ID G0L0B6_ZOBGA Unreviewed; 1379 AA.
AC G0L0B6;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=zobellia_169 {ECO:0000313|EMBL:CAZ94242.1};
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:CAZ94242.1, 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:CAZ94242.1, 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; CAZ94242.1; -; Genomic_DNA.
DR RefSeq; WP_013991555.1; NC_015844.1.
DR STRING; 63186.ZOBELLIA_169; -.
DR KEGG; zga:ZOBELLIA_169; -.
DR PATRIC; fig|63186.3.peg.171; -.
DR HOGENOM; CLU_000445_28_1_10; -.
DR OrthoDB; 1522078at2; -.
DR Proteomes; UP000008898; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:DNA-binding transcription factor activity; IEA:InterPro.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR GO; GO:0043565; F:sequence-specific DNA binding; IEA:InterPro.
DR CDD; cd00075; HATPase; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR Gene3D; 2.130.10.10; YVTN repeat-like/Quinoprotein amine dehydrogenase; 2.
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; IPR009057; Homeobox-like_sf.
DR InterPro; IPR018060; HTH_AraC.
DR InterPro; IPR018062; HTH_AraC-typ_CS.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR011110; Reg_prop.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR011123; Y_Y_Y.
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; PF12833; HTH_18; 1.
DR Pfam; PF07494; Reg_prop; 3.
DR Pfam; PF00072; Response_reg; 1.
DR Pfam; PF07495; Y_Y_Y; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00342; HTH_ARAC; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF63829; Calcium-dependent phosphotriesterase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF101898; NHL repeat; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS00041; HTH_ARAC_FAMILY_1; 1.
DR PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000008898};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transferase {ECO:0000313|EMBL:CAZ94242.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..1379
FT /note="histidine kinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003402154"
FT TRANSMEM 811..829
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 862..1095
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1135..1250
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1282..1379
FT /note="HTH araC/xylS-type"
FT /evidence="ECO:0000259|PROSITE:PS01124"
FT MOD_RES 1183
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1379 AA; 156054 MW; A2DA22DD245F3458 CRC64;
MKFVKAVCKL ILCALCAQGH LCAQVSKTDY TFVNIEQDNT QRAVSAIVED SMGLIWMGTN
GVGLKKYNGI DFITYKQDLN EPKSISNSLI HTTYIDRKDR LWVGTETGLD LYNRDLDNFD
KIELRDEAVI EGGVLIRAIQ EGINGELLVG SHYHGMFRVD PLSLRSESIP IQSTINKSVI
QINYILKSVT GKIYVATNYG LFEYDGVKLS PSQIVNGKGE VVESLSRNIE TLFQDKDGAI
WLGTLSDGLI KIKLLSSNKY KIDSFSLTQE RVFSIAQAAD GNIICGTEND GLFVLKADGS
LIKNYRYDKF DVNSIKSNSI WTVFVDSQER IWIGYYNKGV GVYDTLYDKF KDIESSANLN
NSLQLPSVTG IVSDKKGRLW IGLDGGGIDV YDSESKKIVH LKDPGNPIAT NLHAAAVAGM
FFDSQGNLWV GTWNSGIYLL KKNTSTFINY KTSNTEGGLT SNRIMTFDED KNGIIWIGSY
VTGLHSYDPQ TEKFTAHNEE IFHDLIPSHG EVRKILVDSN GFIWLGTTGG LYKISSDFSA
GDKAISLVER MHEDTGRQLV VDRIVSLFED RRNILWIGTD GGGLCKYDPS KDTFTWYGDR
NGLSQQTIAS ILEDDSGAIW IGGNNGISRL DVEQENFKNF DIHDGLLAND FNFNSIFKDE
SGILYFGSYE GVNSIDPENL RFNEVKPEVY FTDFKLFNKS VVPGTQNSPL EKVIDRTKAI
TLTHDQSVFT IEYAGINFTR PKKNQYAYFL EGFDNRWNYV GKTRSATYTN LPPGDYVFKV
KAANNDGVWN NSPTALKIKV LSPWWSTNTA IFLYVLAILL ITYFLANLAS QRIREKRMVQ
FEREKRLQEE VLNDRKIQFF TNISHEFRTP LTLILNPLED ILTDTENQFS KKIREKLRTI
QKNTNRMKRL IDELMDFRKL DINKLTVKIS ELEAIAFVSE IAGHFEEEAS LKNILFQVES
DEMPITLWSD PSMLEKIIFN ILSNAFKITP DNGSITIGVF KCNEAMVFPQ VNDEKPVQAV
EIAIEDSGSG IKKEDLEKIF ERFYQAEHMN SQYYGGTGIG LEVVKSFIDL LKGKISVESE
ASIGTKFRIF LPLGKAHFKP SELFLAPDIN LDDKLEVKQE DGLLDQLTVD TDNQTLLVVE
DNAELRAYLK KELREEYNVI EAVNGTQGLE MALKRIPDVI LSDVVMPEMD GFEFCKRVRE
DLKTSHIPIL MLTAKTMTDD WVRGIDSGAD VYLNKPFEMK VLRAQLKQML NSRRVLFNKY
LNDSNNVKVP ENTSELDKGF ITKVLDYITA NLSDENLNVE QLAEELHLSR SQLYRKIKAL
TGCSANEFLR KIRLEKAKQM IENGNESISE VCFKVGFSSP SYFTKCFKAH FGYLPTEVK
//
