ID   A1VT21_POLNA            Unreviewed;       807 AA.
AC   A1VT21;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   27-MAR-2024, entry version 112.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Pnap_3502 {ECO:0000313|EMBL:ABM38799.1};
OS   Polaromonas naphthalenivorans (strain CJ2).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Polaromonas.
OX   NCBI_TaxID=365044 {ECO:0000313|EMBL:ABM38799.1, ECO:0000313|Proteomes:UP000000644};
RN   [1] {ECO:0000313|Proteomes:UP000000644}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CJ2 {ECO:0000313|Proteomes:UP000000644};
RX   PubMed=19453698; DOI=10.1111/j.1462-2920.2009.01947.x;
RA   Yagi J.M., Sims D., Brettin T., Bruce D., Madsen E.L.;
RT   "The genome of Polaromonas naphthalenivorans strain CJ2, isolated from coal
RT   tar-contaminated sediment, reveals physiological and metabolic versatility
RT   and evolution through extensive horizontal gene transfer.";
RL   Environ. Microbiol. 11:2253-2270(2009).
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};
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DR   EMBL; CP000529; ABM38799.1; -; Genomic_DNA.
DR   RefSeq; WP_011802870.1; NC_008781.1.
DR   AlphaFoldDB; A1VT21; -.
DR   STRING; 365044.Pnap_3502; -.
DR   KEGG; pna:Pnap_3502; -.
DR   eggNOG; COG2203; Bacteria.
DR   eggNOG; COG3829; Bacteria.
DR   eggNOG; COG4251; Bacteria.
DR   HOGENOM; CLU_000445_114_71_4; -.
DR   OrthoDB; 9808408at2; -.
DR   Proteomes; UP000000644; Chromosome.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 2.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 3.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 3.
DR   PANTHER; PTHR42878:SF7; BACTERIOPHYTOCHROME; 1.
DR   PANTHER; PTHR42878; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF13188; PAS_8; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 3.
DR   SMART; SM00091; PAS; 3.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 2.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:ABM38799.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000644};
KW   Transferase {ECO:0000313|EMBL:ABM38799.1}.
FT   DOMAIN          13..58
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          458..528
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          531..583
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          594..807
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   807 AA;  88555 MW;  DE7508DDC95BFD86 CRC64;
     MMPEDKPMQA SITASLLAGV LESAMDAIIT VDAQQNIVLF NHAAEKMFGW SRQEVMQQPL
     DKLIPGRFRH AHARHLAQFG ATGATVRSMA DSLVPIYGLR ANGQEFAVDV SISRVDTPEG
     KLFTAMVRDI TGRKLAGQAL VDSEQRYAAL FASAPVPMWV IDRASRKFLT VNQAAIEGYG
     HSAGEFLSMT LPDIHADAER SCLPYYLADA AQKRQGSCQH RRKDGSLFNA DIVVRPIQYA
     GQEALFMVAL DMSAQVKAEK EVQDHLFTLQ RAADAAQAIT WHLTLDGMMQ ELAEQARGVI
     GAHQAVVSLA AERKGGPGAH ALSLSGEYAQ YRDQPLLTHG FGIYAKGCHG TRPVRMAQTE
     LQEHADWCRV GNHADRERML NGWLAVPLTG RDGQPIGLLQ LSDKYEGEFI QQDEYVATEL
     AQLASIAIVN VRLLHEVSQL NTGLEKKVAE RTLALARQEA LFRALAEQAP QVIWTLDPNG
     DATYFNQAWF DLVGGSLRDW SGKQWFGAVH PDDLPDTKAN WQLAQANQHS FSGLRRLLCK
     DGSVHTMAYR ASPVRGEKGV AAFWVGIDAD VTEIKHIEAA LRLSNQELEA FSYSVSHDLR
     APLSTINGFG SLLAKQLAGD GNDKMRHYVS RIQQGVAQMG QLIEDLLSLA QVARTQVRNE
     PVDLSEMALG ILDAWRARQP EREVNVQIEN DLQAYGDKPL LRVVMENLLG NAWKFSAHQP
     QATISVGQQV DAAGLPVFFV RDNGAGFDMA HAEKLFLPFE RLHAASEFAG TGVGLATVSR
     VINRHGGKLW AEAAPGLGAT FFFTLHG
//