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Database: UniProt
Entry: K9VNF8_9CYAN
LinkDB: K9VNF8_9CYAN
Original site: K9VNF8_9CYAN 
ID   K9VNF8_9CYAN            Unreviewed;      2163 AA.
AC   K9VNF8;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 63.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=Osc7112_4472 {ECO:0000313|EMBL:AFZ08770.1};
OS   Oscillatoria nigro-viridis PCC 7112.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Oscillatoriales; Oscillatoriaceae; Oscillatoria.
OX   NCBI_TaxID=179408 {ECO:0000313|EMBL:AFZ08770.1, ECO:0000313|Proteomes:UP000010478};
RN   [1] {ECO:0000313|EMBL:AFZ08770.1, ECO:0000313|Proteomes:UP000010478}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7112 {ECO:0000313|EMBL:AFZ08770.1,
RC   ECO:0000313|Proteomes:UP000010478};
RG   US DOE Joint Genome Institute;
RA   Gugger M., Coursin T., Rippka R., Tandeau De Marsac N., Huntemann M.,
RA   Wei C.-L., Han J., Detter J.C., Han C., Tapia R., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA   Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA   Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished chromosome of genome of Oscillatoria sp. PCC 7112.";
RL   Submitted (MAY-2012) 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   -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC       family. {ECO:0000256|ARBA:ARBA00006402}.
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DR   EMBL; CP003614; AFZ08770.1; -; Genomic_DNA.
DR   RefSeq; WP_015178010.1; NC_019729.1.
DR   STRING; 179408.Osc7112_4472; -.
DR   KEGG; oni:Osc7112_4472; -.
DR   PATRIC; fig|179408.3.peg.5553; -.
DR   eggNOG; COG0745; Bacteria.
DR   eggNOG; COG0784; Bacteria.
DR   eggNOG; COG2202; Bacteria.
DR   eggNOG; COG2203; Bacteria.
DR   eggNOG; COG2205; Bacteria.
DR   HOGENOM; CLU_000445_114_65_3; -.
DR   OrthoDB; 433983at2; -.
DR   Proteomes; UP000010478; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 8.
DR   CDD; cd00156; REC; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 2.
DR   Gene3D; 3.40.50.2300; -; 2.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 9.
DR   InterPro; IPR011006; CheY-like_superfamily.
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; IPR013656; PAS_4.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR016132; Phyto_chromo_attachment.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 8.
DR   PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR   PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 4.
DR   Pfam; PF08448; PAS_4; 2.
DR   Pfam; PF13426; PAS_9; 2.
DR   Pfam; PF00072; Response_reg; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 2.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 8.
DR   SMART; SM00091; PAS; 9.
DR   SMART; SM00448; REC; 2.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 2.
DR   SUPFAM; SSF55781; GAF domain-like; 2.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 9.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 5.
DR   PROSITE; PS50112; PAS; 7.
DR   PROSITE; PS50046; PHYTOCHROME_2; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AFZ08770.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000010478};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          15..137
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          185..228
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          232..284
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          285..355
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          356..408
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          553..602
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          770..811
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          892..966
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          971..1024
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          1195..1267
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          1271..1323
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          1320..1362
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          1391..1443
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          1463..1599
FT                   /note="Phytochrome chromophore attachment site"
FT                   /evidence="ECO:0000259|PROSITE:PS50046"
FT   DOMAIN          1647..1924
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1949..2065
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         72
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   MOD_RES         1998
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   2163 AA;  244352 MW;  35C4EA4CCA2D5299 CRC64;
     MISVLSPPAK RNGFKVLLVE DNQAEAELIE ELLLETNVSR AEPQRLSVSC TDRLSKAQQL
     LVCEHFDVIL LDLSLPDSQD LNTIVKIQEY SLNTPIVVLT ARNDEELAVQ SIQAGAQDYL
     VKRKIDSEVL IRSLRYAVER QHNQEALRKS EEKYRSVVEN SLVGIAILAP PISPSAPEKY
     EWLEVNDALC DLLGYDRQDF LHENWERWSF PEDLQASLEQ LNKILAGESE GYVLDQRWRR
     KDGNIVYTRV YLRCMRARDG AIDHLIKVVL DVSDSYRYEA QLKASEEFLN HTINSIPDPI
     FVKDEQHRWI VLNDAFCNLI GKRRSELIGK SGYDFLPPAQ AAFFWEQDEQ VLQRSLSQET
     EEIFTDGGKE RIISTKKTVF NNADSRKMLV GTMRDVSEYK HQQIALQESE ARFQVMTDNV
     PGMIYQYRLY VDGKTSFTYV SSGSWQIYNL KPEEIEENAT LAFATVHPDD ISDLQRSIAT
     SAATQQAWQH QWRQVMGDRV KWLQGASKPE MQANGDIVWD GLVMDVTELK QTQQDRDRFF
     NLSLDLLCIA GFDGYFKRLN PAWSNVLGYS SDEILAKPLI ELVHPEDLEI TVAELEKLKK
     SYPVISLENR YLCQDGTYKW LSWTASPFAE EGLIYAVARD VTFSKQAEAE LRKSEATNRA
     LLNAIPDMIF RCRADGTFVD FKPAKNFENI LPQKALIGKK AQDILPAAFA EKILSGHQQA
     IATGEIQVVE YQMPVNDELY DFEARIVFCT DDEIIAIVRD ITNRKRFESK LHRQAAAMAA
     ASEGIAIIDT DGLLIYCNAA RLKIYGYDSL EEVLGKSWKV FYEGAELQRF EQEFVPVLVQ
     EGSYMTEAVG CRRDGSKVPL DVSLTMLADG EIICVVRDIS QRKQAEAALR ESQRFIQQIA
     GASPNILYVC DLIEKKNIYG NASIYHILGY TVEEIQAMEP WMMSTLIHPE DSIKMPDYLQ
     QVETGSEGDI FEIEYRIRHK DGSWRWMVSR DTVFAKTADG KLKQILGTAT DITESKQAED
     EIKLLLAATQ AISQSADFYS ALPDILRLLC NAIGWNFAEA WIPTANGTFL EHSETWYASD
     RDLDRFGRES KKIRFAAGVA VPGRIWSTRN VEWIEDISLA KNHLFARAQM AASVGLKGCF
     GVPIHANSEV LAVLVFCKRE RSTMEPRIVE LVKAVATQLG DHIQRKQAEE ELRKSEERWQ
     LVLKGNQDGI WDLNLQTNEA FRSARWQEII GYTDGEIDST NSAWIDRIHP DDRSRVQAAI
     QGYLDRQTPN YAAEYRLQCK DGSYKWVLAR AQAVWDEAGN PLRMVGSMTD ISDRKAAELA
     LQQVTQAVES TSDAIAIADL KGRSIYHNQA FIQRYGYTVE ELNDLGDMAA LYVRHKNYKQ
     IYKSLRQGRS WCGEVSLQTK SGEAVTALVR ADSIQDINGN YIGLIAVITD ITKRKESELI
     LRQKLKREQL AVAMLERIRS SLNLEEILTK SVEEVRHFLQ VDRTVIYQFN PDWSGFIAVE
     SVAENCRPIV GMEIYDPCFG AAYVSLYQDG RIRAIEDVYN AGLADCHLAL LTRLDVIANI
     VVPILQGENL WGLLIAHHCT GPRPWQQLEG ECLKQLGVQL AIAIQQSMLF EQAQTEIADR
     KLAEAALQLA KEAAESANRA KSDFLANMSH ELRTPLNGIL GYIQLLKADK NFTADQQESL
     NNINQCGNHL LMLINDVLDL SKIEASKMDL SLTNVNFSSF VKSIIDLFQM RSAQKGIAFN
     YEQVSALPDG ILADEKRLRQ VLINLLSNAV KFTNSGSVTF KVGYAENFAD NSPQTNCENS
     SLTAEIATQT LNLTANLDAP LLSLPPLGTT EAREVITAAN TCDRPPTPKI RFQIEDTGIG
     IGQNKLEEIF LPFHQVGDHN NFVEGTGLGL SISQKLVKMM GSQIRVQSTS GKGSIFWVDL
     DLPAVAHCSE LPSRPEKRRL VGFTGPQRKV LIVDDHEVNR AMLHRLLFHL GFEIAEATDG
     EDCLHKAQEF LPDIILMDLL MPVMNGWEAT RRLRQLPELK DTVILALSAN VYETTKQESI
     LAGCDNFLTK PIQTNELLEL LRLHLRLEWV YEERSQTKKR REPTAKASSE IAAADSRMVS
     PASESVLALL RLAAMGDIEA ILEETAKLEH SDPTLVPFVH HLRQLAKGFQ LKQIRDFLKQ
     HLS
//
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