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Entry: P0A8F8
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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   01-OCT-2014, entry version 94.
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; Enterobacteriales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83333;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-8, AND
RP   PROTEOLYTIC 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
RT   DNA 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.,
RA   Mau B., 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
RT   MG1655 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.,
RA   Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K.,
RA   Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K.,
RA   Mori H., Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N.,
RA   Sampei G., Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y.,
RA   Yano M., Horiuchi T.;
RT   "A 718-kb DNA sequence of the Escherichia coli K-12 genome
RT   corresponding to 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.,
RA   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   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.,
RA   Vernede X., Fontecilla-Camps J.-C., Champness J., Sanderson M.R.;
RT   "Crystal structure of Escherichia coli UvrB C-terminal domain, and a
RT   model for UvrB-uvrC interaction.";
RL   FEBS Lett. 465:161-164(2000).
RN   [9]
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.,
RA   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   [10]
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
RT   structure 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
CC       of 2 UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon
CC       binding of the UvrA(2)B(2) complex to a putative damaged site, the
CC       DNA wraps around one UvrB monomer. DNA wrap is dependent on ATP
CC       binding by UvrB and probably causes local melting of the DNA
CC       helix, facilitating insertion of UvrB beta-hairpin between the DNA
CC       strands. Then UvrB probes one DNA strand for the presence of a
CC       lesion. If a lesion is found the UvrA subunits dissociate and the
CC       UvrB-DNA preincision complex is formed. This complex is
CC       subsequently bound by UvrC and the second UvrB is released. If no
CC       lesion is found, the DNA wraps around the other UvrB subunit that
CC       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       P0AFY8:seqA; NbExp=2; IntAct=EBI-552176, EBI-552553;
CC       P76373:ugd; NbExp=2; IntAct=EBI-552176, EBI-1120497;
CC   -!- SUBCELLULAR LOCATION: Cytoplasm.
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
CC       amino acids from the C-terminus of the protein. The exact cleavage
CC       site being unknown, it was proposed to be between Lys-630 and Ala-
CC       631. There was no indication that cleavage occured in vivo and
CC       therefore it is not known if it has any physiological
CC       significance.
CC   -!- SIMILARITY: Belongs to the UvrB family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 UVR domain. {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; YP_489052.1; NC_007779.1.
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   ProteinModelPortal; P0A8F8; -.
DR   SMR; P0A8F8; 5-596, 627-672.
DR   DIP; DIP-48012N; -.
DR   IntAct; P0A8F8; 31.
DR   MINT; MINT-1244062; -.
DR   STRING; 511145.b0779; -.
DR   PaxDb; P0A8F8; -.
DR   PRIDE; P0A8F8; -.
DR   EnsemblBacteria; AAC73866; AAC73866; b0779.
DR   EnsemblBacteria; BAA35437; BAA35437; BAA35437.
DR   GeneID; 12930963; -.
DR   GeneID; 945385; -.
DR   KEGG; ecj:Y75_p0752; -.
DR   KEGG; eco:b0779; -.
DR   PATRIC; 32116759; VBIEscCol129921_0805.
DR   EchoBASE; EB1055; -.
DR   EcoGene; EG11062; uvrB.
DR   eggNOG; COG0556; -.
DR   HOGENOM; HOG000073580; -.
DR   KO; K03702; -.
DR   OMA; LEKQMHE; -.
DR   OrthoDB; EOG6B360R; -.
DR   PhylomeDB; P0A8F8; -.
DR   BioCyc; EcoCyc:EG11062-MONOMER; -.
DR   BioCyc; ECOL316407:JW0762-MONOMER; -.
DR   BioCyc; MetaCyc:EG11062-MONOMER; -.
DR   EvolutionaryTrace; P0A8F8; -.
DR   PRO; PR:P0A8F8; -.
DR   Genevestigator; P0A8F8; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-HAMAP.
DR   GO; GO:0005515; F:protein binding; IPI:IntAct.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-HAMAP.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-HAMAP.
DR   Gene3D; 3.40.50.300; -; 4.
DR   Gene3D; 4.10.860.10; -; 1.
DR   HAMAP; MF_00204; UvrB; 1.
DR   InterPro; IPR006935; Helicase/UvrB_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR001943; UVR_dom.
DR   InterPro; IPR004807; UvrB.
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   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF46600; SSF46600; 1.
DR   SUPFAM; SSF52540; SSF52540; 3.
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; Complete proteome; Cytoplasm;
KW   Direct protein sequencing; DNA damage; DNA excision; DNA repair;
KW   Excision nuclease; Nucleotide-binding; Reference proteome;
KW   SOS response.
FT   INIT_MET      1      1       Removed. {ECO:0000269|PubMed:3515321}.
FT   CHAIN         2    673       UvrABC system protein B.
FT                                /FTId=PRO_0000138390.
FT   DOMAIN       26    415       Helicase ATP-binding.
FT   DOMAIN      431    597       Helicase C-terminal.
FT   DOMAIN      633    668       UVR.
FT   NP_BIND      39     46       ATP. {ECO:0000255}.
FT   MOTIF        92    115       Beta-hairpin.
FT   SITE        630    631       Cleavage. {ECO:0000255}.
FT   MUTAGEN      95     96       YY->AA: Defective in DNA-unwinding
FT                                activity.
FT   MUTAGEN     101    101       Y->A: Defective in DNA-unwinding
FT                                activity; when associated with A-108.
FT                                {ECO:0000269|PubMed:11689453}.
FT   MUTAGEN     108    108       F->A: Defective in DNA-unwinding
FT                                activity; when associated with A-101.
FT                                {ECO:0000269|PubMed:11689453}.
FT   CONFLICT    477    477       H -> R (in Ref. 1; CAA27314).
FT                                {ECO:0000305}.
FT   HELIX       629    648
FT   HELIX       654    671
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
//
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