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Database: UniProt
Entry: D8JXP8_HYPDA
LinkDB: D8JXP8_HYPDA
Original site: D8JXP8_HYPDA 
ID   D8JXP8_HYPDA            Unreviewed;       622 AA.
AC   D8JXP8;
DT   05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT   05-OCT-2010, sequence version 1.
DT   24-JAN-2024, entry version 68.
DE   RecName: Full=Blue-light-activated histidine kinase {ECO:0000256|ARBA:ARBA00021740};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Hden_3438 {ECO:0000313|EMBL:ADJ25229.1};
OS   Hyphomicrobium denitrificans (strain ATCC 51888 / DSM 1869 / NCIMB 11706 /
OS   TK 0415).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Hyphomicrobiaceae; Hyphomicrobium.
OX   NCBI_TaxID=582899 {ECO:0000313|EMBL:ADJ25229.1, ECO:0000313|Proteomes:UP000002033};
RN   [1] {ECO:0000313|Proteomes:UP000002033}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 51888 / DSM 1869 / NCIB 11706 / TK 0415
RC   {ECO:0000313|Proteomes:UP000002033};
RX   PubMed=21705585; DOI=10.1128/JB.05453-11;
RG   US DOE Joint Genome Institute;
RA   Brown P.J., Kysela D.T., Buechlein A., Hemmerich C., Brun Y.V.;
RT   "Genome sequences of eight morphologically diverse alphaproteobacteria.";
RL   J. Bacteriol. 193:4567-4568(2011).
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; CP002083; ADJ25229.1; -; Genomic_DNA.
DR   RefSeq; WP_013217388.1; NC_014313.1.
DR   AlphaFoldDB; D8JXP8; -.
DR   STRING; 582899.Hden_3438; -.
DR   KEGG; hdn:Hden_3438; -.
DR   eggNOG; COG0784; Bacteria.
DR   eggNOG; COG2203; Bacteria.
DR   eggNOG; COG3920; Bacteria.
DR   HOGENOM; CLU_000445_114_57_5; -.
DR   OMA; DERITCS; -.
DR   OrthoDB; 7185134at2; -.
DR   Proteomes; UP000002033; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0000160; P:phosphorelay signal transduction system; IEA:InterPro.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR036890; HATPase_C_sf.
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; IPR011102; Sig_transdc_His_kinase_HWE.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 2.
DR   PANTHER; PTHR41523:SF8; ETHYLENE RESPONSE SENSOR PROTEIN; 1.
DR   PANTHER; PTHR41523; TWO-COMPONENT SYSTEM SENSOR PROTEIN; 1.
DR   Pfam; PF07536; HWE_HK; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   Pfam; PF13426; PAS_9; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   SMART; SM00911; HWE_HK; 1.
DR   SMART; SM00086; PAC; 2.
DR   SMART; SM00091; PAS; 2.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW   FMN {ECO:0000256|ARBA:ARBA00022643};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ADJ25229.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000002033};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Virulence {ECO:0000256|ARBA:ARBA00023026}.
FT   DOMAIN          149..203
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          222..274
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          499..609
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         549
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   622 AA;  68581 MW;  7B6A9AB8C69B0178 CRC64;
     MKDNPVSEGI SYPNQSSDEI GGCRFENDRQ LLEAIFEASP ECIKIVAPDG RLIQMNPSGM
     RMVEAEPGAK VEGTMVLSLI APEFRDAWQA NHERVCNGER LMWTFDIIGL RGTRRRMETH
     AVPIRLLNGQ TGQLAITRDI TVRRENELKA ARLAAIVASS DDAIVSKTLD GIITSWNAGA
     EKIFGYTADE IIGQHITRII PPELHFEEEE ILARIRRGLH IDHFETVRLA KDGRRIDVSV
     TISPMRDKSD NLIGASKVGR DITERKNAEG LQKLLIGELN HRVKNTLATV QSIANQTVHR
     AKSPGDFATS FGGRLQSLAK THSLLTQSTW QGAELSELIR DQLPFGDNED ERITCSGPLV
     MLNAQAALHL SLVLHELATN AIKHGALSER RGRLSIRWMV RTETERKLVL QWQERGGPTV
     TVPQSRGFGT TLIEKSLEAH GGVTSIRYEA DGLTCDIILP LPDTETGIGG SYHRPLTEGP
     QAVKGLKSSQ QLNTVAGKRI LVVDDEPLIA MDMVASLEDE GCEIVGPATT LQKALTLVET
     EDIDAALLDA NLAGDPVDEL AAVLVRRGIP FAFVSGYGRE GLPQAYQQMA LIRKPFQRQR
     LIDVVREMVV QDNIVVPFRK TT
//
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