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Database: UniProt
Entry: K9WHI6_9CYAN
LinkDB: K9WHI6_9CYAN
Original site: K9WHI6_9CYAN 
ID   K9WHI6_9CYAN            Unreviewed;       785 AA.
AC   K9WHI6;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 60.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=Mic7113_3930 {ECO:0000313|EMBL:AFZ19638.1};
OS   Allocoleopsis franciscana PCC 7113.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC   Coleofasciculaceae; Allocoleopsis; Allocoleopsis franciscana.
OX   NCBI_TaxID=1173027 {ECO:0000313|EMBL:AFZ19638.1, ECO:0000313|Proteomes:UP000010471};
RN   [1] {ECO:0000313|EMBL:AFZ19638.1, ECO:0000313|Proteomes:UP000010471}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7113 {ECO:0000313|EMBL:AFZ19638.1,
RC   ECO:0000313|Proteomes:UP000010471};
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., Chen A., Kyrpides N.,
RA   Mavromatis K., Markowitz V., Szeto E., Ivanova N., Pagani I., Pati A.,
RA   Goodwin L., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T., Kerfeld C.A.;
RT   "Finished chromosome of genome of Microcoleus sp. PCC 7113.";
RL   Submitted (JUN-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};
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DR   EMBL; CP003630; AFZ19638.1; -; Genomic_DNA.
DR   RefSeq; WP_015183777.1; NC_019738.1.
DR   AlphaFoldDB; K9WHI6; -.
DR   STRING; 1173027.Mic7113_3930; -.
DR   KEGG; mic:Mic7113_3930; -.
DR   PATRIC; fig|1173027.3.peg.4327; -.
DR   eggNOG; COG0745; Bacteria.
DR   eggNOG; COG2205; Bacteria.
DR   eggNOG; COG5002; Bacteria.
DR   HOGENOM; CLU_000445_114_15_3; -.
DR   OrthoDB; 9790669at2; -.
DR   Proteomes; UP000010471; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; 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; -; 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; 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; 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; 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; PF00989; PAS; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 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; SSF55781; GAF domain-like; 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   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000010471};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          80..125
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          153..205
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          411..635
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          659..777
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          42..69
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          199..228
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         708
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   785 AA;  88531 MW;  221876C4839E4FDE CRC64;
     MNLDELTPKI EQWFSRVTEL LQQKEVVTDT PSPSPEEQRQ LLREACEELH IALEELSIAQ
     AELLQQNQEL IFTREAVEVQ RQRYVELFDL APDAYLVTDV NGKIQEANRA AASMLNIESR
     FLVGKPLSIY ITQSERQRFY ALLIQLAQVD RVQEWEVSLQ PRYDKVLNAA LTVTPVREPG
     GKVMALRWLL RNITERKQME RQQRLLIREQ AAREAAEAQA EQSAFLAEAS HLLASCLDYP
     TTLNQVAQLA VPTRADWCFI DLVENNPTLF NQPVVAATDA EQKSRILERR ENELLPFEGD
     YGVARVLETG EPELITDIPD AFLVSIARDA THLELLRQFN AKSYMIVPLI AREQTLGTMV
     FVSSKPQRRY SRIDLMMAVE LAQRCAIAMD NARLYQEALQ ANRIKDEFLA IVSHELRTPL
     NAILGWVTIL RNRTVNAVTT HRALETIERN AKSQKKLIGD ILDISRIIRG KIRINTYPVH
     LDYIIGAVVE NVRPTAELKE IQIESMLDPS VGSVMGDLER LQQIVWNLLS NAVKFTPQGG
     RIEVRLEQGT GDPWGCPYAQ ISVRDTGKGI RPEFLPYVFE YFRQADGTTT RPYGGLGLGL
     AIVRQLVEMH NGVVYAKSEG EGKGATFIVQ LPMIDSQQKQ PPQKYRVLLD NFPALDGLRV
     VVVDDCTDTL ELIAFILEQC RAQVQTATSV EEAIQAIAQL KPDILISDIS MPDEDGYSLI
     RQVRTLEVDQ GKPILAVALT AFVREEDRTR TLDAGFQMHL PKPIEPIELV AVVANLTGRS
     QSSDA
//
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