XPB_KINRD
ID XPB_KINRD Reviewed; 557 AA.
AC A6WE36;
DT 03-AUG-2022, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=DNA helicase XPB {ECO:0000303|PubMed:19199647};
DE EC=3.6.4.12 {ECO:0000269|PubMed:19199647};
GN Name=XPB {ECO:0000303|PubMed:19199647};
GN OrderedLocusNames=Krad_3612 {ECO:0000312|EMBL:ABS05075.1};
OS Kineococcus radiotolerans (strain ATCC BAA-149 / DSM 14245 / SRS30216).
OC Bacteria; Actinobacteria; Kineosporiales; Kineosporiaceae; Kineococcus.
OX NCBI_TaxID=266940;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216;
RX PubMed=19057647; DOI=10.1371/journal.pone.0003878;
RA Bagwell C.E., Bhat S., Hawkins G.M., Smith B.W., Biswas T., Hoover T.R.,
RA Saunders E., Han C.S., Tsodikov O.V., Shimkets L.J.;
RT "Survival in nuclear waste, extreme resistance, and potential applications
RT gleaned from the genome sequence of Kineococcus radiotolerans SRS30216.";
RL PLoS ONE 3:e3878-e3878(2008).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP SUBUNIT, DOMAIN, AND DNA-BINDING.
RC STRAIN=ATCC BAA-149 / DSM 14245 / SRS30216;
RX PubMed=19199647; DOI=10.1021/bi8022416;
RA Biswas T., Pero J.M., Joseph C.G., Tsodikov O.V.;
RT "DNA-dependent ATPase activity of bacterial XPB helicases.";
RL Biochemistry 48:2839-2848(2009).
CC -!- FUNCTION: ATP-dependent 3'-5' DNA helicase, unwinds 3'-overhangs,
CC 3'- flaps, and splayed-arm DNA substrates but not 5'-overhangs or 5'-
CC flap substrates. Requires ATP hydrolysis for activity; the ATPase
CC activity is DNA-dependent and requires a minimum of 4 single-stranded
CC nucleotides (nt) with 6-10 nt providing all necessary interactions for
CC full processive unwinding. The ATPase prefers ATP over CTP or GTP, is
CC almost inactive with TTP. {ECO:0000269|PubMed:19199647}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=3.6.4.12;
CC Evidence={ECO:0000269|PubMed:19199647};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:19199647};
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:19199647};
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:19199647};
CC Note=ATPase activity has a small preference for Mn(2+) over Mg(2+) or
CC Ca(2+). Co(2+) and Zn(2+) are inactive. {ECO:0000269|PubMed:19199647};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=10 uM for 21-mer ssDNA substrate {ECO:0000269|PubMed:19199647};
CC KM=50 uM for 10-mer ssDNA substrate {ECO:0000269|PubMed:19199647};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:19199647}.
CC -!- DOMAIN: Removal of the N-terminus decreases solubility and/or
CC structural integrity of the protein. {ECO:0000269|PubMed:19199647}.
CC -!- SIMILARITY: Belongs to the helicase family. RAD25/XPB subfamily.
CC {ECO:0000305}.
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DR EMBL; CP000750; ABS05075.1; -; Genomic_DNA.
DR RefSeq; WP_012086663.1; NC_009664.2.
DR STRING; 266940.Krad_3612; -.
DR EnsemblBacteria; ABS05075; ABS05075; Krad_3612.
DR KEGG; kra:Krad_3612; -.
DR eggNOG; COG1061; Bacteria.
DR HOGENOM; CLU_008213_4_0_11; -.
DR OMA; LKLGWPA; -.
DR OrthoDB; 377818at2; -.
DR Proteomes; UP000001116; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003678; F:DNA helicase activity; IEA:UniProtKB-EC.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR032438; ERCC3_RAD25_C.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR032830; XPB/Ssl2_N.
DR Pfam; PF16203; ERCC3_RAD25_C; 1.
DR Pfam; PF13625; Helicase_C_3; 1.
DR Pfam; PF04851; ResIII; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
PE 1: Evidence at protein level;
KW ATP-binding; DNA-binding; Helicase; Hydrolase; Magnesium; Manganese;
KW Nucleotide-binding; Reference proteome.
FT CHAIN 1..557
FT /note="DNA helicase XPB"
FT /id="PRO_0000455758"
FT DOMAIN 190..344
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 398..544
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT REGION 1..135
FT /note="Required for protein stability or solubility"
FT /evidence="ECO:0000269|PubMed:19199647"
FT MOTIF 298..301
FT /note="DEAH box"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 203..210
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
SQ SEQUENCE 557 AA; 61373 MW; F45AC8064F6D0456 CRC64;
MTDGPLIVQS DKTLLLEVDH PRAGACRAAI APFAELERAP EHVHTYRLTP LGLWNARAAG
HDAEQVVDTL LEFSRYSVPH ALLVDVAETM ARYGRLQLVK DEEHGLVLRS LDPAVLEEVL
RSRKSAPLLG TRIAPDAVLV HPSERGNLKQ VLLKLGWPAE DLAGYVDGEA HAIDLAEDGW
ALRPYQSEAV DNFWNGGSGV VVLPCGAGKT LVGAAAMAKA RATTLILVTN TVSARQWRDE
LLKRTSLTED EIGEYSGARK EIRPVTIATY QVVTTKRKGV YPHLELFDAR DWGLILYDEV
HLLPAPIFRM TADLQARRRL GLTATLVRED GREGDVFSLI GPKRYDAPWK DIEAQGYIAP
ADCVEVRVTL PDAERLAYAT AEDDEKYRLC STSLSKSRVV EKLVAQHAGE PTLVIGQYID
QLDDLAARLD APVIKGETTV KERQRLFDAF RHGEITTLVV SKVANFSIDL PEAKVAIQVS
GSFGSRQEEA QRLGRVLRPK GDHGSARFYT VVSRDTKDQD YAAHRQRFLA EQGYAYRIVD
ADDIDGGVPD ADGVLPG
