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Database: UniProt
Entry: A8ZYQ9_DESOH
LinkDB: A8ZYQ9_DESOH
Original site: A8ZYQ9_DESOH 
ID   A8ZYQ9_DESOH            Unreviewed;       403 AA.
AC   A8ZYQ9;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 94.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=Dole_1360 {ECO:0000313|EMBL:ABW67164.1};
OS   Desulfosudis oleivorans (strain DSM 6200 / JCM 39069 / Hxd3) (Desulfococcus
OS   oleovorans).
OC   Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC   Desulfosudaceae; Desulfosudis.
OX   NCBI_TaxID=96561 {ECO:0000313|EMBL:ABW67164.1, ECO:0000313|Proteomes:UP000008561};
RN   [1] {ECO:0000313|EMBL:ABW67164.1, ECO:0000313|Proteomes:UP000008561}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 6200 / JCM 39069 / Hxd3
RC   {ECO:0000313|Proteomes:UP000008561};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA   Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA   Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Wawrik B.,
RA   Richardson P.;
RT   "Complete sequence of Desulfococcus oleovorans Hxd3.";
RL   Submitted (OCT-2007) 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; CP000859; ABW67164.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8ZYQ9; -.
DR   STRING; 96561.Dole_1360; -.
DR   KEGG; dol:Dole_1360; -.
DR   eggNOG; COG0745; Bacteria.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_000445_114_72_7; -.
DR   Proteomes; UP000008561; Chromosome.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 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; 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; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 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; 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   Kinase {ECO:0000313|EMBL:ABW67164.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000008561};
KW   Transferase {ECO:0000313|EMBL:ABW67164.1}.
FT   DOMAIN          1..112
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          150..367
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   MOD_RES         47
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   403 AA;  44200 MW;  6C22470F7656CB3B CRC64;
     MVDDEADFLN AVSRRLEKRG IPPVLAGSGE DGLALLAETP MDVVVLDVKM PGMGGLEALR
     RIKDSWPDME VILLTGNVSA ADGVEGIKQG AFDYITKPIE IDHLAGKIRQ AWDKRRRKQE
     QEEQRQFQEK MEQQMTAMDR LASLGTLSTG VAHEINNPLA MMREAAGYMR LVLEKEDMVQ
     WPGKTGLAKG LEKIEKGIER IRRITHLLLG FVRPADHACA RTDVKELVSE SIELVTKEMQ
     GKQIAVDRKM DDTEGVAWTD PYALRQVMIN LLTNAVHAIQ REGTITVSLS EAEGCLAIAV
     SDTGVGIPGE NLNKIFEPFF STKPSDKGTG LGLYVSRGIV ERLDGRIGVK SAVGRGTTFT
     VEIPVCRRGD AVECVDENTC DEILTKIKEI GGDDEDTRKS AGG
//
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