ID K9XQF4_STAC7 Unreviewed; 1026 AA.
AC K9XQF4;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Sta7437_1280 {ECO:0000313|EMBL:AFZ34850.1};
OS Stanieria cyanosphaera (strain ATCC 29371 / PCC 7437).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Pleurocapsales; Dermocarpellaceae;
OC Stanieria.
OX NCBI_TaxID=111780 {ECO:0000313|EMBL:AFZ34850.1, 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}.
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DR EMBL; CP003653; AFZ34850.1; -; Genomic_DNA.
DR RefSeq; WP_015192523.1; NC_019748.1.
DR AlphaFoldDB; K9XQF4; -.
DR STRING; 111780.Sta7437_1280; -.
DR KEGG; scs:Sta7437_1280; -.
DR PATRIC; fig|111780.3.peg.1333; -.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_50_0_3; -.
DR OrthoDB; 474548at2; -.
DR Proteomes; UP000010473; Chromosome.
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; 3.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 3.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 3.
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 NCBIfam; TIGR00229; sensory_box; 3.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF01590; GAF; 2.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 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; 3.
DR SMART; SM00091; PAS; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
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); 3.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 2.
DR PROSITE; PS50112; PAS; 3.
DR PROSITE; PS50046; PHYTOCHROME_2; 1.
PE 3: Inferred from homology;
KW Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AFZ34850.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000010473};
KW Transferase {ECO:0000313|EMBL:AFZ34850.1}.
FT DOMAIN 24..165
FT /note="Phytochrome chromophore attachment site"
FT /evidence="ECO:0000259|PROSITE:PS50046"
FT DOMAIN 196..270
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 273..326
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 546..616
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 619..671
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 672..742
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 803..1020
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 317..344
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 490..549
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1026 AA; 117707 MW; 50E14C76682BBB39 CRC64;
MKIPKQEINR LLASVALGIR QSLDLEEILH KSVAEVRDFL ECDRVIIYRF YPDWSGAVIV
ESVAQSQWSI LGSRIKDPCF ENTWVEYYQQ GNVTARTDIN QITIDPCYQE LLQNFNVTAN
LVVPIIQTTS NQTIQLWGLL IAHQCQHSRE WQEVEIEFLK QLTTQIGIAI AQAELLALTK
YELRQRQLAQ QKVQQARHFL QTTIDHLPVA VFVKDASQSN FGKFLLWNKA SERMFGLRAE
QALGKTVYDY FCFSEANLLN QQDQQAFETR TVIEIPEQII TIGTLGKKIL RTTKVPIFDD
LGQPEYLLCI AEDITRRHQA EVQLQQKSEE LAAFSSNLKQ LHRLNTTNYA TFDQLFHDYV
QTGCRIFGCS TGIVSHIEGD IYTIYAVTSD LTSLSPNQQF ELGNTYCAEV VKQKKTIAYH
CVGTIEELRS HPVYQNFKLE TYIGTPIFVE QAIYGTLNFS STKIRNLPFT SHEREIIEMM
AQSIGKFINA HQIELQRQQA VVELQQAKQE LEDRVKQRTE ELSQTNQRLQ QELYQRQQAQ
VALEESEARF RSMVNSFPML VWVSGSDSHS TFFNQAWLEF TGRTMAEELA HGWSEGVHPD
DQSQYFNTYQ TAFNNRQPFQ LEYRLKRADG EYRWMLDYGA PRFRPDGSFA GFIGSCLDIS
DRKQIEATLQ ESEKRWRTLL ENVRLLVIGM DLQGRLDYAN PFFLELMGYT VTEAIGKHFI
DLVHPQNRQE AVKIFQSIIQ PNSPYYYHHQ KILLTKSGEE KRISWNSTQM CDLQGKPIGM
MCIGEDITAR HAMERMKDEF ISVVSHELRT PLTSIHGALG LLVSGIVQPQ SEQGQRIIKI
AAESTESLVR LVNDILELER LESGKIDLIK KIVQVQEIML KAIELVQLIA NRAGIILEVT
NQNLEFYGDC DRIVQVLTNL LTNAIKFSER GSRVWLDVVQ QSDQILFVVQ DQGRGIPSDK
LETIFERFHQ VDASDSRRKG GTGLGLAICR NIVEQHGGKI WAESIYGKGS NFFFTIPLVK
ADEINN
//
