UVRB_BEUC1
ID UVRB_BEUC1 Reviewed; 698 AA.
AC C5BV49;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 72.
DE RecName: Full=UvrABC system protein B {ECO:0000255|HAMAP-Rule:MF_00204};
DE Short=Protein UvrB {ECO:0000255|HAMAP-Rule:MF_00204};
DE AltName: Full=Excinuclease ABC subunit B {ECO:0000255|HAMAP-Rule:MF_00204};
GN Name=uvrB {ECO:0000255|HAMAP-Rule:MF_00204}; OrderedLocusNames=Bcav_2184;
OS Beutenbergia cavernae (strain ATCC BAA-8 / DSM 12333 / NBRC 16432).
OC Bacteria; Actinobacteria; Micrococcales; Beutenbergiaceae; Beutenbergia.
OX NCBI_TaxID=471853;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-8 / DSM 12333 / NBRC 16432;
RX PubMed=21304633; DOI=10.4056/sigs.1162;
RA Land M., Pukall R., Abt B., Goker M., Rohde M., Glavina Del Rio T.,
RA Tice H., Copeland A., Cheng J.F., Lucas S., Chen F., Nolan M., Bruce D.,
RA Goodwin L., Pitluck S., Ivanova N., Mavromatis K., Ovchinnikova G.,
RA Pati A., Chen A., Palaniappan K., Hauser L., Chang Y.J., Jefferies C.C.,
RA Saunders E., Brettin T., Detter J.C., Han C., Chain P., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.,
RA Lapidus A.;
RT "Complete genome sequence of Beutenbergia cavernae type strain (HKI
RT 0122).";
RL Stand. Genomic Sci. 1:21-28(2009).
CC -!- FUNCTION: The UvrABC repair system catalyzes the recognition and
CC processing of DNA lesions. A damage recognition complex composed of 2
CC UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of
CC the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps
CC around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB
CC and probably causes local melting of the DNA helix, facilitating
CC insertion of UvrB beta-hairpin between the DNA strands. Then UvrB
CC probes one DNA strand for the presence of a lesion. If a lesion is
CC found the UvrA subunits dissociate and the UvrB-DNA preincision complex
CC is formed. This complex is subsequently bound by UvrC and the second
CC UvrB is released. If no lesion is found, the DNA wraps around the other
CC UvrB subunit that will check the other stand for damage.
CC {ECO:0000255|HAMAP-Rule:MF_00204}.
CC -!- SUBUNIT: Forms a heterotetramer with UvrA during the search for
CC lesions. Interacts with UvrC in an incision complex.
CC {ECO:0000255|HAMAP-Rule:MF_00204}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00204}.
CC -!- DOMAIN: The beta-hairpin motif is involved in DNA binding.
CC {ECO:0000255|HAMAP-Rule:MF_00204}.
CC -!- SIMILARITY: Belongs to the UvrB family. {ECO:0000255|HAMAP-
CC Rule:MF_00204}.
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DR EMBL; CP001618; ACQ80436.1; -; Genomic_DNA.
DR RefSeq; WP_015882676.1; NC_012669.1.
DR AlphaFoldDB; C5BV49; -.
DR SMR; C5BV49; -.
DR STRING; 471853.Bcav_2184; -.
DR EnsemblBacteria; ACQ80436; ACQ80436; Bcav_2184.
DR KEGG; bcv:Bcav_2184; -.
DR eggNOG; COG0556; Bacteria.
DR HOGENOM; CLU_009621_2_1_11; -.
DR OMA; EYVDRMV; -.
DR OrthoDB; 95696at2; -.
DR Proteomes; UP000007962; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009380; C:excinuclease repair complex; IEA:InterPro.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-UniRule.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-UniRule.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 3.
DR HAMAP; MF_00204; UvrB; 1.
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; IPR001943; UVR_dom.
DR InterPro; IPR036876; UVR_dom_sf.
DR InterPro; IPR004807; UvrB.
DR InterPro; IPR041471; UvrB_inter.
DR InterPro; IPR024759; UvrB_YAD/RRR_dom.
DR PANTHER; PTHR24029; PTHR24029; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF04851; ResIII; 1.
DR Pfam; PF02151; UVR; 1.
DR Pfam; PF12344; UvrB; 1.
DR Pfam; PF17757; UvrB_inter; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF46600; SSF46600; 1.
DR SUPFAM; SSF52540; SSF52540; 2.
DR TIGRFAMs; TIGR00631; uvrb; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS50151; UVR; 1.
PE 3: Inferred from homology;
KW ATP-binding; Cytoplasm; DNA damage; DNA excision; DNA repair;
KW Excision nuclease; Helicase; Hydrolase; Nucleotide-binding;
KW Reference proteome; SOS response.
FT CHAIN 1..698
FT /note="UvrABC system protein B"
FT /id="PRO_1000204129"
FT DOMAIN 35..210
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 438..604
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 654..689
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT MOTIF 101..124
FT /note="Beta-hairpin"
FT BINDING 48..55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
SQ SEQUENCE 698 AA; 78462 MW; 825499DE47B7E65B CRC64;
MRPVTDLQRR VFPFEVISDF TPSGDQPDAI AQLTARLQAG EKDIVLLGAT GTGKSATTAW
LIEQVQRPTL VMAPNKTLAA QLATEFRELL PNNAVEYFVS YYDYYQPEAY VPSSDTYIEK
DSSINDEVER LRHSATNSLL TRRDVVVVAS VSCIYGLGTP QEYVDRMVRL RVGMQIERDD
LLRQFVGMQY TRNDLSFQRG TFRVRGDTVE IIPVYEELAL RIEFFGDEVE AIHTLHPLTG
DVVRAEEEMY LFPATHYVAG PERMERAIAG IEVELEDRLA ELEGGGRLLE AQRLRMRTTY
DIEMMRQIGT CSGIENYSRH IDGREPGSPP HTLLDYFPED FMLVIDESHQ TVPQIGAMYE
GDSSRKRTLV EHGFRLPSAM DNRPLRWEEF LERIGQTVYL SATPGPYELG QSDGVVEQVI
RPTGLVDPEI VVKPTKGQID DLLAEINARA ERDERVLVTT LTKKMSEDLT DYLLERGVRV
RYLHSEVDTL RRVELLRELR TGVFDVLVGI NLLREGLDLP EVSLVAILDA DKEGFLRSGT
SLIQTIGRAA RNVSGQVHMY ADSVTPSMAL AIEETNRRRE KQVAYNTERG IDPEPLRKRI
GDITELLARE DIDTKELLAG GYRQAGSKAP VPRKAGGDGS MRERLAGAAT ADLAELIQEL
TDQMHVAAGE LQFEVAARLR DEISDLKKEL RQMSAASA
