ID A0A098U9A5_9BURK Unreviewed; 548 AA.
AC A0A098U9A5;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 26.
DE SubName: Full=Membrane protein {ECO:0000313|EMBL:KGF79523.1};
GN ORFNames=IA69_23570 {ECO:0000313|EMBL:KGF79523.1};
OS Massilia sp. JS1662.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1519190 {ECO:0000313|EMBL:KGF79523.1, ECO:0000313|Proteomes:UP000029701};
RN [1] {ECO:0000313|EMBL:KGF79523.1, ECO:0000313|Proteomes:UP000029701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS1662 {ECO:0000313|EMBL:KGF79523.1,
RC ECO:0000313|Proteomes:UP000029701};
RA Fida T.T., Spain J.C.;
RT "Identification of Arachidin-3 degrading bacteria in the peanut
RT rhizosphere.";
RL Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
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:KGF79523.1}.
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DR EMBL; JPQD01000031; KGF79523.1; -; Genomic_DNA.
DR RefSeq; WP_036237891.1; NZ_JPQD01000031.1.
DR AlphaFoldDB; A0A098U9A5; -.
DR OrthoDB; 5441488at2; -.
DR Proteomes; UP000029701; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; cd19411; MCP2201-like_sensor; 1.
DR CDD; cd11386; MCP_signal; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR024478; HlyB_4HB_MCP.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR047347; YvaQ-like_sensor.
DR PANTHER; PTHR43531:SF14; METHYL-ACCEPTING CHEMOTAXIS PROTEIN II-RELATED; 1.
DR PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR Pfam; PF12729; 4HB_MCP_1; 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.
PE 3: Inferred from homology;
KW Membrane {ECO:0000256|SAM:Phobius};
KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 191..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 213..265
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 270..499
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT REGION 522..548
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 548 AA; 57233 MW; 1F7C3639607EDDE5 CRC64;
MNIQNLKIGA RLGLAFAAVL ALSALLTVVG ALRLQQVVSA TADMDASVSK TRLADRRLAS
TRINRALTEA RLRAVDAQDR ERINAKMKAN SEEISRIDEE LQRLVASDKG KQLMAALGER
RKAYTTARKK VFALKDGGTV DASAIERAAD AEMNPALAAY EAAAADLAEH QKTGFDDAKA
RIQDIAASGR LLLVGVGIVA VLLGAALAWW LTRSITGPLR RAVTVANAVA QGDLTTRIEV
ERRDETGELM IALQTMNANL NALVTRVRSG ADTIATAAVE VATGNHDLSA RTEQQAGALE
ESAASMEELT STVRQNADNA RQGNQMAASA STVAVRGGDV VAQVVETMGA IDASSKKIVD
IIGVIDGIAF QTNILALNAA VEAARAGEQG RGFAVVANEV RTLAQRSAGA AREIKELIGD
SVEKVAAGSR LVGEAGTTIQ EVVASVRRVS DIMAEISAAS GEQSAGIEQV GAAIQQMDQV
TQQNAALVEE AAAATESMQE QARSLAEAVS VFKLDHAGAS AARAPARPQP ALASHRPAAA
SGKGWELF
//