UVRB_ECOLI
ID UVRB_ECOLI Reviewed; 673 AA.
AC P0A8F8; P07025;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 141.
DE RecName: Full=UvrABC system protein B;
DE Short=Protein UvrB;
DE AltName: Full=Excinuclease ABC subunit B;
GN Name=uvrB; OrderedLocusNames=b0779, JW0762;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-8, AND PROTEOLYTIC
RP PRODUCT.
RC STRAIN=K12;
RX PubMed=3515321; DOI=10.1093/nar/14.6.2637;
RA Arikan E., Kulkarni M.S., Thomas D.C., Sancar A.;
RT "Sequences of the E. coli uvrB gene and protein.";
RL Nucleic Acids Res. 14:2637-2650(1986).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3008099; DOI=10.1093/nar/14.7.2877;
RA Backendorf C., Spaik H., Barbeiro A.P., van de Putte P.;
RT "Structure of the uvrB gene of Escherichia coli. Homology with other DNA
RT repair enzymes and characterization of the uvrB5 mutation.";
RL Nucleic Acids Res. 14:2877-2890(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 168-673.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [6]
RP IDENTIFICATION BY 2D-GEL.
RX PubMed=9298644; DOI=10.1002/elps.1150180805;
RA VanBogelen R.A., Abshire K.Z., Moldover B., Olson E.R., Neidhardt F.C.;
RT "Escherichia coli proteome analysis using the gene-protein database.";
RL Electrophoresis 18:1243-1251(1997).
RN [7]
RP FUNCTION, AND DIMERIC STATE OF UVRB.
RX PubMed=12145219; DOI=10.1093/emboj/cdf396;
RA Verhoeven E.E., Wyman C., Moolenaar G.F., Goosen N.;
RT "The presence of two UvrB subunits in the UvrAB complex ensures damage
RT detection in both DNA strands.";
RL EMBO J. 21:4196-4205(2002).
RN [8]
RP INDUCTION BY HYDROXYUREA.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=20005847; DOI=10.1016/j.molcel.2009.11.024;
RA Davies B.W., Kohanski M.A., Simmons L.A., Winkler J.A., Collins J.J.,
RA Walker G.C.;
RT "Hydroxyurea induces hydroxyl radical-mediated cell death in Escherichia
RT coli.";
RL Mol. Cell 36:845-860(2009).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 619-673.
RX PubMed=10631326; DOI=10.1016/s0014-5793(99)01690-7;
RA Sohi M., Alexandrovich A., Moolenaar G., Visse R., Goosen N., Vernede X.,
RA Fontecilla-Camps J.-C., Champness J., Sanderson M.R.;
RT "Crystal structure of Escherichia coli UvrB C-terminal domain, and a model
RT for UvrB-uvrC interaction.";
RL FEBS Lett. 465:161-164(2000).
RN [10]
RP STRUCTURE BY NMR OF 619-673.
RX PubMed=10371161; DOI=10.1016/s0014-5793(99)00542-6;
RA Alexandrovich A., Sanderson M.R., Moolenaar G.F., Goosen N., Lane A.N.;
RT "NMR assignments and secondary structure of the UvrC binding domain of
RT UvrB.";
RL FEBS Lett. 451:181-185(1999).
RN [11]
RP MUTAGENESIS OF 95-TYR-TYR-96; TYR-101 AND PHE-108.
RX PubMed=11689453; DOI=10.1093/emboj/20.21.6140;
RA Moolenaar G.F., Hoeglund L., Goosen N.;
RT "Clue to damage recognition by UvrB: residues in the beta-hairpin structure
RT prevent binding to non-damaged DNA.";
RL EMBO J. 20:6140-6149(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.
CC {ECO:0000269|PubMed:12145219}.
CC -!- SUBUNIT: Forms a heterotetramer with UvrA during the search for
CC lesions. Interacts with UvrC in an incision complex.
CC -!- INTERACTION:
CC P0A8F8; P0AFY8: seqA; NbExp=2; IntAct=EBI-552176, EBI-552553;
CC P0A8F8; P76373: ugd; NbExp=2; IntAct=EBI-552176, EBI-1120497;
CC P0A8F8; P0A698: uvrA; NbExp=7; IntAct=EBI-552176, EBI-552091;
CC P0A8F8; P0A8F8: uvrB; NbExp=3; IntAct=EBI-552176, EBI-552176;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- INDUCTION: Induced 1.5-fold by hydroxyurea.
CC {ECO:0000269|PubMed:20005847}.
CC -!- DOMAIN: The beta-hairpin motif is involved in DNA binding.
CC -!- MISCELLANEOUS: According to PubMed:3515321, a cleaved form of the
CC protein was observed that resulted from the removal of about 40 amino
CC acids from the C-terminus of the protein. The exact cleavage site being
CC unknown, it was proposed to be between Lys-630 and Ala-631. There was
CC no indication that cleavage occured in vivo and therefore it is not
CC known if it has any physiological significance.
CC -!- SIMILARITY: Belongs to the UvrB family. {ECO:0000305}.
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DR EMBL; X03678; CAA27314.1; -; Genomic_DNA.
DR EMBL; X03722; CAA27357.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73866.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35437.2; -; Genomic_DNA.
DR PIR; A93613; BVECUB.
DR RefSeq; NP_415300.1; NC_000913.3.
DR RefSeq; WP_000042533.1; NZ_STEB01000028.1.
DR PDB; 1E52; NMR; -; A/B=619-673.
DR PDB; 1QOJ; X-ray; 3.00 A; A/B=619-673.
DR PDBsum; 1E52; -.
DR PDBsum; 1QOJ; -.
DR AlphaFoldDB; P0A8F8; -.
DR SMR; P0A8F8; -.
DR BioGRID; 4259957; 140.
DR BioGRID; 849761; 19.
DR ComplexPortal; CPX-2151; UvrAB DNA damage sensor complex.
DR ComplexPortal; CPX-2152; UvrB pre-incision complex.
DR ComplexPortal; CPX-2153; UvrBC excinuclease repair complex.
DR DIP; DIP-48012N; -.
DR IntAct; P0A8F8; 32.
DR STRING; 511145.b0779; -.
DR jPOST; P0A8F8; -.
DR PaxDb; P0A8F8; -.
DR PRIDE; P0A8F8; -.
DR EnsemblBacteria; AAC73866; AAC73866; b0779.
DR EnsemblBacteria; BAA35437; BAA35437; BAA35437.
DR GeneID; 66670950; -.
DR GeneID; 945385; -.
DR KEGG; ecj:JW0762; -.
DR KEGG; eco:b0779; -.
DR PATRIC; fig|1411691.4.peg.1499; -.
DR EchoBASE; EB1055; -.
DR eggNOG; COG0556; Bacteria.
DR HOGENOM; CLU_009621_2_1_6; -.
DR InParanoid; P0A8F8; -.
DR OMA; EYVDRMV; -.
DR PhylomeDB; P0A8F8; -.
DR BioCyc; EcoCyc:EG11062-MON; -.
DR BioCyc; MetaCyc:EG11062-MON; -.
DR EvolutionaryTrace; P0A8F8; -.
DR PRO; PR:P0A8F8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0009380; C:excinuclease repair complex; IDA:UniProtKB.
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:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0006289; P:nucleotide-excision repair; IC:ComplexPortal.
DR GO; GO:0000715; P:nucleotide-excision repair, DNA damage recognition; IDA:ComplexPortal.
DR GO; GO:0033683; P:nucleotide-excision repair, DNA incision; IDA:ComplexPortal.
DR GO; GO:0006294; P:nucleotide-excision repair, preincision complex assembly; IDA:ComplexPortal.
DR GO; GO:0009314; P:response to radiation; IMP:EcoCyc.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Cytoplasm; Direct protein sequencing;
KW DNA damage; DNA excision; DNA repair; Excision nuclease;
KW Nucleotide-binding; Reference proteome; SOS response.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:3515321"
FT CHAIN 2..673
FT /note="UvrABC system protein B"
FT /id="PRO_0000138390"
FT DOMAIN 26..415
FT /note="Helicase ATP-binding"
FT DOMAIN 431..597
FT /note="Helicase C-terminal"
FT DOMAIN 633..668
FT /note="UVR"
FT REGION 608..627
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 92..115
FT /note="Beta-hairpin"
FT BINDING 39..46
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT SITE 630..631
FT /note="Cleavage"
FT /evidence="ECO:0000255"
FT MUTAGEN 95..96
FT /note="YY->AA: Defective in DNA-unwinding activity."
FT /evidence="ECO:0000269|PubMed:11689453"
FT MUTAGEN 101
FT /note="Y->A: Defective in DNA-unwinding activity; when
FT associated with A-108."
FT /evidence="ECO:0000269|PubMed:11689453"
FT MUTAGEN 108
FT /note="F->A: Defective in DNA-unwinding activity; when
FT associated with A-101."
FT /evidence="ECO:0000269|PubMed:11689453"
FT CONFLICT 477
FT /note="H -> R (in Ref. 1; CAA27314)"
FT /evidence="ECO:0000305"
FT HELIX 629..648
FT /evidence="ECO:0007829|PDB:1QOJ"
FT HELIX 654..671
FT /evidence="ECO:0007829|PDB:1QOJ"
SQ SEQUENCE 673 AA; 76226 MW; 2F172045344FDAD7 CRC64;
MSKPFKLNSA FKPSGDQPEA IRRLEEGLED GLAHQTLLGV TGSGKTFTIA NVIADLQRPT
MVLAPNKTLA AQLYGEMKEF FPENAVEYFV SYYDYYQPEA YVPSSDTFIE KDASVNEHIE
QMRLSATKAM LERRDVVVVA SVSAIYGLGD PDLYLKMMLH LTVGMIIDQR AILRRLAELQ
YARNDQAFQR GTFRVRGEVI DIFPAESDDI ALRVELFDEE VERLSLFDPL TGQIVSTIPR
FTIYPKTHYV TPRERIVQAM EEIKEELAAR RKVLLENNKL LEEQRLTQRT QFDLEMMNEL
GYCSGIENYS RFLSGRGPGE PPPTLFDYLP ADGLLVVDES HVTIPQIGGM YRGDRARKET
LVEYGFRLPS ALDNRPLKFE EFEALAPQTI YVSATPGNYE LEKSGGDVVD QVVRPTGLLD
PIIEVRPVAT QVDDLLSEIR QRAAINERVL VTTLTKRMAE DLTEYLEEHG ERVRYLHSDI
DTVERMEIIR DLRLGEFDVL VGINLLREGL DMPEVSLVAI LDADKEGFLR SERSLIQTIG
RAARNVNGKA ILYGDKITPS MAKAIGETER RREKQQKYNE EHGITPQGLN KKVVDILALG
QNIAKTKAKG RGKSRPIVEP DNVPMDMSPK ALQQKIHELE GLMMQHAQNL EFEEAAQIRD
QLHQLRELFI AAS
