GenomeNet

Database: UniProt
Entry: A9R3D3
LinkDB: A9R3D3
Original site: A9R3D3 
ID   UVRB_YERPG              Reviewed;         671 AA.
AC   A9R3D3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   18-SEP-2019, entry version 80.
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};
GN   OrderedLocusNames=YpAngola_A1430;
OS   Yersinia pestis bv. Antiqua (strain Angola).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=349746;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Angola;
RX   PubMed=20061468; DOI=10.1128/jb.01518-09;
RA   Eppinger M., Worsham P.L., Nikolich M.P., Riley D.R., Sebastian Y.,
RA   Mou S., Achtman M., Lindler L.E., Ravel J.;
RT   "Genome sequence of the deep-rooted Yersinia pestis strain Angola
RT   reveals new insights into the evolution and pangenome of the plague
RT   bacterium.";
RL   J. Bacteriol. 192:1685-1699(2010).
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. {ECO:0000255|HAMAP-
CC       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}.
DR   EMBL; CP000901; ABX86091.1; -; Genomic_DNA.
DR   RefSeq; WP_002210767.1; NZ_CP009935.1.
DR   SMR; A9R3D3; -.
DR   EnsemblBacteria; ABX86091; ABX86091; YpAngola_A1430.
DR   KEGG; ypg:YpAngola_A1430; -.
DR   PATRIC; fig|349746.12.peg.2396; -.
DR   HOGENOM; HOG000073580; -.
DR   KO; K03702; -.
DR   OMA; RYMHSEI; -.
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: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   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   SOS response.
FT   CHAIN         1    671       UvrABC system protein B.
FT                                /FTId=PRO_1000099582.
FT   DOMAIN       26    183       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      431    593       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      631    666       UVR. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   NP_BIND      39     46       ATP. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   MOTIF        92    115       Beta-hairpin.
SQ   SEQUENCE   671 AA;  76345 MW;  8627E50C544A19DE CRC64;
     MSKSFKLHSV FKPAGDQPEA IRKLEEGLEN GLAHQTLLGV TGSGKTFTVA NVIADLNRPT
     MILAPNKTLA AQLYGEMKEF FPDNAVEYFV SYYDYYQPEA YVPSSDTFIE KDASVNEHIE
     QMRLSATKAL LERRDVVVVA SVSAIYGLGD PDLYLKMMLH LTRGMIIDQR SILRRLSELQ
     YSRNDQVFQR GTFRVRGEVI DIFPAESDEW ALRVELFDEE VERLSIFDPL TGQLQHEVPR
     FTVYPKTHYV TPRERILQAM EEIKVELAER RQVLLANNKL LEEQRLSQRT QFDLEMMNEL
     GYCSGIENYS RYLSGRGPGE APPTLFDYLP ADGLLIVDES HVTIPQIGGM YKGDRSRKET
     LVEYGFRLPS ALDNRPMRFE EFEALAPQTI YVSATPGKYE LEKSGGDIIE QVVRPTGLLD
     PLIEVRPVAT QVDDLLSEIR IRAAINERVL VTTLTKRMAE DLTDYLSEHG AKVRYLHSDI
     DTVERVEIIR DLRLGEFDVL VGINLLREGL DMPEVSLVAI LDADKEGFLR SERSLIQTIG
     RAARNLNGKA ILYGDRITAS MEKAIGETER RRAKQQAYNE ERRIIPQGLN KKIGDILQLG
     QPSMRGKGKG RGSHKMADTT QYQSLSPKAL DQKIRELEAK MYTYAQNLEF EQAAELRDQV
     HQLRQQFIAI S
//
DBGET integrated database retrieval system