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Database: UniProt
Entry: A0A1W9R9Z2_9BACT
LinkDB: A0A1W9R9Z2_9BACT
Original site: A0A1W9R9Z2_9BACT 
ID   A0A1W9R9Z2_9BACT        Unreviewed;       777 AA.
AC   A0A1W9R9Z2;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=B6D64_02210 {ECO:0000313|EMBL:OQX81247.1};
OS   Bacteroidetes bacterium 4484_276.
OC   Bacteria; Bacteroidota.
OX   NCBI_TaxID=1970779 {ECO:0000313|EMBL:OQX81247.1, ECO:0000313|Proteomes:UP000192605};
RN   [1] {ECO:0000313|Proteomes:UP000192605}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Dombrowski N., Seitz K., Teske A., Baker B.;
RT   "Novel pathways for hydrocarbon cycling and metabolic interdependencies in
RT   hydrothermal sediment communities.";
RL   Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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:OQX81247.1}.
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DR   EMBL; NATG01000026; OQX81247.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1W9R9Z2; -.
DR   Proteomes; UP000192605; Unassembled WGS sequence.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   CDD; cd00130; PAS; 3.
DR   CDD; cd17574; REC_OmpR; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 4.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 4.
DR   PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR   Pfam; PF08447; PAS_3; 2.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   SMART; SM00086; PAC; 3.
DR   SMART; SM00091; PAS; 3.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR   PROSITE; PS50113; PAC; 2.
DR   PROSITE; PS50112; PAS; 3.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          22..139
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          352..424
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          427..479
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          480..552
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          556..609
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          610..680
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   COILED          165..206
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         71
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   777 AA;  89681 MW;  E7FCB008215C323D CRC64;
     MHGTALFRCA SKKINKVKKK YKILIVEDST TAMLYTSDIV RRAGYEVIEA INGKVALQKL
     RGGTIDMVIS DILMPEMDGF QLLKHVREDD NLKDIPFIFR TATYTSDKDR AFGFKLGVDE
     YIRKFSVHKV LTELIQDIFK KVEAGGFVPN KPIMGQEGET YKLYNERLVR KLEKKMLDLE
     NETIEHKKAE EDLKQSEENY RNIFDSNPLP LGEEDWSGAK ELLEKEKTKG RAINKEYFDE
     NPEFFNKCMS SIKVIQVNRA ILDLFKYKTS DGFIHNILDI FTERAYETNK NELIAVANDE
     PTFSEETELL DSEGNLISAI VQYKIVGSYK KVIFSVIDIT ERKKAEEALI ASKEKFHTVA
     DFAYDWEYWI SPQDEFIYIS PSCERITGYK PNEFKQNPGL LTSIVHPDDV DNWKNHKHHA
     FNKAEIESIE FRIIKKSGEE CWIGHVCQTV YNDNGDNIGI RGSNRNITDS KKTEEALKVS
     EDRLSKTLMA ANDGMWDWDL TTNKVYFDPR YYEMAGYAID GFPHEFDEFQ KRVHPDDFEN
     VLSQAQQHIE GKIARFRVEF RFKKKSGDWL WVLGRGLIVE HDVNNRPLRF IGTHTDITER
     KKAEEEIIKI NSKLTATINA LPDLMFETDN EGRIYDYHAQ KSDLLYAKPE DFLGKKIDEI
     LPTAAAKICN NAISEAIGTG KYSGAVYSLQ LPRGLSWFEL SIATKDDANT AEKRAIMLVR
     DITGRKKAEE ELKSRMQELE IFNEVTVDRE LLINGLRDEV NSLLNKLGKE RKYDIVQ
//
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