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Database: UniProt
Entry: A0A024FIV7_9FLAO
LinkDB: A0A024FIV7_9FLAO
Original site: A0A024FIV7_9FLAO 
ID   A0A024FIV7_9FLAO        Unreviewed;       576 AA.
AC   A0A024FIV7;
DT   09-JUL-2014, integrated into UniProtKB/TrEMBL.
DT   09-JUL-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=WPG_2427 {ECO:0000313|EMBL:BAO76657.1};
OS   Winogradskyella sp. PG-2.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Winogradskyella.
OX   NCBI_TaxID=754409 {ECO:0000313|EMBL:BAO76657.1, ECO:0000313|Proteomes:UP000031636};
RN   [1] {ECO:0000313|EMBL:BAO76657.1, ECO:0000313|Proteomes:UP000031636}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PG-2 {ECO:0000313|EMBL:BAO76657.1,
RC   ECO:0000313|Proteomes:UP000031636};
RX   PubMed=24874677; DOI=10.1128/genomeA.00490-14;
RA   Kumagai Y., Yoshizawa S., Oshima K., Hattori M., Iwasaki W., Kogure K.;
RT   "Complete Genome Sequence of Winogradskyella sp. Strain PG-2, a
RT   Proteorhodopsin-Containing Marine Flavobacterium.";
RL   Genome Announc. 2:e00490-14(2014).
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; AP014583; BAO76657.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A024FIV7; -.
DR   STRING; 754409.WPG_2427; -.
DR   KEGG; win:WPG_2427; -.
DR   HOGENOM; CLU_000445_114_15_10; -.
DR   OrthoDB; 9811889at2; -.
DR   Proteomes; UP000031636; 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; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 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; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43719:SF28; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK2; 1.
DR   PANTHER; PTHR43719; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 1.
DR   SMART; SM00091; PAS; 1.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:BAO76657.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000031636};
KW   Transferase {ECO:0000313|EMBL:BAO76657.1}.
FT   DOMAIN          73..119
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          146..198
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          209..430
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          451..569
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          56..83
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         500
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   576 AA;  66333 MW;  6BCC8CC97A96A55B CRC64;
     MLDVNQHRLL LRQIRNAGFN EADILKFKKF FSVVNDAYKS FDDDVKHIEI ILEQSSNELY
     KVNQTLKSQV DNVENELNTI VNTIDDVIFK TDMQGNFKYL NKAWEDLFGV KVEEAINRNY
     RDLLFGINKK EKVRISKFLS EEHDGYETLF EFYKPSGKKI WVQLRLALTY NSNNKADGTI
     GTMSDVTQLK ETEIELNNAN KIKDEFVSTM SHEIRTPLNA VMGMSDILLM ETFLPEQLEN
     LQVLKYSSEH LLTLINDLLD LNKYKSKQIR LVEEDFNLSE LIQNIQLHFK QAALKKGLSF
     DTVLDSEMPN ILKGDSLKLS QVLKNLLSNA FKFTHEGGVS FRTEVIDKKV ENTTIRFLVE
     DSGIGVSYNK QKDIFKSFVQ ASVDTSKLYG GSGLGLYISK ELLKIQGSDL QLDSVEEEGS
     LFWFDITFKH SNTVSLKREN NKLNITPINL NVLVAEDNNL NAMLLKKLFK KWGINYIIAK
     NGQELLDVYK DRDFDIILMD LQMPVLDGYD TTRIIRKMSD SGKALIPIVA LTAFSESEVG
     DKIRRYRMNG YLSKPFKINE LHDLLNFYCK KKQQVV
//
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