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
//