ID Q72F83_DESVH Unreviewed; 973 AA.
AC Q72F83;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 142.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=DVU_0331 {ECO:0000313|EMBL:AAS94814.1};
OS Desulfovibrio vulgaris (strain ATCC 29579 / DSM 644 / NCIMB 8303 / VKM
OS B-1760 / Hildenborough).
OC Bacteria; Thermodesulfobacteriota; Desulfovibrionia; Desulfovibrionales;
OC Desulfovibrionaceae; Nitratidesulfovibrio.
OX NCBI_TaxID=882 {ECO:0000313|EMBL:AAS94814.1, ECO:0000313|Proteomes:UP000002194};
RN [1] {ECO:0000313|EMBL:AAS94814.1, ECO:0000313|Proteomes:UP000002194}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29579 / DSM 644 / NCIMB 8303 / VKM B-1760 / Hildenborough
RC {ECO:0000313|Proteomes:UP000002194};
RX PubMed=15077118; DOI=10.1038/nbt959;
RA Heidelberg J.F., Seshadri R., Haveman S.A., Hemme C.L., Paulsen I.T.,
RA Kolonay J.F., Eisen J.A., Ward N., Methe B., Brinkac L.M., Daugherty S.C.,
RA Deboy R.T., Dodson R.J., Durkin A.S., Madupu R., Nelson W.C.,
RA Sullivan S.A., Fouts D., Haft D.H., Selengut J., Peterson J.D.,
RA Davidsen T.M., Zafar N., Zhou L., Radune D., Dimitrov G., Hance M.,
RA Tran K., Khouri H., Gill J., Utterback T.R., Feldblyum T.V., Wall J.D.,
RA Voordouw G., Fraser C.M.;
RT "The genome sequence of the anaerobic, sulfate-reducing bacterium
RT Desulfovibrio vulgaris Hildenborough.";
RL Nat. Biotechnol. 22:554-559(2004).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE017285; AAS94814.1; -; Genomic_DNA.
DR RefSeq; WP_010937638.1; NC_002937.3.
DR RefSeq; YP_009555.1; NC_002937.3.
DR AlphaFoldDB; Q72F83; -.
DR STRING; 882.DVU_0331; -.
DR PaxDb; 882-DVU_0331; -.
DR EnsemblBacteria; AAS94814; AAS94814; DVU_0331.
DR KEGG; dvu:DVU_0331; -.
DR PATRIC; fig|882.5.peg.313; -.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG3290; Bacteria.
DR eggNOG; COG4191; Bacteria.
DR HOGENOM; CLU_000445_114_39_7; -.
DR OrthoDB; 9769169at2; -.
DR PhylomeDB; Q72F83; -.
DR Proteomes; UP000002194; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR CDD; cd00130; PAS; 2.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.30.450.40; -; 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; IPR003018; GAF.
DR InterPro; IPR029016; GAF-like_dom_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013767; PAS_fold.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
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; PF01590; GAF; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00989; PAS; 1.
DR Pfam; PF13426; PAS_9; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00065; GAF; 1.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00091; PAS; 3.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 2.
PE 4: Predicted;
KW Kinase {ECO:0000313|EMBL:AAS94814.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002194};
KW Transferase {ECO:0000313|EMBL:AAS94814.1}.
FT DOMAIN 144..214
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 575..638
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 646..698
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 711..968
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 973 AA; 106011 MW; 992EBDCC6428E565 CRC64;
MTTVTATHIG QQSGKAASRG LSGPACLNEM LLSLVSLRDA DNAEQIADKM RTVAWLLPPA
LGEGCYAARI VWLGTAYDPP GLPAFPPHII HPFDVASRET GSIELWRTPA APLPPRAYAL
LEDCGQIISS CLQQIVTVAA TRERAEQYRS IFDYVTEALV LYDLEGIILD INAAALRLLG
ADHERLRGRW FGDLLPPDDA AELAAHINRI RLRGMTFAES HLRRMDGRPV PVEMTDRLLL
LQGRQVVLSN ARDISERHSA REALERRMER EHLVGDIATL LAGSTPEATQ AALTAVTERL
GNFLGVRHVW FIEMPPGETT VSLRHEWRAA GATSRKGTLD ATPLNMLPWS LWRLTDFETV
AIEDAGSLGK GHEHERDRHR EMGLVSTLAV PLRRRAELAG CLAMDDIGNR KWSAEDIALA
ETVGGMLGAA LDRTATLLQH QRAHAHIAAI LDTLPAQVAV VDGTGRITHV NASWLHAAAD
MSLPEPMRCL PGADYLSALD AKTPDIPSAG DAATLLREIL AGRREGGSLE YEVMADGRRH
FMLQLAPLMP PLTGAVLMRS DVTALRRAEA DLARSEVRYR MLLDTMQEGL LFTDAAGRMT
YINGPFCAMV EHDADALAGR EALDLVAPES RQAFQNLLFP EEAPPSLQEI TWLTSKGGRA
FSLVSPSILR DSHGHFIGLT AMITNITQRR ILESQLAQTQ KLEAVGSLAT GIAHEINSPV
QYLGSNLTFL QHAFDEIMKA YTTCDTALRT ARDGSSDVPS IDAALDAMQH LDTAYLRDEA
PRALRECLEG VEHIAAIVRS VRQFAHPGNG TVVPVNINFN IESTVNVARS SWRRVASLRL
DLAPGLPPVP CVPSEFNQTV LNLLINAVHA IEDRKAEDPA HEGSIVITSR LKAGWAEVSV
SDNGAGIKPE HAAHVFDPFF TTKPMERGTG QGLAIAHACI VGRLGGQLFF RSEPGLGSTF
FIRLPFTSPS QEA
//
