ID C0QBJ8_DESAH Unreviewed; 825 AA.
AC C0QBJ8;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 85.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=HRM2_39420 {ECO:0000313|EMBL:ACN17000.1};
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:ACN17000.1, ECO:0000313|Proteomes:UP000000442};
RN [1] {ECO:0000313|EMBL:ACN17000.1, 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; ACN17000.1; -; Genomic_DNA.
DR AlphaFoldDB; C0QBJ8; -.
DR STRING; 177437.HRM2_39420; -.
DR KEGG; dat:HRM2_39420; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG2202; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR eggNOG; COG4936; Bacteria.
DR HOGENOM; CLU_000445_114_51_7; -.
DR OrthoDB; 9806821at2; -.
DR Proteomes; UP000000442; Chromosome.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 2.10.70.100; -; 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; IPR018771; PocR_dom.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR PANTHER; PTHR43065; SENSOR 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; PF10114; PocR; 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; 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; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:ACN17000.1};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000000442};
KW Transferase {ECO:0000313|EMBL:ACN17000.1}.
FT DOMAIN 266..318
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 393..441
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 461..684
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 704..821
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT MOD_RES 756
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 825 AA; 92868 MW; 1055A63C6C18711D CRC64;
MVNTKIVDFI DFKKVNPLLE GFNQITGFVT AILDLEGNVL SKSKWRQICT EFHRINPETA
KNCTVSDTVL SNKMNGGGKY HFYKCLNGLI DVAVPIIIDG NHVANLFSGQ FLFEEPDISF
FKKQAKIHGF EESSYLKALA KVPIISQEKV KTAMDFLLNM TKVISEITSQ KLEQIELNKQ
REKNEEALRH SEEDLKKSQR IAHVGSWRLD LASNHVVWSE ELYRMYGFDP SSPPPPYTEH
QKLFTPESWN KLSTALTNTR ETGIPYELEL ETLREDGSRG WMWVHGEVIR DATGTTVGLR
GVTQDITGRK QTEEALKTSE KKYHSLFKNA QVALFRNRLS DGKILEINER YAKMSGYSNI
EDCMAEFNAA DAWVDPNGRK EFLRILHKNG VISDYETEII RRDGTHIWIS FSATIFPEQG
FLEGSIVDIT ERKRSERNQE KLQLQLNQAQ KMESVGRLAG GVAHDFNNML SIILGNAEII
MEDMDPSNPI VTNLEEIYKA AERSSSLTRQ LLAFARKQTI APKILNLNHV LADMLKMLMR
LIGEDIDLTW NPAPNLWSVK IDPSQIDQIL ANLCVNARDS IKSVGKVTIE TGNISFDEAY
CKEHQGFNPG SYVMMAVSDN GSGMDKKILD KLFEPFFTTK SIGQGTGLGL ATVYGIVKQN
HGFINVYSEP GEGTTFKIYL PVHSETAVAK QKDFKKTSLK GNETILLVED EKAILKMTKI
MLERLGYTVL TASAPTEAIS IMETSNVNEI QLLMTDVVMP EMNGRDLSRK LLTIYPGLKC
LFMSGYTANV IAHHGVLDTG VQFINKPFSM QDLAAKVRDV LDDGE
//
