ID A0A098UGQ9_9BURK Unreviewed; 670 AA.
AC A0A098UGQ9;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=Chemotaxis protein {ECO:0000313|EMBL:KGF82078.1};
GN ORFNames=IA69_09135 {ECO:0000313|EMBL:KGF82078.1};
OS Massilia sp. JS1662.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=1519190 {ECO:0000313|EMBL:KGF82078.1, ECO:0000313|Proteomes:UP000029701};
RN [1] {ECO:0000313|EMBL:KGF82078.1, ECO:0000313|Proteomes:UP000029701}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JS1662 {ECO:0000313|EMBL:KGF82078.1,
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:KGF82078.1}.
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DR EMBL; JPQD01000007; KGF82078.1; -; Genomic_DNA.
DR RefSeq; WP_036231730.1; NZ_JPQD01000007.1.
DR AlphaFoldDB; A0A098UGQ9; -.
DR OrthoDB; 9763018at2; -.
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; cd11386; MCP_signal; 1.
DR CDD; cd12912; PDC2_MCP_like; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR033462; Cache_3-Cache_2.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR029151; Sensor-like_sf.
DR PANTHER; PTHR43531:SF14; METHYL-ACCEPTING CHEMOTAXIS PROTEIN I-RELATED; 1.
DR PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR Pfam; PF17201; Cache_3-Cache_2; 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 SUPFAM; SSF103190; Sensory domain-like; 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 20..39
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 334..353
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 355..407
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 412..641
FT /note="Methyl-accepting transducer"
FT /evidence="ECO:0000259|PROSITE:PS50111"
SQ SEQUENCE 670 AA; 71782 MW; 6290DD085B30332C CRC64;
MNKKSFSVAN WTVGSKITAF TFALVSVILA GLVLTITWTT SSMLHARAIA NVHSELQSVV
NAVEMFDNVM KSQATSFGRI FATHFEGEFS LDPDAIVAVG DKQVPTLKVG GKPLNLDFTL
PDRFTRQTGG NATIFVASGD DFVRVSTSVK KENGDRAVGT ILAHESPAYA AIRAGKPYVG
LVKLFGKQFM TDYEPIRDTS GKVIGILYIG LDVDANIAAL RDRIKKMKVG DTGYYFVLDA
TKGKTYGDLV VHPVKEGKNI LASKDASGRE FIREMLETKQ GLITYPWMNA EAGETSPRTK
VAAYTLFKDW NWLIAGGTYE DEITKEAARL RNHYIVVGLV ALAIFAAILH TVMKRTVTRP
LVRARDAAVR IAEGDLTVRM AVDRSDEIGL LAEAMNSISS SLSTVVGQVR SGAEQIANAS
GEISSGNLDL CSRTEQQAAN LASTANSMQD LTETVRRNAG DAHEANQLAV NTSMVAQEGG
RMVREVIDTM DTIKASSGKI GDIIGVIDGI AFQTNILALN AAVEAARAGE QGRGFAVVAT
EVRNLAQRSA AAAKEIKGLI VASTAEVDTG SRIVQEAGVT MNEVLASAEK VTAIMARIST
ANAAQSSGIE HINRSIGEMD QVTQQNAALV EEASAAAQAM QEQADQLARS VRLFKLDQQQ
ASARPALPQY
//