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Database: UniProt
Entry: A0A017HGG9_9RHOB
LinkDB: A0A017HGG9_9RHOB
Original site: A0A017HGG9_9RHOB 
ID   A0A017HGG9_9RHOB        Unreviewed;       731 AA.
AC   A0A017HGG9;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=Rumeso_04673 {ECO:0000313|EMBL:EYD73552.1};
OS   Rubellimicrobium mesophilum DSM 19309.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Rubellimicrobium.
OX   NCBI_TaxID=442562 {ECO:0000313|EMBL:EYD73552.1, ECO:0000313|Proteomes:UP000019666};
RN   [1] {ECO:0000313|EMBL:EYD73552.1, ECO:0000313|Proteomes:UP000019666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19309 {ECO:0000313|EMBL:EYD73552.1,
RC   ECO:0000313|Proteomes:UP000019666};
RA   Fiebig A., Goeker M., Klenk H.-P.P.;
RL   Submitted (FEB-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   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:EYD73552.1}.
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DR   EMBL; AOSK01000130; EYD73552.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A017HGG9; -.
DR   STRING; 442562.Rumeso_04673; -.
DR   PATRIC; fig|442562.3.peg.4603; -.
DR   HOGENOM; CLU_019564_1_0_5; -.
DR   OrthoDB; 9776727at2; -.
DR   Proteomes; UP000019666; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd06225; HAMP; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 1.
DR   InterPro; IPR003660; HAMP_dom.
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; IPR017232; NtrY.
DR   InterPro; IPR045671; NtrY-like_N.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF19312; NtrY_N; 1.
DR   Pfam; PF08448; PAS_4; 1.
DR   PIRSF; PIRSF037532; STHK_NtrY; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 2.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777}; Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019666};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:EYD73552.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        33..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        76..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        281..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          303..356
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          493..713
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          712..731
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   731 AA;  80238 MW;  0ADFBE81D1873F60 CRC64;
     MRNAATLGLV VLGPVLAGLT YVVLGPLDQG ASSTALRIVL LTDLVYVLAI AALVAREVAR
     MVAARRAKSA GSRLHLRLVG VFALLALLPT VTVAVFSVLT INVGLEGWFS ERVREVVTNS
     MAAAEAYEQE HRQELTRDGE ALAEALDQQK QANVALSDGD IRQALGRMQA QIERGLTEAF
     VIDGAGDIRA RGARSYEFAY ERPSDEDFRL AQAEGIRIIE DWPNDEFRAL IPLPSFLDRY
     LYVTRAVDGE ILSLLDETKD TVELYRQLDS DKGRLLFEFG LLYLGFAVIL ILAAVWLGLW
     FAEGLSKPIG RLLSASQRVG EGDLDVRVIE EEGDDEIAAL GRHFNQMTRQ LKAQRGRLLE
     TTEQIEQRRR LFDSVLSSVT SGVVGLDAMG RVTFANRSAQ RLLDVGEAPG RVALAVAVPE
     FGPLFDALSQ ESREVVQEQV ALVRGGKQET LLVRMSPRRA DDGSLEGYVV AFDDVTDLVS
     AQRMAAWGDV ARRIAHEIKN PLTPIRLSAE RIKRKFRRHL DETAAGDLDQ MTDVIVRQTE
     DLRRIVDEFS KFARMPEPDR RDSDLTALVR DAVTLQEAGQ PGVKFVSVLP AAQVPAEVDP
     GMISQALTNL IKNAGEAIES YQEQGAEPGF QPVIKVQLQP EGAVARITIE DNGIGLPEDR
     ARLFEPYVTT RAKGTGLGLP IVKKIIEEHG GTLQLEDAEG RGARAVIRLP TKARPSIEAD
     QPETSQARRA V
//
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