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Database: UniProt
Entry: K9XD83_9CHRO
LinkDB: K9XD83_9CHRO
Original site: K9XD83_9CHRO 
ID   K9XD83_9CHRO            Unreviewed;      1165 AA.
AC   K9XD83;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 53.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=Glo7428_2030 {ECO:0000313|EMBL:AFZ30575.1};
OS   Gloeocapsa sp. PCC 7428.
OC   Bacteria; Cyanobacteriota; Cyanophyceae; Oscillatoriophycideae;
OC   Chroococcales; Chroococcaceae; Gloeocapsa.
OX   NCBI_TaxID=1173026 {ECO:0000313|EMBL:AFZ30575.1, ECO:0000313|Proteomes:UP000010476};
RN   [1] {ECO:0000313|EMBL:AFZ30575.1, ECO:0000313|Proteomes:UP000010476}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7428 {ECO:0000313|EMBL:AFZ30575.1,
RC   ECO:0000313|Proteomes:UP000010476};
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., Davenport K.,
RA   Daligault H., Erkkila T., Gu W., Munk A.C.C., Teshima H., Xu Y., Chain P.,
RA   Chen A., Krypides N., Mavromatis K., Markowitz V., Szeto E., Ivanova N.,
RA   Mikhailova N., Ovchinnikova G., Pagani I., Pati A., Goodwin L., Peters L.,
RA   Pitluck S., Woyke T., Kerfeld C.;
RT   "Finished chromosome of genome of Gloeocapsa sp. PCC 7428.";
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; CP003646; AFZ30575.1; -; Genomic_DNA.
DR   RefSeq; WP_015188448.1; NC_019745.1.
DR   AlphaFoldDB; K9XD83; -.
DR   STRING; 1173026.Glo7428_2030; -.
DR   KEGG; glp:Glo7428_2030; -.
DR   PATRIC; fig|1173026.3.peg.2164; -.
DR   eggNOG; COG0784; Bacteria.
DR   eggNOG; COG2202; Bacteria.
DR   eggNOG; COG2205; Bacteria.
DR   eggNOG; COG5000; Bacteria.
DR   HOGENOM; CLU_000445_114_15_3; -.
DR   OrthoDB; 5555607at2; -.
DR   Proteomes; UP000010476; 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; 5.
DR   CDD; cd17580; REC_2_DhkD-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 2.10.70.100; -; 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; 6.
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; IPR013656; PAS_4.
DR   InterPro; IPR013655; PAS_fold_3.
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; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 3.
DR   Pfam; PF08448; PAS_4; 3.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 3.
DR   SMART; SM00091; PAS; 6.
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; 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; 3.
DR   PROSITE; PS50112; PAS; 4.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:AFZ30575.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000010476};
KW   Transferase {ECO:0000313|EMBL:AFZ30575.1}.
FT   DOMAIN          35..88
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          264..333
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          392..463
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          461..517
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          594..647
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          648..718
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          721..773
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          798..1021
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1046..1161
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          240..267
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         1092
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1165 AA;  131978 MW;  59D2EB01A3AA459D CRC64;
     MQPVPSTQQN QASEQDSVVV DTAIFFELST GLLCVVSWDG TFKKVNPAFS KTLGFANGEL
     LEQKFIELVH PEDRAVTKAA IAQIQTSDQR TGYFENRYLC RDSSYKELGW TVRFEAEPGL
     FYGIARELTL IKSTKDTALY RTLARNLPKA AVFLFDDNLR YELCEGQEIA SMGFNQETLE
     GKTIWDVLPP KTCTEIEPLY RATLAGQEVV TEIAFCGHAY AVQIVPVRNE QQEIVAGMML
     LENIDERKQT EEALDQSEET VQRQLKEIEA IYTSAPVGLC FLDTNLRYVR VNDRLAEING
     IPAAEHIGKS VEELLPEIGE VQAKLFAQVI QTGVPILDAE VRGTTPAQPG IERDWLVSYY
     PLRDINDRIL GINIVVQEIT QRKQQAAALA ERERQLTTIL SNTPDVICRY SKDFRYLYIS
     PAAERITGIP TQRFIGKTNA EIGMPEIYTK TWEKAIAEVL QTREQQILEF NFPLASKTWY
     FYSIFIPEFA PDGSVESVLV VSRDVTERRQ AEESLAKSQD WLQLSQQAGQ IGAFIWDIVN
     GDIVWTQQLE ILYGLTPGSF GGTYEHWQQQ VHPEDIVRIE QSLQEKMQTR GEEWQGDFRI
     FHAQTGEIRW IAAKSRFFYD NFGQPIRMIG VNLDISDRKH TEVALRESEL NYRMLADTMP
     QLFWTTLPDG YHEYYNQRWY DYTGLTLEET KGAGWNHVLH PDDQQRSWEV WHESLRTGKN
     YEIEYRFRRF DGEYRWFLGR AFPLHDDTGQ IIRWFGSCTD IHDQKIALEE RDRAVERERT
     ARSQAEAANR IKDEFLAVLS HELRSPLNPI LGWAKLLLTR QFDENTTRKA LQTIERNAQL
     QTRLIEDLLD ISRILRGKLS LNITQVNLVT IAEAALETVR LAAEEKAIHL QLIIEDSARY
     SEFQIAGDAA RLQQIVWNLL TNAVKFTPHG GRVEVKLEKL ASSSVQIQVS DTGKGIAPEF
     LPHVFDYFRQ ADSSITRKFG GLGLGLAIVR HLVELHGGTV KADSQGEGQG ATFSVTLPLP
     ESEIVDENSG DRIHYNDSDL PLLGIRALIV DDEADMRELL VVTLEQYGAQ VTAAASASEV
     LELPQYQILI SDIGMPNMDG YTLMRQIRTL PPDQGGSILA IALTAYAGET DQQAAIAAGF
     NRHLAKPVEP AKLLATIVNL LSKKS
//
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