GenomeNet

Database: UniProt
Entry: Q2P0Z3
LinkDB: Q2P0Z3
Original site: Q2P0Z3 
ID   UVRB_XANOM              Reviewed;         673 AA.
AC   Q2P0Z3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   31-JUL-2019, entry version 91.
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=XOO3029;
OS   Xanthomonas oryzae pv. oryzae (strain MAFF 311018).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xanthomonas.
OX   NCBI_TaxID=342109;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MAFF 311018;
RA   Ochiai H., Inoue Y., Takeya M., Sasaki A., Kaku H.;
RT   "Genome sequence of Xanthomonas oryzae pv. oryzae suggests
RT   contribution of large numbers of effector genes and insertion
RT   sequences to its race diversity.";
RL   Jpn. Agric. Res. Q. 39:275-287(2005).
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; AP008229; BAE69784.1; -; Genomic_DNA.
DR   RefSeq; WP_011409045.1; NC_007705.1.
DR   SMR; Q2P0Z3; -.
DR   EnsemblBacteria; BAE69784; BAE69784; BAE69784.
DR   KEGG; xom:XOO3029; -.
DR   KO; K03702; -.
DR   OMA; RYMHSEI; -.
DR   BioCyc; XORY342109:G1G2D-3361-MONOMER; -.
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    673       UvrABC system protein B.
FT                                /FTId=PRO_1000077942.
FT   DOMAIN       26    183       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      431    597       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      635    670       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   673 AA;  76075 MW;  ACA27CCF0A6A766E CRC64;
     MTDRFQLVSP YSPAGDQPAA IDKLVANFEA GLAKQTLLGV TGSGKTYTIA NVVQQVQKPT
     LVMAPNKTLA AQLYGEFKSF FPHNAVEYFV SYYDYYQPEA YVPSSDTFIE KDSSINEHIE
     QMRLSATKTL LSRRDSLVVA TVSAIYGLGA PEDYLSLRLI LSIGEHIDQR QLIRHLTDLQ
     YTRNEFELTR GAFRVRGEVL DVFPAESDTE ALRIELFDGD IEQLTLFDPL TGETLRKLQR
     YTVYPKTHYA TTRERTLSAV DTIKEELKER LEQLYSQSKL VEAQRLAQRT QFDLEMMAEV
     GFCNGIENYS RHLTGKAPGE PPPTLFDYLP PDALLVIDES HVTIPQIGAM YKGDRSRKET
     LVEFGFRLPS ALDNRPLRFE EWEARSPRSI YVSATPGPYE LRESAGEVTE LVVRPTGLID
     PVVEIRPVGM QVDDLMSEIH ERIKLGDRVL VTTLTKRMAE NLTEYLGEHG IRVRYLHSDI
     DTVERVEIIR DLRLGKFDVL VGINLLREGL DMPEVSLVAI LDADKEGFLR STGSLIQTIG
     RAARNLRGKA ILYADKMTRS MQAAIDESDR RREKQVEYNL EHGITPESVE RPISDIMEGA
     REDAAEKKSG KGRSKSRQVA EETPDYRAMK PAEIAGKLKS LEQKMYQHAK DLEFEAAAQI
     RDQIQKLKTA SLA
//
DBGET integrated database retrieval system