ID K9ZAU6_CYAAP Unreviewed; 1472 AA.
AC K9ZAU6;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 65.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Cyan10605_3477 {ECO:0000313|EMBL:AFZ55513.1};
OS Cyanobacterium aponinum (strain PCC 10605).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC Chroococcales; Geminocystaceae; Cyanobacterium.
OX NCBI_TaxID=755178 {ECO:0000313|EMBL:AFZ55513.1, ECO:0000313|Proteomes:UP000010480};
RN [1] {ECO:0000313|Proteomes:UP000010480}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 10605 {ECO:0000313|Proteomes:UP000010480};
RX PubMed=23277585; DOI=10.1073/pnas.1217107110;
RA Shih P.M., Wu D., Latifi A., Axen S.D., Fewer D.P., Talla E., Calteau A.,
RA Cai F., Tandeau de Marsac N., Rippka R., Herdman M., Sivonen K.,
RA Coursin T., Laurent T., Goodwin L., Nolan M., Davenport K.W., Han C.S.,
RA Rubin E.M., Eisen J.A., Woyke T., Gugger M., Kerfeld C.A.;
RT "Improving the coverage of the cyanobacterial phylum using diversity-driven
RT genome sequencing.";
RL Proc. Natl. Acad. Sci. U.S.A. 110:1053-1058(2013).
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 -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP003947; AFZ55513.1; -; Genomic_DNA.
DR RefSeq; WP_015221231.1; NC_019776.1.
DR STRING; 755178.Cyan10605_3477; -.
DR KEGG; can:Cyan10605_3477; -.
DR PATRIC; fig|755178.3.peg.3703; -.
DR eggNOG; COG0517; Bacteria.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_250123_0_0_3; -.
DR OrthoDB; 415806at2; -.
DR Proteomes; UP000010480; 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; 5.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 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; 5.
DR InterPro; IPR046342; CBS_dom_sf.
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; IPR013656; PAS_4.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 4.
DR PANTHER; PTHR43047:SF79; HISTIDINE KINASE; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF08447; PAS_3; 3.
DR Pfam; PF08448; PAS_4; 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; 5.
DR SMART; SM00091; PAS; 5.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF54631; CBS-domain pair; 1.
DR SUPFAM; SSF52172; CheY-like; 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); 5.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 5.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AFZ55513.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000010480};
KW Transferase {ECO:0000313|EMBL:AFZ55513.1}.
FT DOMAIN 389..464
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 467..519
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 602..654
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 735..786
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 787..857
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 859..911
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 986..1038
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 1063..1297
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1355..1471
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 1029..1056
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1404
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1472 AA; 169407 MW; C485DCE95F6F9002 CRC64;
MSSFSFSLEY QPPYFPVTFI SADESFSRVL SLSEEHPHNS IFFIVQKEEK ESSSCRKYLG
ILARKNLSKY TQDSEDNDSL KAENLDLLPI VSIKKSELTN LFIVLYKFIS SGSDYLAIIN
DNSDIIGVLA HEDLRDYIEI HTNFNYQEIE KLVSELNITI TEDISEKKAD KKQGKIFIKN
NNKDSQVKTK NNSDTILHLD KIIDEHREQE RYWHKLIEGA AAISGKDFFN KIAEYISINF
DVDYVFITEK KEQYLETLVF LVNGKIQNNF CFPCTNFPCG KAVQEGIFTC QNNLRSLFPN
NEFLEKSEME GFAGVQLING NKEVIGGLSV GSKSFIPKIK LEMIADILQV FAARITSELE
REKAVTELTN LQQQLKNEII IKTTQLEINE RKYRTLIENF PGIVYSCLND NFWTMEFLSG
EILNITGYYP EEVTGNKLIS YADLIHPDDR DIVNELIQES LQKKEIFTVE YRLQHRDGHI
RWVYEKGQGV YDFQGNLIHL CGAIIDVSDR KLAEEALKHS EKDLFNAKEM LELVLNTIPQ
RVFWKNTQSV LLGCNQAFAN DFDSTVSELQ GKQINEICFN SEDAHQYQQC DCEVINTREP
IYHQQYTYHR RDGSTMYIEG SKFPLKNNEG EIIGILGTYQ DITQRKEYEA KLAQENNFNQ
QILENMAEGL CVCSEISDFP YIRFSVWNHK MEEITGYTLE EINQKGWYQS LYPDPNLREK
AIERMKRMRQ GEHIHKEIWR IIRADSQPRL IQISTCIVQK MDNSTHILAL MQDVTEQKRA
EKALKQSESR YRKIVETANE GIWILNKKGI TTFVNRTLAD MLGYSAEDIR GKSFLSFMED
SEKVFAQQLF ERRIQGVSEQ HDFKFLRADG STLWAILSTS PIFNDEGEFI GALGMITDIS
DRKLIESHIN ELSKRLKLAV ESAQIGIWEL DLKTQKLTWD EQMYKLYDVP IGTPCYYKTW
TNALHPEDFE DTVNLFERAS LDLAEYDTVF RVIHSDGKII YIKANGMLEK DEEGKPLKMI
GINYDITPQK EAEIVLKESN ENLEKINLEL EKTTRMKDEF LASMSHELRT PLNSILGLSE
ALKEQVFGTL NQKQLDSLNN IHRSGRHLLD LINDILDLAK IESGKTEFNF SLVDVVSLSL
DSLNFIRYLA EKKNITLTFI NEIPSSHKLC QIDDRRIRQA LINLLNNGIK FTPEGGKIKL
KINLVTKINS TYQELETGET FIHFSVTDTG IGIAEENISK LFQTFVQIDS RLNRQYAGTG
LGLALVKRIV DAHGGFVGVE SEINQGSCFS FYIPYSKDVK EYHSAFWHPK NPHRVNLFTK
KKIKENDESL LYNGRLEFSS NNSEQKTAIN SINNLILLVD DNEENIYAVS DYLKIKGFSL
EIAKNGKDAL NKLEEVNPCI ILMDIQMPEL DGFETIRLIK ENPRWQNIPI IAVTALAMTG
DKEKCLNAGA DDYLSKPFRL KDLIEKINKV LS
//
