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Database: UniProt
Entry: C0QIA3_DESAH
LinkDB: C0QIA3_DESAH
Original site: C0QIA3_DESAH 
ID   C0QIA3_DESAH            Unreviewed;       954 AA.
AC   C0QIA3;
DT   05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   05-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 81.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   OrderedLocusNames=HRM2_27470 {ECO:0000313|EMBL:ACN15839.1};
OS   Desulforapulum autotrophicum (strain ATCC 43914 / DSM 3382 / VKM B-1955 /
OS   HRM2) (Desulfobacterium autotrophicum).
OC   Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC   Desulfobacteraceae; Desulforapulum.
OX   NCBI_TaxID=177437 {ECO:0000313|EMBL:ACN15839.1, ECO:0000313|Proteomes:UP000000442};
RN   [1] {ECO:0000313|EMBL:ACN15839.1, ECO:0000313|Proteomes:UP000000442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43914 / DSM 3382 / HRM2
RC   {ECO:0000313|Proteomes:UP000000442};
RX   PubMed=19187283; DOI=10.1111/j.1462-2920.2008.01825.x;
RA   Strittmatter A.W., Liesegang H., Rabus R., Decker I., Amann J., Andres S.,
RA   Henne A., Fricke W.F., Martinez-Arias R., Bartels D., Goesmann A.,
RA   Krause L., Puehler A., Klenk H.P., Richter M., Schuler M., Gloeckner F.O.,
RA   Meyerdierks A., Gottschalk G., Amann R.;
RT   "Genome sequence of Desulfobacterium autotrophicum HRM2, a marine sulfate
RT   reducer oxidizing organic carbon completely to carbon dioxide.";
RL   Environ. Microbiol. 11:1038-1055(2009).
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; CP001087; ACN15839.1; -; Genomic_DNA.
DR   RefSeq; WP_015904602.1; NC_012108.1.
DR   AlphaFoldDB; C0QIA3; -.
DR   STRING; 177437.HRM2_27470; -.
DR   KEGG; dat:HRM2_27470; -.
DR   eggNOG; COG0745; Bacteria.
DR   eggNOG; COG2202; Bacteria.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_308987_0_0_7; -.
DR   OMA; MIEDISA; -.
DR   OrthoDB; 5417856at2; -.
DR   Proteomes; UP000000442; Chromosome.
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; cd00130; PAS; 3.
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; IPR013656; PAS_4.
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; 3.
DR   PANTHER; PTHR43304:SF1; PAC DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43304; PHYTOCHROME-LIKE PROTEIN CPH1; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF08447; PAS_3; 2.
DR   Pfam; PF08448; PAS_4; 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; 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; 2.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:ACN15839.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000000442};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..27
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        133..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          184..256
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          260..313
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          330..373
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          390..442
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          512..570
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          590..808
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          829..948
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         880
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   954 AA;  109472 MW;  A3C4573AD5FBCD3D CRC64;
     MIKNYKVIFT VVLIVLTAIF LSFVVYYQKS TQHKADLALD GHAVIIADAL WRYEKSTPIE
     YLKLAAKALH YKKVSVFDDS SNAFIEIKNT DKETAEDFLT NAGLLPVYHL EKNIFYNKKH
     IGKITIDWQN RAVFTYFYIF LCLVLVLMAV WLFLNLTVAK MTLEDRVIER TADLKASENR
     LRLSEERLEM ALAGANDGIW DWNLETGSVH YDTRYYVMLG YKPHEFQSSF EAFEKRVHSD
     DIVGVKNAIE NYLSGKIDIF HQEFRMLNKN GDYQWIRSKG KIAVRDKQNK PVRFIGTHSD
     INEHKILEKA RDDAYGIINS SPLVAFIWKN EQGWPVEFVT ENIENVFGYH PDELLSHTIR
     YDQIVFPDDL KRVGHEIGKP NFEKKSNNFI HRPYRIITKS GNIRWVEDRT YIKRNDTGEI
     THYHGILMDI TNRIDAEEAQ IKSNRILKLV LNSIPVRVFW KDTQSIYLGG NQAFAEDAGL
     RSPDDLVGKT DHDLAFSAQA GVFQRDEKEV IRSGKSKLFY EEPQDRPDGK TNWLLTSKVP
     MRDAQQKIIG ILGTYQDITD RKQAEKEKIA AQKIAGDNEK LALVGQIAGK MAHDFNNILG
     IIMGNTELSL LYCKEPKTKK TLELIYEQTI RGKNLTKNLV AFAKDQELKQ EFFRISEKIN
     LVINLMRKDL EGIELIKQES PGVPELLADP GMIEHALVNL IQNSIHALSM VEHPRITVRT
     YSRGNQICFE IEDNGCGISK ENLENIYEPS FTLKGSRDVA GSYKTGIKGT GYGMSNVKKY
     IEQHKGTISI ESEYGSGTKF TISLPVIKKE LTSDERIKTQ TGTAYFEKYI LLVEDETAIA
     DVQYRILTQA PCNHKVDIAN NGQVAMDLFD RNEYDLISLD YILPGDINGM DMYHHIRASD
     KTIPILFISG NIEFLESIKY LMKKDPYVDH LSKPCKNIHY LNSINKLFSR PKLI
//
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