ID A0A0J1FWS7_9BURK Unreviewed; 514 AA.
AC A0A0J1FWS7;
DT 14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2015, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Chemotaxis protein {ECO:0000313|EMBL:KLU24373.1};
GN ORFNames=EOS_20485 {ECO:0000313|EMBL:KLU24373.1};
OS Caballeronia mineralivorans PML1(12).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Caballeronia.
OX NCBI_TaxID=908627 {ECO:0000313|EMBL:KLU24373.1, ECO:0000313|Proteomes:UP000035963};
RN [1] {ECO:0000313|EMBL:KLU24373.1, ECO:0000313|Proteomes:UP000035963}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PML1(12) {ECO:0000313|Proteomes:UP000035963};
RX PubMed=26205858;
RA Uroz S., Oger P.;
RT "Draft Genome Sequence of Burkholderia sp. Strain PML1(12), an
RT Ectomycorrhizosphere-Inhabiting Bacterium with Effective Mineral-Weathering
RT Ability.";
RL Genome Announc. 3:e00798-15(2015).
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:KLU24373.1}.
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DR EMBL; AEJF01000127; KLU24373.1; -; Genomic_DNA.
DR RefSeq; WP_047848576.1; NZ_AEJF01000127.1.
DR AlphaFoldDB; A0A0J1FWS7; -.
DR PATRIC; fig|908627.4.peg.4589; -.
DR OrthoDB; 9806477at2; -.
DR Proteomes; UP000035963; 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:UniProtKB-KW.
DR GO; GO:0007165; P:signal transduction; IEA:UniProtKB-KW.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd11386; MCP_signal; 1.
DR Gene3D; 1.20.120.30; Aspartate receptor, ligand-binding domain; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR InterPro; IPR035440; 4HB_MCP_dom_sf.
DR InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR004089; MCPsignal_dom.
DR InterPro; IPR003122; Tar_rcpt_lig-bd.
DR PANTHER; PTHR43531:SF14; METHYL-ACCEPTING CHEMOTAXIS PROTEIN I-RELATED; 1.
DR PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF00015; MCPsignal; 1.
DR Pfam; PF02203; TarH; 1.
DR PRINTS; PR00260; CHEMTRNSDUCR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00283; MA; 1.
DR SUPFAM; SSF47170; Aspartate receptor, ligand-binding domain; 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; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Chemotaxis {ECO:0000256|ARBA:ARBA00022500};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Methylation {ECO:0000256|ARBA:ARBA00022481};
KW Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 186..207
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 COILED 470..508
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 514 AA; 53818 MW; 08A223F75E6265C9 CRC64;
MLKNFTIRRG LTITIAGYTL ALVAVLLAAA ACLRQSNQAL EQMVATDTVA ITHLKTSSQR
LLQVRLALGS FETLFMLGKA GDDLLPNARK TLKASDAEFD AYLAKPRDPL EEPLVQAAKA
ARDALIAKAL NLEFDALAQN DFSTFRTLQV QTADGLYATY DHAMSALEAF QIAHQQDRYA
QAQAQFHTMA TAAVIVAALA LVFGFIARGA LSAAVMKPIE SAIHHFEQIA AGDLTASIDA
SRNNEMGRLF AALGKMQQGL VGTVQQVRGG TGAISHGARE IAAGNIDLSQ RTEEQAASLQ
QTASSMEQLT ATVRQNADNA RQASELAVDA SATAVRGGAV VGKVVHTMDD IATSSTRIAD
IIGVIEGIAF QTNILALNAA VEAARAGEEG RGFAVVAGEV RSLAQRSAAA AKEIKELINA
SADKVQAGNA LAGQAGQTMS EVVAAVKRVS DIISEISAAS NEQTGGIEQI NRAVAQMDEV
TQQNAALVEE AAAAAASLEQ QAAQLDVAVA VFRV
//
