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Database: UniProt
Entry: P0A8F9
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ID   UVRB_ECO57              Reviewed;         673 AA.
AC   P0A8F9; P07025;
DT   01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   31-JUL-2019, entry version 101.
DE   RecName: Full=UvrABC system protein B;
DE            Short=Protein UvrB;
DE   AltName: Full=Excinuclease ABC subunit B;
GN   Name=uvrB; OrderedLocusNames=Z0998, ECs0857;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(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 (By similarity).
CC       {ECO:0000250}.
CC   -!- SUBUNIT: Forms a heterotetramer with UvrA during the search for
CC       lesions. Interacts with UvrC in an incision complex (By
CC       similarity). {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}.
DR   EMBL; AE005174; AAG55150.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB34280.1; -; Genomic_DNA.
DR   PIR; A99736; A99736.
DR   PIR; B85586; B85586.
DR   RefSeq; NP_308884.1; NC_002695.1.
DR   RefSeq; WP_000042533.1; NZ_SDVX01000001.1.
DR   SMR; P0A8F9; -.
DR   STRING; 155864.EDL933_0900; -.
DR   EnsemblBacteria; AAG55150; AAG55150; Z0998.
DR   EnsemblBacteria; BAB34280; BAB34280; BAB34280.
DR   GeneID; 917595; -.
DR   KEGG; ece:Z0998; -.
DR   KEGG; ecs:ECs0857; -.
DR   PATRIC; fig|386585.9.peg.971; -.
DR   eggNOG; ENOG4105CCW; Bacteria.
DR   eggNOG; COG0556; LUCA.
DR   HOGENOM; HOG000073580; -.
DR   KO; K03702; -.
DR   BioCyc; ECOO157:UVRB-MONOMER; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; 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:ATPase 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   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; Complete proteome; Cytoplasm; DNA damage; DNA excision;
KW   DNA repair; Excision nuclease; Nucleotide-binding; Reference proteome;
KW   SOS response.
FT   INIT_MET      1      1       Removed. {ECO:0000250}.
FT   CHAIN         2    673       UvrABC system protein B.
FT                                /FTId=PRO_0000138391.
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}.
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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