ID A0A1H1VGC2_9FLAO Unreviewed; 1025 AA.
AC A0A1H1VGC2;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN04487764_3193 {ECO:0000313|EMBL:SDS83783.1};
OS Gillisia sp. Hel1_33_143.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Gillisia.
OX NCBI_TaxID=1336796 {ECO:0000313|EMBL:SDS83783.1, ECO:0000313|Proteomes:UP000199552};
RN [1] {ECO:0000313|EMBL:SDS83783.1, ECO:0000313|Proteomes:UP000199552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hel1_33_143 {ECO:0000313|EMBL:SDS83783.1,
RC ECO:0000313|Proteomes:UP000199552};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; LT629737; SDS83783.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1VGC2; -.
DR STRING; 1336796.SAMN04487764_3193; -.
DR Proteomes; UP000199552; Chromosome i.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00130; PAS; 5.
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; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
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; IPR013767; PAS_fold.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR NCBIfam; TIGR00229; sensory_box; 5.
DR PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00989; PAS; 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; SM00387; HATPase_c; 1.
DR SMART; SM00086; PAC; 5.
DR SMART; SM00091; PAS; 5.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 5.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 5.
DR PROSITE; PS50112; PAS; 3.
PE 4: Predicted;
KW Reference proteome {ECO:0000313|Proteomes:UP000199552}.
FT DOMAIN 145..218
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 222..275
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 341..393
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 473..525
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 526..596
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 600..652
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 653..699
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 742..793
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 811..1024
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 1025 AA; 117618 MW; C5DD4532F7BF6646 CRC64;
MTYLKEELHA LIQKDIRIFD FIQESGLDGI IFRDLINEDH EWQDMKFWNS LGYLKKEVSK
LKSSKELYKS SRLLRIDSKA EYSENLTTIS FDLQEFDEFK EYHHKSGKVL TFKAAQYLVY
NDKNEPIRQL IGLKNITSND DLAKKIKHYE QIIEGTGIGA WEWNLQTHEV IFNEQWAKIL
GYSLEELQPI TPDIWNRFCH PDDTERCAKL LDDHISGKND VYESEARMRH KNGSWIWVLD
KGKVVSYTPD GKAEWMTGFH EEITQRKKEF ERNKLFIDKA PSEIAMFDNN MRYLAASQRW
KIGYGIDEIE IIGRCHYNIF PNISDEWKAI HKECLGGKTL KKEEDSYIGL DGELHWLSWE
VSPWYNHNNE IGGILMHTSD ITPIKAAEQA IKEKQALLEA VLNNIEVGIV CCDTQGKLTL
FNKATQEWHG LPAEPINPSE FPEYYNLFEA DGETPLATEN IPLIKSLRTG SVKNQEIIIQ
KVDGTYKIVS VNGSHLKDID GNVLGAVVAM HDITTKKIAE DRLRISEQTF RGNFENAAIG
MAIVDIAGQW VEVNKSLCSI FGYTEEELLE STLEDLTHPD DLEIDLQRLE ELIRGIRNFY
HIEKRYIHKN GETIHGILSV SIVLDETGAP LHFVSQITDI TLRKKTQQKL QNTLAYLESI
FQASSRVSII ATDTNGIITS FNKGAENLLG YSREEMENKC SPQKIHLKKE IKKRGRELEK
LLGIDVREIK PLTALADKGQ FDTREWTYVR KNGTQFPVLL TVTPIKDEEE IIGYLGIGTE
ITQLKNAEKE IISLLEVTKD QNERLKNFAH IVSHNLRSHS GNFEMLLDLY VQENPEAKEN
EMIQYLNVAS ENLKETIAHL NEVVLINTSM KDNLVKIDLK ECIDKSSKNI GAIARDIDVK
IINEVDATIR VLGIPAYMDS ILLNFLTNGV KYSSRERDSY IKLSTYIEDE FVVLSIEDNG
IGIDLKKNES KLFGMYKTFH KNKDARGIGL FITKNQVEAL GGKIETESTV DKGTTFKIYF
KYEKN
//
