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Database: UniProt
Entry: A0A1H1S5X4_9BACT
LinkDB: A0A1H1S5X4_9BACT
Original site: A0A1H1S5X4_9BACT 
ID   A0A1H1S5X4_9BACT        Unreviewed;       765 AA.
AC   A0A1H1S5X4;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   24-JAN-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=SAMN05444173_2874 {ECO:0000313|EMBL:SDS43136.1};
OS   Opitutus sp. GAS368.
OC   Bacteria; Verrucomicrobiota; Opitutae; Opitutales; Opitutaceae; Opitutus.
OX   NCBI_TaxID=1882749 {ECO:0000313|EMBL:SDS43136.1, ECO:0000313|Proteomes:UP000199432};
RN   [1] {ECO:0000313|EMBL:SDS43136.1, ECO:0000313|Proteomes:UP000199432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GAS368 {ECO:0000313|EMBL:SDS43136.1,
RC   ECO:0000313|Proteomes:UP000199432};
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; LT629735; SDS43136.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H1S5X4; -.
DR   STRING; 1882749.SAMN05444173_2874; -.
DR   OrthoDB; 184236at2; -.
DR   Proteomes; UP000199432; Chromosome i.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 3.
DR   CDD; cd00156; REC; 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; 3.30.450.20; PAS domain; 3.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013767; PAS_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 3.
DR   PANTHER; PTHR42878:SF7; OSMOLARITY TWO-COMPONENT SYSTEM PROTEIN SSK1; 1.
DR   PANTHER; PTHR42878; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00989; PAS; 1.
DR   Pfam; PF13426; PAS_9; 2.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 3.
DR   SMART; SM00091; PAS; 3.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 3.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 3.
DR   PROSITE; PS50112; PAS; 3.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000199432}.
FT   DOMAIN          6..122
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          140..187
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          215..267
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          264..334
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          337..389
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          390..444
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          468..518
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          547..761
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   COILED          509..540
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         57
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   765 AA;  84367 MW;  B0A15220FE314A33 CRC64;
     MKKEINVLII EDVPADVVII NHELRRGGLS FRSKRVGTKE EFLEELRSGP PDLILSDHGL
     PQFDGFSALA IAQNQCPEVP FLFVTGSMGE EVAIESLKSG ATDYVLKNRL TGLVPAVTRA
     LRLAEERRKR VEAEHALGLS EEHFRNLVEG VRDYAIFMLD TAGNITTWNT GAEWIMGYPA
     AEIVGRSHEC MFLASDVAAG QPGKLLRLAE NKGRSEREGW RLRKGGARFW ANTVVSTLRN
     PEGGLRGFAV ITRDITTHKE VEAVLARLAA IVQGSDDAII SKTLEGIITS WNHGAEKIFG
     YTAEEAVGRS IVMLLPPERS EEELSTLSKL ARGEKVEHFE TVRVTKDGRR IDVSEGISPI
     KDDTGRVIGA AKIARDITQQ KLAQEQLRRA EARNTAILQA ALDAVITIDR ESIVHDWNTA
     AERMFGYPRA EAIGRNVDAL IIPSTLLQVY RDGLAQYLIL GAGSLIGRPI ELTARRANGA
     ELAIELGITP IAASEPPLYT AIIRDISARK ETEAEIRRLN VELEQRVRAR TAELEAANQE
     LESFSYSVSH DLRAPLRHIT GFIEMLQARA APALDEESQR LARSIADSAA RMTRLIDALL
     GFSRLGRADL RKIRVSLAAL VRGAQRELRS EMHDRKIEWI SGPLPDVDGD PALLQQVLIN
     LLANALKYTR PREVARIEVG AKADAREVVC FVRDNGVGFD MRYADKLFGV FQRLHHPSEF
     EGTGIGLANV RLIVHRHGGR SWAEGTVNEG ATFFFSLPVA AAPVP
//
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