ID K9XWY9_STAC7 Unreviewed; 1481 AA.
AC K9XWY9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 57.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Sta7437_3065 {ECO:0000313|EMBL:AFZ36579.1};
OS Stanieria cyanosphaera (strain ATCC 29371 / PCC 7437).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Dermocarpellaceae;
OC Stanieria.
OX NCBI_TaxID=111780 {ECO:0000313|EMBL:AFZ36579.1, ECO:0000313|Proteomes:UP000010473};
RN [1] {ECO:0000313|Proteomes:UP000010473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29371 / PCC 7437 {ECO:0000313|Proteomes:UP000010473};
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 -!- SIMILARITY: In the N-terminal section; belongs to the phytochrome
CC family. {ECO:0000256|ARBA:ARBA00006402}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00169}.
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DR EMBL; CP003653; AFZ36579.1; -; Genomic_DNA.
DR RefSeq; WP_015194244.1; NC_019748.1.
DR STRING; 111780.Sta7437_3065; -.
DR KEGG; scs:Sta7437_3065; -.
DR PATRIC; fig|111780.3.peg.3186; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG2205; Bacteria.
DR eggNOG; COG3829; Bacteria.
DR HOGENOM; CLU_256762_0_0_3; -.
DR OrthoDB; 5555607at2; -.
DR Proteomes; UP000010473; 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; 4.
DR CDD; cd00156; REC; 1.
DR CDD; cd17580; REC_2_DhkD-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 1.
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; 6.
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; 5.
DR PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR Pfam; PF01590; GAF; 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; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 6.
DR SMART; SM00091; PAS; 5.
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; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 6.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 4.
DR PROSITE; PS50112; PAS; 4.
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 Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AFZ36579.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000010473};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 7..125
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 157..293
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 337..411
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 412..464
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 661..712
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 706..776
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 779..831
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 832..902
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 905..957
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 958..1030
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 1107..1332
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1354..1472
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 1067..1100
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1403
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1481 AA; 167841 MW; 547FC6EC6373025A CRC64;
MVQIPRTILI VDDASEARKY RRYLVENRAY SYTVLEASRG QQGLELWQQH QPDLILLNAQ
LPDLNGLEFL ARLQSLIQQT CLPVIMMSKP SQEAIALQAL KAGAQDYLVK EQITPARLDH
SINRVIETAQ LRSELQRRIE KEQLIAQITL KIAQTFNLNE ILQTTVTEVR RFLQSDRSLI
FRLDLDGWGE VITESVADQW TSLLSTSLSA SCLSENYLES FHQGLVTVQS DLHDGRIAPA
QVELLANLQV RANLVAPIVV GERLWGMLIV HHCAAPRQWQ RLEVDLVQEL AIELGIALQQ
SELAQKVESE RLERQKVELK LRESLKNTQL AEIWRESAAQ FRQLAENIDA VFWIREELEQ
RVSYVSPAYE RLWGLDPQEL YKNPLVWGNY IHPDDREAIA FAFQEKAAKG EFDQEYRIIL
PDGSIRWIRD RCFPLQDETG KIYRFTGIAE DITKRKQAEL ERQRSEATLQ GFLAASPIAL
VLFDRELRFL YANEALARLN ELPLSEHLGR TLAEVMPLMA SKFAPMLLEI MATQEPVFNL
EFSGEIRPGV FRSTIANYYP VCLANGEVIG VGVSVTDTTE LRQTEIALQQ TTERLNVALK
SAPLTLFNQD LELRYTWIYN PTHNYSIAEV IGKRDEDLAS PDTAASLTQL KQQVLATGIG
LREEVKVTRN EQTTYYDLTI DPIKARHNAI VGITCAAVDI TERKEFEEHL RYTIELNPQV
PWTANPAGDI TDLSERWLEL TGLTREQSLG KGWMQVIHPD DLSAVVAAWT NSFKTGVAYD
IEYRIKLTDD SYCWVRSRAF PRRSEHNEIV RWYGTTEDID DRKKSEEALR ISEEQFRTIA
NAAPALVWVC SVTGEIVFMN ERWYEYTGQS QEEVKGFGWT STLHPDDTER ILSHWQHCYT
TGEPYEGEGR YRQKNGEYRW HRFRALPQRN ELGIIEKWFG CSVDIHDAKR AEEVIAANEA
KLRGFVDANV VGMLYGDIYG NIYEANDKLL KIVGYTREEL RAGKLRWIDI TPPEYLPLDQ
QAIAEALLKG ACTPYEKEYL RPDGSRVPIL LGYSLVGEAR EESVAFILDL SERKQAEQER
EQLLQREQSA RQEAERANRI KDEFLAILSH ELRSPLNPIL GWAQMLQTGR LDSIKTTEGL
ATIERNAKLQ TQLIDDLLDV AKILRGKLSM KMASVNLALV IEAAIGTVRA AALAKSIHLE
VKLPQIGQVF GDAARLQQII WNLLSNAIKF TPNHGRVDIQ LSLVVSQSST IKAKYAKIIV
SDTGKGIKPE FLPYIFESFR QEDASTTRKY GGLGLGLAIV RYLVEAHGGT IWADSKGDGQ
GATFTVRLPL LNSKPILNQS ETLSTQELDL TGIRILTVDD EPDARNLLTV LLTQYGAEVL
SVASTTEVLA NLESFQPDLL ISDIGMPNLD GYSLIEQVRA LPPEKGGEVN AIALTAYARE
EDRQQALSKG YQWHINKPLE PEQLIRAVIS LVSHQTQNNP D
//
