UVRB_STRR6
ID UVRB_STRR6 Reviewed; 662 AA.
AC Q8DPK7;
DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=UvrABC system protein B;
DE Short=Protein UvrB;
DE AltName: Full=Excinuclease ABC subunit B;
GN Name=uvrB; Synonyms=uvr402; OrderedLocusNames=spr1118;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1551859; DOI=10.1128/jb.174.7.2412-2415.1992;
RA Sicard N., Oreglia J., Estevenson A.M.;
RT "Structure of the gene complementing uvr-402 in Streptococcus pneumoniae:
RT homology with Escherichia coli uvrB and the homologous gene in Micrococcus
RT luteus.";
RL J. Bacteriol. 174:2412-2415(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
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 (By
CC similarity). {ECO:0000250}.
CC -!- SUBUNIT: Forms a heterotetramer with UvrA during the search for
CC lesions. Interacts with UvrC in an incision complex (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- DOMAIN: The beta-hairpin motif is involved in DNA binding.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the UvrB family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA27020.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M80215; AAA27020.1; ALT_INIT; Genomic_DNA.
DR EMBL; AE007317; AAK99921.1; -; Genomic_DNA.
DR PIR; A42385; A42385.
DR PIR; E98011; E98011.
DR RefSeq; NP_358711.1; NC_003098.1.
DR RefSeq; WP_000607031.1; NC_003098.1.
DR AlphaFoldDB; Q8DPK7; -.
DR SMR; Q8DPK7; -.
DR STRING; 171101.spr1118; -.
DR EnsemblBacteria; AAK99921; AAK99921; spr1118.
DR GeneID; 60234226; -.
DR KEGG; spr:spr1118; -.
DR PATRIC; fig|171101.6.peg.1214; -.
DR eggNOG; COG0556; Bacteria.
DR HOGENOM; CLU_009621_2_1_9; -.
DR OMA; EYVDRMV; -.
DR Proteomes; UP000000586; 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: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; Nucleotide-binding; Reference proteome; SOS response.
FT CHAIN 1..662
FT /note="UvrABC system protein B"
FT /id="PRO_0000138433"
FT DOMAIN 31..418
FT /note="Helicase ATP-binding"
FT DOMAIN 435..601
FT /note="Helicase C-terminal"
FT DOMAIN 626..661
FT /note="UVR"
FT MOTIF 97..120
FT /note="Beta-hairpin"
FT BINDING 44..51
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT CONFLICT 364
FT /note="E -> K (in Ref. 1; AAA27020)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 662 AA; 75752 MW; C13DA06AD4206B11 CRC64;
MINHITDNQF KLVSKYQPSG DQPQAIEQLV DNIEGGEKAQ ILMGATGTGK TYTMSQVISK
VNKPTLVIAH NKTLAGQLYG EFKEFFPENA VEYFVSYYDY YQPEAYVPSS DTYIEKDSSV
NDEIDKLRHS ATSALLERND VIVVASVSCI YGLGSPKEYA DSVVSLRPGL EISRDKLLND
LVDIQFERND IDFQRGRFRV RGDVVEIFPA SRDEHAFRVE FFGDEIDRIR EVEALTGQVL
GEVDHLAIFP ATHFVTNDDH MEVAIAKIQA ELEEQLAVFE KEGKLLEAQR LKQRTEYDIE
MLREMGYTNG VENYSRHMDG RSEGEPPYTL LDFFPDDFLI MIDESHMTMG QIKGMYNGDR
SRKEMLVNYG FRLPSALDNR PLRREEFESH VHQIVYVSAT PGDYENEQTE TVIEQIIRPT
GLLDPEVEVR PTMGQIDDLL GEINARVEKN ERTFITTLTK KMAEDLTDYF KEMGIKVKYM
HSDIKTLERT EIIRDLRLGV FDVLVGINLL REGIDVPEVS LVAILDADKE GFLRNERGLI
QTIGRAARNS EGHVIMYADT VTQSMQRAID ETARRRKIQM AYNEEHGIVP QTIKKEIRDL
IAVTKAVAKE EDKEVDINSL NKQERKELVK KLEKQMQEAV EVLDFELAAQ IRDMMLEVKA
LD
