accepting chemotaxis protein 4 {ECO:0000313|EMBL:EGY01830.1};
GN ORFNames=AZA_88383 {ECO:0000313|EMBL:EGY01830.1};
OS Nitrospirillum amazonense Y2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Nitrospirillum.
OX NCBI_TaxID=1003237 {ECO:0000313|EMBL:EGY01830.1, ECO:0000313|Proteomes:UP000018435};
RN [1] {ECO:0000313|EMBL:EGY01830.1, ECO:0000313|Proteomes:UP000018435}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y2 (ATCC 35120) {ECO:0000313|Proteomes:UP000018435};
RX PubMed=21838888; DOI=10.1186/1471-2164-12-409;
RA Sant'anna F.H., Almeida L.G., Cecagno R., Reolon L.A., Siqueira F.M.,
RA Machado M.R., Vasconcelos A.T., Schrank I.S.;
RT "Genomic insights into the versatility of the plant growth-promoting
RT bacterium Azospirillum amazonense.";
RL BMC Genomics 12:409-409(2011).
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}.
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:EGY01830.1}.
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DR EMBL; AFBX01000226; EGY01830.1; -; Genomic_DNA.
DR RefSeq; WP_004272274.1; NZ_AFBX01000226.1.
DR AlphaFoldDB; G1XY30; -.
DR PATRIC; fig|1003237.3.peg.1510; -.
DR Proteomes; UP000018435; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd18774; PDC2_HK_sensor; 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; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR033480; sCache_2.
DR InterPro; IPR000727; T_SNARE_dom.
DR PANTHER; PTHR32089:SF112; METHYL-ACCEPTING CHEMOTAXIS PROTEIN CTPH; 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 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 inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000018435};
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 193..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..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"
SQ SEQUENCE 562 AA; 60540 MW; E67EF3517799029C CRC64;
MLNKLKISHR LALFMPMLVL ALGLAVSFAL TSLRHTLTED RKEELKQILM VTRGVAQNWY
DREQSGELTR AQAQKGAQDD IRKLRFGNGE YVYVNQYDGL TVVHIKKEFE GKNRMDFKTA
DGVETVRLGI EAAKQGGGSF TYTYPRPGNK GGPSQNFPKM TYSLGFEPWQ WALGTGIYVD
DIDDIYHDIL IDMLMLTAIV VGAGGLVAYM LARSIAKPLK LMTERMGQLA DGDLTVDIPL
LNDRHEIGRL ARALEVFKRN GLRNAELTQA QQAEQQEKLR RQEAVEASLA DFQQRSARVL
SNVVHASEDV RNHSSGLADM ATQSRGMVEM ANHASAETTG NVQMIASAAE ELAAAVGEVN
SQVTRSTDIA ERAVAQAEQT GVTMQGLADA AQSIGNIIQV IQEIAGQTNL LALNATIEAA
RAGEAGKGFA VVASEVKTLA SQTTKATDEI QGYITGIQQE TTRAVEAIGS IATVVGDMRT
IATAIASAME QQGATTSEIA RNINQAAMGT QQVSTNIVGV AGAAEQTSQS ANALHTASEA
LRQDADALNA EITGFFARLR AI
//