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
//