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Database: UniProt
Entry: G0L4Q0_ZOBGA
LinkDB: G0L4Q0_ZOBGA
Original site: G0L4Q0_ZOBGA 
ID   G0L4Q0_ZOBGA            Unreviewed;      1406 AA.
AC   G0L4Q0;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 71.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=zobellia_4695 {ECO:0000313|EMBL:CAZ98830.1};
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:CAZ98830.1, 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:CAZ98830.1, 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; CAZ98830.1; -; Genomic_DNA.
DR   STRING; 63186.ZOBELLIA_4695; -.
DR   KEGG; zga:ZOBELLIA_4695; -.
DR   HOGENOM; CLU_000445_28_1_10; -.
DR   OMA; VNTIFER; -.
DR   OrthoDB; 1522078at2; -.
DR   Proteomes; UP000008898; Chromosome.
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; 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; 4.
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; 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; 8.
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; 3.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS01124; HTH_ARAC_FAMILY_2; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000008898};
KW   Transferase {ECO:0000313|EMBL:CAZ98830.1}.
FT   DOMAIN          874..1100
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1151..1266
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          1298..1397
FT                   /note="HTH araC/xylS-type"
FT                   /evidence="ECO:0000259|PROSITE:PS01124"
FT   MOD_RES         1199
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1406 AA;  159587 MW;  3E109F3F20E308BE CRC64;
     MKTKPLDKLF YLLMFFSVLL GNAQNHISFK HITTSDGLSQ SDINAVYQDK QGFMWFATHD
     GLNKYDGYKF TVYNPSPIKP NCISSNLISA ISGDDEGNLW VGTTGSGLNF YNASTGDFTT
     FTHNEEDVSS IIGNYVTALY RDSKNRLWVG EKDGLNMVDL SLPIDHLKFQ HYNSEQDPFI
     IGWDGSSIYS IYEDKNGQLL VGGATGLFKL KKDPNGNEYF GNINKSLGLP DCIVRDIKED
     NLGRLIIATD VGLFCQVKGN GLKLAKIHDN NVNNILVDNN NHLWVGSNEG LFYFENASPE
     KLPRYIKRFT YDSRDSGSIS KNIIKSLYLD KTGIIWIGTN GGGINIFDPG RKQFLHVRNT
     PDPQSLSYDK IRAMYEDSNG TVWVGTEGGG LNMLTKQDDD GNYDKFRRFS SISRTFAITE
     TVLDNKKTLF IGAESTPGLY LLNIDDPSQI KESDLRPQGL MHGVFSLLND SDENIWIGTY
     TSGVQRWIKK EDGKGYDKTT FKSYPKQAHV LPSNIVRYIL EDKFGNIWFA TGDGLSVVKA
     IERYKKHPKF ETYKNNSEDP KSLSHNYILS LYESTEGELW IGTFGGGLNK FVPGENGETD
     SFISYSVQDG LPNDVIKGIL EDSEANLWLS TNMGLSKFNP KKETFKNYNE NDGLQDNEFQ
     ELACVKRSDG EMLFGGINGF NAFYPEDIGD NEHLAETVIT DMLVSNESVK VGAELDGKVI
     LDKSINKIKN IELGYRQNNF SFEFAALHYA APSKNKFAYM LEGFDPNWVQ TTSNKRFATY
     TNLEPGDYVF KVKASNNDGL WDETPSQIQI TITPPIWQTS AAYLFYGALV LGMLWLFWRY
     TFIRTSEKHQ LELDHLEKEK SEEMQRVKLE FFTNISHEFR TPLTLIKGPL EYLRKDGDKI
     SRTKVHEQYN IMYKNTNYLL KLVNQLLDFR KIDQGKMHLV VRNSNIVEFI QEVGQPFQFL
     AHKQNIEFTI QADQESLQTW FDHDALEKIM NNLLSNAFKY TPDGGRITVE IATEGEAKND
     QGENVIIKVR DSGYGIAENR VNTIFERFNT QDKKDRRNLQ GAGIGLSFTK NLIELHQGSI
     VVKSKPNKGT DFIVRLPVDK AVYMNIPEVS IKEVSESDFL VRSSETESFA IGINDEILDA
     DVSKSRPKQP ILLVVDDNAD IRTLVKQGLE SDYVIYEAEN GKQALKVAKN IMPNIILTDI
     LMPIMDGTEF CKSLKSDKET SHIPVVMLTA KASQESEIEN LKIGVEGYIR KPFDMELLQL
     TLGNILKHRE QLRKQFTRNI TLQPAEIAVT SVDESFLQTA IEIVEKHMMN TDFNVEMLVK
     EMGYSRSNLY MKFKEITGLS SSEFIRNIRL KRAVQLFEQS DLSVKEIMYK TGFNTASYFS
     KCFKKQFGVI PSEYVAQLKN KKNTTS
//
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