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
//