ID K9W745_9CYAN Unreviewed; 631 AA.
AC K9W745;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=Mic7113_0265 {ECO:0000313|EMBL:AFZ16195.1};
OS Allocoleopsis franciscana PCC 7113.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Coleofasciculales;
OC Coleofasciculaceae; Allocoleopsis; Allocoleopsis franciscana.
OX NCBI_TaxID=1173027 {ECO:0000313|EMBL:AFZ16195.1, ECO:0000313|Proteomes:UP000010471};
RN [1] {ECO:0000313|EMBL:AFZ16195.1, ECO:0000313|Proteomes:UP000010471}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7113 {ECO:0000313|EMBL:AFZ16195.1,
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; AFZ16195.1; -; Genomic_DNA.
DR RefSeq; WP_015180359.1; NC_019738.1.
DR AlphaFoldDB; K9W745; -.
DR STRING; 1173027.Mic7113_0265; -.
DR KEGG; mic:Mic7113_0265; -.
DR PATRIC; fig|1173027.3.peg.289; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_51_3; -.
DR OrthoDB; 9788063at2; -.
DR Proteomes; UP000010471; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 1.
DR CDD; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 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; 1.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 1.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF13426; PAS_9; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 1.
DR SMART; SM00091; PAS; 1.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 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; PS50007; PIPLC_X_DOMAIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AFZ16195.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000010471};
KW Transferase {ECO:0000313|EMBL:AFZ16195.1}.
FT DOMAIN 7..124
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 133..205
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 206..258
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 271..493
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 512..628
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 59
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 563
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 631 AA; 70272 MW; 2921036553B0F97A CRC64;
MDNHPVRILL VDDDEDDYIL TRDLLSESQG TRFEVEWASD WDCALDVMGK NQHDIYLLDY
RLGEHNGLEL LQQAVAQGCR APMILLTGQG DREIDIEAMK AGAADYLDKS QLRAPLLERS
IRYAIERKRA EQKIREQAAL LDIATDAILV QNLQNQILFW NQGAQRMYGW KAEEVLGRDA
NQLLCTPENC LRLKEVQTLV ALEGNWYGEL QQVTQDGKAI IVESRWTLVQ NEQEQPTSIL
IVNTDITEKK QLEAQFLRAQ RMESIGTLAS GIAHDLNNVL APILMSVQLL ALKLHDEQAR
QWLKILEDNA RRGAELVKQV VSFARGVKGD RTLVQVRHII SEIRQIAKET FPKSIEVHTD
LAPDLWTVSA DATQLHQVLM NLCVNARDAL PDGGTLGISA QNLFLNEQSA RMNIDAKAGS
YIVITISDTG TGIPPEILDR IFEPFFTTKE VGKGTGLGLS TVIGIVKSHG GFVNVVSKLG
QGTEFEVYLP ALKETPIPIS EDAEMPRGHG EVILVVDDEA AIRQITQTSL ETYAYKVLTA
SDGIEALAVY AQHKEDINVV LIDMMMPVMD GPTTIRTLRR MNPQGKIVAV TGLVSDEKLA
QARDLGVQTF LYKPYTAKEL LKTLNAVLRS P
//
