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Database: UniProt
Entry: A0A085EV05_9BURK
LinkDB: A0A085EV05_9BURK
Original site: A0A085EV05_9BURK 
ID   A0A085EV05_9BURK        Unreviewed;       545 AA.
AC   A0A085EV05;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   SubName: Full=Methyl-accepting chemotaxis protein {ECO:0000313|EMBL:KFC63050.1};
GN   ORFNames=FG94_04392 {ECO:0000313|EMBL:KFC63050.1};
OS   Massilia sp. LC238.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Telluria group; Massilia.
OX   NCBI_TaxID=1502852 {ECO:0000313|EMBL:KFC63050.1, ECO:0000313|Proteomes:UP000028601};
RN   [1] {ECO:0000313|EMBL:KFC63050.1, ECO:0000313|Proteomes:UP000028601}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LC238 {ECO:0000313|EMBL:KFC63050.1,
RC   ECO:0000313|Proteomes:UP000028601};
RA   Gan H.M., Gan H.Y., Barton H.A., Savka M.A.;
RT   "Genome sequence of acyl-homoserine lactone-producing cave bacterial
RT   isolate.";
RL   Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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:KFC63050.1}.
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DR   EMBL; JNNN01000078; KFC63050.1; -; Genomic_DNA.
DR   RefSeq; WP_051996992.1; NZ_JNNN01000078.1.
DR   AlphaFoldDB; A0A085EV05; -.
DR   STRING; 1502852.FG94_04392; -.
DR   PATRIC; fig|1502852.3.peg.4338; -.
DR   eggNOG; COG0840; Bacteria.
DR   OrthoDB; 5441488at2; -.
DR   Proteomes; UP000028601; 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; cd11386; MCP_signal; 1.
DR   Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 1.
DR   InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR   InterPro; IPR024478; HlyB_4HB_MCP.
DR   InterPro; IPR004089; MCPsignal_dom.
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; PF00015; MCPsignal; 1.
DR   PRINTS; PR00260; CHEMTRNSDUCR.
DR   SMART; SM00283; MA; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR   PROSITE; PS50111; CHEMOTAXIS_TRANSDUC_2; 1.
PE   4: Predicted;
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        12..31
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        193..215
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          277..506
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   COILED          477..515
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   545 AA;  57361 MW;  4E0E7DF1D23D8FF1 CRC64;
     MKKKSLTIGT RLAVGYGAVS FLMIVLTALA ISRVGNIDSI LNHINDVNNV KQRYAINFRG
     SVHDRAIALR DVVLAADPAA AAAPVKPIQV LDENYTRSAE PMDRLFRELN DIQPAEKAAL
     ASIKEQERRT RPLIERVIAL HAAGQAQEAA ALLSREAAPA FVDWLASINA FIDMQEQQNK
     LEAAGARKMA SGFFGWMTLL CLGAIAVGAT GAWIITRGLL RQLGGQPDYA ASIVRAIAAG
     DLGVKIETAP GDSRSLLFAM KGMRDSLVAI VGQVRHGTLN MASVSTEIAD GNRDLSHRTE
     RQAGTLEATT ASVEQLTATV RQNADNARQA NALAESASEV ALRGGMVVSQ VVETMASIND
     SSKRIVDIIG VIDGIAFQTN ILALNAAVEA ARAGEQGRGF AVVATEVRNL AQRSASAARE
     IKLLIGSSVE RVDAGARLVD EAGSTMNDIV ASVRRVTDIM AEISRASAEQ SAGIGKVNDA
     IGQMDEATRQ NAALVQQATA AAAALEEEAE RLAQVVSVFC LEATNDGALA APARLAIAEG
     GSISD
//
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