GenomeNet

Database: UniProt
Entry: A0A1G5B0I3_9PROT
LinkDB: A0A1G5B0I3_9PROT
Original site: A0A1G5B0I3_9PROT 
ID   A0A1G5B0I3_9PROT        Unreviewed;       702 AA.
AC   A0A1G5B0I3;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SAMN05216308_101490 {ECO:0000313|EMBL:SCX83649.1};
OS   Nitrosospira sp. Nsp13.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Nitrosomonadales;
OC   Nitrosomonadaceae; Nitrosospira.
OX   NCBI_TaxID=1855332 {ECO:0000313|EMBL:SCX83649.1, ECO:0000313|Proteomes:UP000198731};
RN   [1] {ECO:0000313|EMBL:SCX83649.1, ECO:0000313|Proteomes:UP000198731}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Nsp13 {ECO:0000313|EMBL:SCX83649.1,
RC   ECO:0000313|Proteomes:UP000198731};
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};
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; FMVD01000001; SCX83649.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G5B0I3; -.
DR   OrthoDB; 8552871at2; -.
DR   Proteomes; UP000198731; Unassembled WGS sequence.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   CDD; cd17580; REC_2_DhkD-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   Gene3D; 3.30.450.20; PAS domain; 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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 1.
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; PF08447; PAS_3; 1.
DR   Pfam; PF13188; PAS_8; 1.
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; 1.
DR   SMART; SM00091; PAS; 2.
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); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 1.
DR   PROSITE; PS50112; PAS; 1.
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}.
FT   DOMAIN          176..246
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          249..301
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          326..544
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          572..690
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          18..56
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          292..322
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         621
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   702 AA;  78937 MW;  8A50F424BE81EF23 CRC64;
     MIDDNEEKLL RSVALQTCNT ILLARQRAEN ELKQAKKSLE EKARRLDHSL SILRATIEST
     ADGILVTDQD GLVLRFNELY LQMWQIPRDI PNLSDHRQLL KFCCKCAKNP QWLMEETEGI
     YTSWPADSYD VLELADGRVF EQFSKIQYIE NQSIGRVWSF RDITARRHAE DALRESGERQ
     HFMAESMPLK IFTARADGVV DYFNQQWKDY TGLPLEQMEC WENTKLIHPD DLDENTRRWR
     HSLATGEPFQ MEIRLRQADG GYRWHLTRAH AKCDALGKVS MWVCSSTDID SIKRADEEKK
     QLLESERAAR NEAERANRMK DEFLATLSHE LRTPLNAILG WAQLISQGTM NQETVRRGLE
     TIERNARMQN KLIEDLLEMS SIISGKIRLD VQQLNLASIA EAALESLAPA AEAKDIHLIK
     KIDPAAGLVS GDYNRLQQII WNLLSNAVKF TPKGGNIEVI VERVASYLEI TVKDSGIGVK
     PEFLAYIFDR FRQADSSLTR HYGGLGLGLS IVKQLVALHG GTVHAESAGE GLGASFIVSL
     PLASVGDRRD QRMAASAAQA PRNRYITLSG IRILVIDDET DSRELINEVL TECDADVITA
     ASAAEGLELL QSSRPDVIIS DIGMPEKDGY QLIREVRNLP AAHGGKTPAI ALTAFARSED
     RTRAMIAGYQ MHLSKPVESH ELIATIGSLS KWTRKPRIEG EA
//
DBGET integrated database retrieval system