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Database: UniProt
Entry: A0A063BQ63_9BURK
LinkDB: A0A063BQ63_9BURK
Original site: A0A063BQ63_9BURK 
ID   A0A063BQ63_9BURK        Unreviewed;       517 AA.
AC   A0A063BQ63;
DT   03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT   03-SEP-2014, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Methyl-accepting chemotaxis sensory transducer with Cache sensor {ECO:0000313|EMBL:KDB10649.1};
GN   ORFNames=LIG30_4825 {ECO:0000313|EMBL:KDB10649.1};
OS   Burkholderia sp. lig30.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Burkholderia.
OX   NCBI_TaxID=1192124 {ECO:0000313|EMBL:KDB10649.1, ECO:0000313|Proteomes:UP000027020};
RN   [1] {ECO:0000313|EMBL:KDB10649.1, ECO:0000313|Proteomes:UP000027020}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LIG30 {ECO:0000313|Proteomes:UP000027020};
RA   Woo H.L., Utturkar S.M., Klingeman D.M., Simmons B.A., DeAngelis K.M.,
RA   Brown S.D., Hazen T.C.;
RT   "Draft Genome of the Lignin-degrading Burkholderia sp. Strain LIG30,
RT   Isolated from Wet Tropical Forest Soil.";
RL   Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {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:KDB10649.1}.
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DR   EMBL; JGVW01000004; KDB10649.1; -; Genomic_DNA.
DR   RefSeq; WP_038708660.1; NZ_JGVW01000004.1.
DR   AlphaFoldDB; A0A063BQ63; -.
DR   STRING; 1192124.LIG30_4825; -.
DR   PATRIC; fig|1192124.4.peg.80; -.
DR   eggNOG; COG0840; Bacteria.
DR   OrthoDB; 8555762at2; -.
DR   Proteomes; UP000027020; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma 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   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR004090; Chemotax_Me-accpt_rcpt.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR004089; MCPsignal_dom.
DR   InterPro; IPR033480; sCache_2.
DR   PANTHER; PTHR43531:SF14; METHYL-ACCEPTING CHEMOTAXIS PROTEIN I-RELATED; 1.
DR   PANTHER; PTHR43531; PROTEIN ICFG; 1.
DR   Pfam; PF00015; MCPsignal; 1.
DR   Pfam; PF17200; sCache_2; 1.
DR   PRINTS; PR00260; CHEMTRNSDUCR.
DR   SMART; SM01049; Cache_2; 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   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000027020};
KW   Transducer {ECO:0000256|PROSITE-ProRule:PRU00284};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        191..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          215..266
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          271..500
FT                   /note="Methyl-accepting transducer"
FT                   /evidence="ECO:0000259|PROSITE:PS50111"
FT   COILED          471..509
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   517 AA;  55232 MW;  C3BDA6F282060FBC CRC64;
     MRNLTLNQKL ASMIVILWLG LLVIAGLGAW QTRTSMIEDR REQLATLVAQ ATSVADHFYK
     LSQQNAMTEA DAKQKAIEAI AAMRYNGDGY MALNDSTPRM IMHPIKPELN GKDVSQLTDP
     KGTHVFVAAV KAANQGAGKG YFDYYWPRPG ADKPIPKTSA VQRFAPWDWY VVTGMYTDDV
     QAAVLASVGR WLAMTTVLGT IATIVMLLVV RSVRANLGGE LEAALDTAQR IAQGDLTSRV
     DVKHENPGSL LHALHAMQGA LIDMVSRVRA GTENINVGAS EIAAGNTDLS QRTEEQAAAL
     VQTASSMDQM TANVKQNADS AAQAASLADQ AAQVATRGSV VVEDVVRTMD EITDRSRKIG
     DIIGVIDGIA FQTNILALNA AVEAARAGEQ GRGFAVVAAE VRSLAQRSAT AAKEIKTLIE
     SSNETVEQGA TLVTRAGTTM GEVVQSVRRV NEILDEISNA SREQSAGIEQ VNRAVGEMDQ
     VTQQNAALVE EAAAAAHSLR DQAEALRDAV TRFALPA
//
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