ID A0A098UGD0_9BURK Unreviewed; 516 AA.
AC A0A098UGD0;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Chemotaxis protein {ECO:0000313|EMBL:KGF83526.1};
GN ORFNames=IA69_01745 {ECO:0000313|EMBL:KGF83526.1};
OS Massilia sp. JS1662.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1519190 {ECO:0000313|EMBL:KGF83526.1, ECO:0000313|Proteomes:UP000029701};
RN [1] {ECO:0000313|EMBL:KGF83526.1, ECO:0000313|Proteomes:UP000029701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS1662 {ECO:0000313|EMBL:KGF83526.1,
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:KGF83526.1}.
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DR EMBL; JPQD01000001; KGF83526.1; -; Genomic_DNA.
DR RefSeq; WP_036228085.1; NZ_JPQD01000001.1.
DR AlphaFoldDB; A0A098UGD0; -.
DR OrthoDB; 8576332at2; -.
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 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 I-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 Coiled coil {ECO:0000256|SAM:Coils}; 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 190..211
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 212..264
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 269..498
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
FT COILED 487..514
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 516 AA; 54133 MW; 19F9EA956F82D020 CRC64;
MKMSNFRIGT RLAGGFGLVL VLLAFVVAVG LQRFHDVGLA TTTLIDDDWA KAEAAATIDT
MTRANARRTL ELFIAPDDGY RARVREKIAA NRREIDGALA TLRRLVASEE GKAVLARVIE
RREAYVASFT QVNALVAAGK RDEAQQLVLA ETLPRLDVLQ QAVHDLNVLQ KGRAVAAGKA
VRDRIASGRV LMLALGAAAL AVSLVLAISL ARSIVLPLRS AVAVAQRVAG GDLTSKIEAR
SKDEVGELLG ALATMNASLG TMVGEVRRGT ETIATASSQI ASGNMDLSAR TEMQASALQQ
SASSMEELTG TVQQNADNAR EANALAAATA TITAEGSDAV ARVAATMDEI SDGARRIADI
TGIIDGIAFQ TNILALNAAV EAARAGEQGK GFAVVATEVR NLAQRSAAAA REIRHLIDDS
TAKIAGGTEL TGRAADTMQR VLASVRKVTG IMADITAASD EQRIGIEQVN QAVGQMDSVT
QQNAALVEQA AGAAQALQEQ AHTLNETIRM FRLEAA
//
