ID S0GQR2_9BACT Unreviewed; 769 AA.
AC S0GQR2;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=C803_03194 {ECO:0000313|EMBL:EOS16970.1};
OS Parabacteroides goldsteinii dnLKV18.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Tannerellaceae;
OC Parabacteroides.
OX NCBI_TaxID=1235789 {ECO:0000313|EMBL:EOS16970.1, ECO:0000313|Proteomes:UP000014140};
RN [1] {ECO:0000313|EMBL:EOS16970.1, ECO:0000313|Proteomes:UP000014140}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=dnLKV18 {ECO:0000313|Proteomes:UP000014140};
RG The Broad Institute Genomics Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A., Xavier R., Kuhn K., Stappenbeck T., Walker B., Young S., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Parabacteroides goldsteinii dnLKV18.";
RL Submitted (APR-2013) 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};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EOS16970.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ASSQ01000016; EOS16970.1; -; Genomic_DNA.
DR RefSeq; WP_010801775.1; NZ_KE159519.1.
DR AlphaFoldDB; S0GQR2; -.
DR GeneID; 82532305; -.
DR PATRIC; fig|1235789.3.peg.3197; -.
DR HOGENOM; CLU_000445_114_50_10; -.
DR Proteomes; UP000014140; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd17584; REC_typeB_ARR-like; 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 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; IPR036641; HPT_dom_sf.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR PANTHER; PTHR43047:SF72; OSMOSENSING HISTIDINE PROTEIN KINASE SLN1; 1.
DR PANTHER; PTHR43047; TWO-COMPONENT HISTIDINE PROTEIN KINASE; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF00072; Response_reg; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 1.
DR SUPFAM; SSF47226; Histidine-containing phosphotransfer domain, HPT domain; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 241..262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 303..515
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 536..653
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 190..224
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 585
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 769 AA; 87310 MW; 00FDBECBAA0FAFF3 CRC64;
MNSIRKLISC GYILIFMFIG IIIYCYKHEW QKLESLEKEN QAADELRQKI NELNFHLTGL
SLLGETVLEW NKDERGHYHA KRMAIDSMLC NFRRTYPTER IDSVRYLLED KERQMLSIVR
ILDKQQAVNK KIADQVPVIA QKSVQEQPKK PKRKGFLGIF GKKEEVKPTA TATMLHSLNK
NIISEQKAQS RRLSERADSL AEHNAELNRQ LQELIRQIDE KVQIDLKNRE NKISLMRKES
LMQIGSLTGF VLLLLIISYI TIYRDAKQIK QYKCKTAELI GQLKQSIQQN EALIVSRKKA
VHTITHELRT PLTTITGYTE LLRKECSNGN NVHFLQSIQQ SSDRMRDMLN TLLDFFRLDN
GKEQPRLSPC RISTIAHTLE TEFMPIAMNR GLSLTVKNEN DAVVLTDKER IIQIGNNLLS
NAIKFTEEGG VSLTTGYTDG VLILIVEDTG TGMTEDEQQR VFGAFERLSN AAAKDGFGLG
LAIVHNIVTM LHGTIRLDSD KGNGSRFIVK IPMQKAEDVP KKEIQTCIHQ KDRNLNVAAI
DNDEVLLLML KEMYAQDGIH CDTCTDTGEL MEMVRRKEYN LLLTDLNMPS INGFELLELL
RSSNVGNSQT IPVVVATASG SCDVEELLER GFAGCLFKPF SISELMEVSD KCAIKNTQDS
KPDFSALLSY GNEAVMLEKL ITETEKEMQA VRDAATRNDL QELDALTHHL RSSWEILRAD
QPLRILYGVL HGKAMPEESE LSHAVTAVLN MGAEIIRQAK EERRKYENG
//
