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Database: UniProt
Entry: G0L288_ZOBGA
LinkDB: G0L288_ZOBGA
Original site: G0L288_ZOBGA 
ID   G0L288_ZOBGA            Unreviewed;      1092 AA.
AC   G0L288;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 67.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=zobellia_3844 {ECO:0000313|EMBL:CAZ97982.1};
OS   Zobellia galactanivorans (strain DSM 12802 / CCUG 47099 / CIP 106680 /
OS   NCIMB 13871 / Dsij).
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC   Flavobacteriaceae; Zobellia.
OX   NCBI_TaxID=63186 {ECO:0000313|EMBL:CAZ97982.1, ECO:0000313|Proteomes:UP000008898};
RN   [1] {ECO:0000313|Proteomes:UP000008898}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij
RC   {ECO:0000313|Proteomes:UP000008898};
RG   Genoscope - CEA;
RT   "Complete genome sequence of Zobellia galactanivorans Dsij.";
RL   Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CAZ97982.1, ECO:0000313|Proteomes:UP000008898}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 12802 / CCUG 47099 / CIP 106680 / NCIMB 13871 / Dsij
RC   {ECO:0000313|Proteomes:UP000008898};
RX   PubMed=22513138; DOI=10.1111/j.1462-2920.2012.02751.x;
RA   Thomas F., Barbeyron T., Tonon T., Genicot S., Czjzek M., Michel G.;
RT   "Characterization of the first alginolytic operons in a marine bacterium:
RT   from their emergence in marine Flavobacteriia to their independent
RT   transfers to marine Proteobacteria and human gut Bacteroides.";
RL   Environ. Microbiol. 14:2379-2394(2012).
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; FP476056; CAZ97982.1; -; Genomic_DNA.
DR   RefSeq; WP_013995172.1; NC_015844.1.
DR   AlphaFoldDB; G0L288; -.
DR   STRING; 63186.ZOBELLIA_3844; -.
DR   KEGG; zga:ZOBELLIA_3844; -.
DR   HOGENOM; CLU_000445_114_18_10; -.
DR   OMA; TEAWGYV; -.
DR   OrthoDB; 9808408at2; -.
DR   Proteomes; UP000008898; Chromosome.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
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; 5.
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; IPR013656; PAS_4.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   NCBIfam; TIGR00229; sensory_box; 3.
DR   PANTHER; PTHR43711:SF26; SENSOR HISTIDINE KINASE RCSC; 1.
DR   PANTHER; PTHR43711; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF08448; PAS_4; 1.
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; 3.
DR   SMART; SM00091; PAS; 5.
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); 4.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 3.
DR   PROSITE; PS50112; PAS; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Kinase {ECO:0000313|EMBL:CAZ97982.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008898};
KW   Transferase {ECO:0000313|EMBL:CAZ97982.1}.
FT   DOMAIN          7..58
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          210..262
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          385..452
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          453..507
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          797..849
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          867..1083
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          61..86
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          671..702
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1092 AA;  123950 MW;  5F87ECB39ECEB97D CRC64;
     MVEKLKDNDL FKGIFESSVE GIIVVDYKGR IFRANPSVEK MFGYGPGELA HKTVEDLVPG
     QYGKSHQNHR KNFAKKPTSR PMGKGGNLWA LRKDGSQFPV EISLSPTQIN DENVVVAFVI
     DITDRLLAEK KAAVSAEKMN EAQSLAHIGS WVWNLRTNER NWSDEFYRIC GLPPGDKRLN
     VDTVLQFIHP DDRQATIDDI AYAIENKTSY SNNKRMVRTD GSIRYITARG KASYDNEGKP
     LEWFGTIQDV TEQKATEQQL EENLTKNKAL LEALPDMMFI LDYEGEFLDY YVPEPEKLFA
     PASSIIGGHI KELLPPHICQ AIRDGIDKTI KTNEIQFVEY NFDGEKGRQF YEGRIVPMDK
     NRLLTIIRDI TNERAIENIL YVRNQALAAT ANGIIICDAR EPDHPIIYAN EAFCKTTGYD
     EDDFMGKNCR FLQREDKDQF EIKLMSEAIR NGEDCRVVLR NYRKDGSLFW NEVSITPIYN
     EEKVLTHFVG VHNDVTAHKV EEFFKIGQSH VMDMIIQHEP LEHIAYKIVE TIETAIPNCH
     GSILLLDKET GSLRQLAAPN VPKSFTDAIE GMQIGAENGS CGAAAYLKKE IIVSDTSSDP
     LWSAFRELAE EANLKACWSF PIFSSNQELL GTFAIYFNVS RIPLDTEKEI IYNITQATSV
     AIEQHNISAA LRKSREELAV YAEALENKVA ERTVELKDMV RKLVESNMNL EDQIQITKTA
     ENSAIASQEL LVTIFRNFPK GFVGVVDMHL RVVFIEGEDL DTLNFRKAIQ VGDTIDELNN
     VPAELKKKVK QNVLKTLKGE HRSFEAKVQG KSYLVNTTPL FNEEQEVVQA LIVYNNISDQ
     KRVEVEIRNT LQKEKELNEL KSRFISMASH EFRTPLSAIL SATNLIERRN GDGQEEKRTK
     YIQTIKGSVK NLVDILNDFL SLSKLEEGKV VAQPILFDFV EFIEVLVEEV QGVKKNGQTI
     DVINSRSRIE VGLDTKLLRH IVHNLLSNAI KYSEEHKPIT LKIDTKDDKL FIEVADRGIG
     IPAEDQDYLF QRFYRAKNAT NFQGTGLGLN IVRQYTLLMN GTISFRSQLG QGTTFIVELP
     LNLLTNEKNT AY
//
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