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Database: UniProt
Entry: B3QSA2_CHLT3
LinkDB: B3QSA2_CHLT3
Original site: B3QSA2_CHLT3 
ID   B3QSA2_CHLT3            Unreviewed;      1332 AA.
AC   B3QSA2;
DT   02-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   02-SEP-2008, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Ctha_0021 {ECO:0000313|EMBL:ACF12493.1};
OS   Chloroherpeton thalassium (strain ATCC 35110 / GB-78).
OC   Bacteria; Chlorobiota; Chlorobiia; Chlorobiales; Chloroherpetonaceae;
OC   Chloroherpeton.
OX   NCBI_TaxID=517418 {ECO:0000313|EMBL:ACF12493.1, ECO:0000313|Proteomes:UP000001208};
RN   [1] {ECO:0000313|EMBL:ACF12493.1, ECO:0000313|Proteomes:UP000001208}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35110 / GB-78 {ECO:0000313|Proteomes:UP000001208};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA   Hauser L., Kyrpides N., Mikhailova N., Liu Z., Li T., Zhao F., Overmann J.,
RA   Bryant D.A., Richardson P.;
RT   "Complete sequence of Chloroherpeton thalassium ATCC 35110.";
RL   Submitted (JUN-2008) 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; CP001100; ACF12493.1; -; Genomic_DNA.
DR   RefSeq; WP_012498577.1; NC_011026.1.
DR   STRING; 517418.Ctha_0021; -.
DR   KEGG; cts:Ctha_0021; -.
DR   eggNOG; COG2202; Bacteria.
DR   eggNOG; COG2203; Bacteria.
DR   eggNOG; COG3887; Bacteria.
DR   eggNOG; COG4251; Bacteria.
DR   HOGENOM; CLU_256762_0_0_10; -.
DR   OrthoDB; 9808408at2; -.
DR   Proteomes; UP000001208; Chromosome.
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; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 4.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 2.10.70.100; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 7.
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; IPR013767; PAS_fold.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 4.
DR   PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR   Pfam; PF01590; GAF; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 2.
DR   Pfam; PF08447; PAS_3; 3.
DR   Pfam; PF13426; PAS_9; 2.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 5.
DR   SMART; SM00091; PAS; 6.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 7.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 5.
DR   PROSITE; PS50112; PAS; 4.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:ACF12493.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001208};
KW   Transferase {ECO:0000313|EMBL:ACF12493.1}.
FT   DOMAIN          60..108
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          340..411
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          414..467
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          545..598
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          792..844
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          845..909
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          916..968
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          969..1035
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          1040..1092
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          1117..1328
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          1..43
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        21..35
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1332 AA;  152314 MW;  4AD616D4BEC5020C CRC64;
     MTQKDIASKT EPAELNHKIS TGEAAAQSQK SSRAQNSHLE HNEPEEIITI HVKNLTDLSI
     TSISERFQTL LGYSKEALLA QEVSFRSLLE PNDVAQFNRD LQHLACGEKK PDGIFCSPFQ
     LRHVNGASVF LHAIVRPEPS SEELAIHLFR YPMAEKVAQQ KSELLKAAAN ANRELLTNQD
     FRSALLKSLQ ILGESTHVDR IYLFENHICQ ETGVLLTSQR YEWTLAGISQ EIHNPDLQNM
     PYLGGLAYWK ERLSSGYSVK GIVENMPDDD VREILLAQNI RSIMVVPIMI GTEFWGFIGF
     DDCTTARLWT ESEEAILVSV GASVGGAIDK ERSQKALLRS QAKYKSVVEN IEEVIFQVDR
     EGKCEFINEA WERITGYKPQ KECLGKNLFD FFGNEKNPHF KEIGQGILEG KIPRFYETMQ
     LKTCDGSLRW VELMLLPRCD EPGNIIGLFG TMMDSTKQVQ ALESLKNSER IYRRISQLIS
     DYAYRLIPLE NGEFDFKWLM VGGFYSNLGF LPNEVSEKAW FEFIYPDDRH ILDLRDACLR
     KGEPVTIQLR VETQEGDLIW LEDAASPFLN HETGEIEEII CVISDITMRK RAEKEIRQAH
     DNLKVIMRTA PFGVVVVGQD QRIRWTNETV KRMARLKETD SLVGRSCSDY FCNGEKNLCP
     ILKYGISDSK CENRFQDIHI LKTVNEIVFE GEDVFLETFV DITELKNAQK ALEENQQRFS
     IAADSAGIGV WELDLVTGGM IWDEWMFKLY QKPKEAFHGN FTDWKSALAP GEFERMDPII
     QSTIASKSDN DFEMSFEIIW PSGEKRVLKT YGRALKDEAG KAVRLTGINY DITDKTKAEE
     RIRKSQEKYK AIFNTIQDVY AEVALDGTIL EISPSIKKIS GYSRQEMLGK NIYHFYSNPL
     ERENLRKELF KHGYLNDYEV KLRHLDGAVR TCSFTVSVIL DRSGQPKKIV GSMRDITDRK
     KAEENIRKSE EKYKAIFNTI QDVYAEVALD GSILEITPSI ERFTGYSREY LLGKKTSTLY
     KDPTARDRMV EELSQKGSLV DYEVVFAHKD GSSKMGSFII GLQYDLNGKP YKLVGSMRDI
     TERKKYEQDI LEKEQRYRLL AHDLQKANRE LKDFAYIVSH DLKAPLRAIG SLSSWLYSDY
     VDRLDEEGKE TLSLLVGRVK RMHDLIEGIL QYSRIGRIKE AFVEIELDLL IDEIVDFLSI
     PKHISVVKDT SLPNIIAEKT RMMQVFQNLI SNAVKYNDKE HGEISIGHVE NGETWQFYVK
     DNGPGIDEKY HEKIFQIFQT LAPRDEHEST GIGLTIVKKI IEMYGGTIAV ESTMGKGTTF
     WIELPKLLNL GA
//
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