ID K8GGX6_9CYAN Unreviewed; 1076 AA.
AC K8GGX6;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=OsccyDRAFT_4860 {ECO:0000313|EMBL:EKQ67039.1};
OS Leptolyngbyaceae cyanobacterium JSC-12.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Leptolyngbyales; Leptolyngbyaceae.
OX NCBI_TaxID=864702 {ECO:0000313|EMBL:EKQ67039.1, ECO:0000313|Proteomes:UP000001332};
RN [1] {ECO:0000313|EMBL:EKQ67039.1, ECO:0000313|Proteomes:UP000001332}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JSC-12 {ECO:0000313|EMBL:EKQ67039.1,
RC ECO:0000313|Proteomes:UP000001332};
RG DOE Joint Genome Institute;
RA Brown I., Huntemann M., Wei C.-L., Han J., Detter J.C., Han C., Tapia R.,
RA Chen A., Kyrpides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L.,
RA Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RT "Improved high quality draft of Oscillatoriales sp. JSC-12.";
RL Submitted (OCT-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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKQ67039.1}.
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DR EMBL; AJUB01000019; EKQ67039.1; -; Genomic_DNA.
DR AlphaFoldDB; K8GGX6; -.
DR STRING; 864702.OsccyDRAFT_4860; -.
DR PATRIC; fig|864702.5.peg.5243; -.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG5000; Bacteria.
DR eggNOG; COG5002; Bacteria.
DR HOGENOM; CLU_000445_114_10_3; -.
DR OrthoDB; 567946at2; -.
DR Proteomes; UP000001332; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 3.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 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; IPR003660; HAMP_dom.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 4.
DR PANTHER; PTHR43047:SF72; PHOSPHOTRANSFERASE RCSD; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 2.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00304; HAMP; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 3.
DR SMART; SM00091; PAS; 4.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF158472; HAMP domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 3.
DR PROSITE; PS50112; PAS; 3.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000001332};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..40
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 229..251
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 248..301
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 310..357
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 384..434
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 435..507
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 511..563
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 691..761
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 765..817
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 821..1072
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT COILED 674..701
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1076 AA; 121466 MW; CDDEB2936294B2F1 CRC64;
MPSSRSLPRS SPKIPLHWVL VIPFVLQTVG AVGIVGWLSY RSGQKVVEQI AYQLLETVSE
QVSDRLDTLL QAQQQEIATN PQTAAQGNLS PQKLQSLRTR LNPYLSHLDF SPSSFVFIVE
PSGNLVATST LNNSLLPGGR YQPKRFASAN GQDARIHKIS QQLLDSFGSF RNFQQTTQLT
LKTSQTGEQP QFVQVTPYQG KGRLDWLIIT VVPESDFIGE IQTNLWRTVL LSFLTLMCTT
ATGVLTAFWI AKPIRQLSRA SQTLASGQWQ QSLQEDSWIT ELSVLAKSFN RTADQLQQSF
DRIKVALQAS EEKFTKVFRT SPDPITIMTL DEGRYLEVNE SFLKFSEYSQ EEVIGRTSAE
LNLSVDYQQD LALKEQLERQ GTVQNFEYYY RTKTGQVGTT LLSIERVELD GQQRILTIAK
DISDRKQTEH ALRQAIQQIN TYFEHSPLAI MEWDQTGRIL RWSTQAERVF GWTADEIQER
RWQEWEIVHE DDQDRVITEL TPLMNGLTTS HMLQNRNRTK DGRVIVCEWY SSAIFDETGN
LISVLSFAQD ITERIQMETA LQESEARNRA ILQAIPDLMI LYTAEGTYVD IIQRNLAQDA
ITDPDPVGKH ISELLPSDIA ERQINASKQV LATGEIVVYE QELWIQGTLQ YEEVRVVPCG
EETVLVIVRD ISDRKRNEIE RQLAEEALQH SEEQIRRAFE DAAIGMAIVG LDGRFLRVSH
SLCEIVGYSE TELLAMTFHE ITHPDDLLTD LGYSEQMLSG ELRTYQLEKR YIHKQGYIIW
ILVNVSLVKD NNDQPLYFVS QIQDISDRHE LDRIKNEFIS IVSHELRTPL TAIRGSLGIL
ATGVLAHEPD TAKAMLHVAL NNSERLVRLV NDILDLERLE SGKTQLVMEE CSVNNLLMQA
IESVQTLVAQ ASISLKVTSC AAKVWASPDA IVQTLTNLIG NAVKFSEPGS TVWLKAELKN
GEWEMGEEAA IEIWESQRPA VSSSTSLSSS PYSQPFILFS VADQGRGIPP EKLESIFGRF
QQVDVSDSRD KCGTGLGLAI CKSIVQQHGG KIWVTSVLNE GSTFYFTVPQ ANRKEE
//