ID UVRB_BURMA Reviewed; 696 AA.
AC Q62CK6;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 01-MAY-2013, entry version 62.
DE RecName: Full=UvrABC system protein B;
DE Short=Protein UvrB;
DE AltName: Full=Excinuclease ABC subunit B;
GN Name=uvrB; OrderedLocusNames=BMAA0880;
OS Burkholderia mallei (strain ATCC 23344).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=243160;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23344;
RX PubMed=15377793; DOI=10.1073/pnas.0403306101;
RA Nierman W.C., DeShazer D., Kim H.S., Tettelin H., Nelson K.E.,
RA Feldblyum T.V., Ulrich R.L., Ronning C.M., Brinkac L.M.,
RA Daugherty S.C., Davidsen T.D., DeBoy R.T., Dimitrov G., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Haft D.H., Khouri H.M., Kolonay J.F.,
RA Madupu R., Mohammoud Y., Nelson W.C., Radune D., Romero C.M.,
RA Sarria S., Selengut J., Shamblin C., Sullivan S.A., White O., Yu Y.,
RA Zafar N., Zhou L., Fraser C.M.;
RT "Structural flexibility in the Burkholderia mallei genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:14246-14251(2004).
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 -!- SUBUNIT: Forms a heterotetramer with UvrA during the search for
CC lesions. Interacts with UvrC in an incision complex (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- DOMAIN: The beta-hairpin motif is involved in DNA binding (By
CC similarity).
CC -!- SIMILARITY: Belongs to the UvrB family.
CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC -!- SIMILARITY: Contains 1 UVR domain.
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DR EMBL; CP000011; AAU46751.1; -; Genomic_DNA.
DR RefSeq; YP_105572.1; NC_006349.2.
DR ProteinModelPortal; Q62CK6; -.
DR SMR; Q62CK6; 25-615.
DR STRING; 243160.BMAA0880; -.
DR EnsemblBacteria; AAU46751; AAU46751; BMAA0880.
DR GeneID; 3086196; -.
DR KEGG; bma:BMAA0880; -.
DR PATRIC; 19123838; VBIBurMal55007_4401.
DR eggNOG; COG0556; -.
DR HOGENOM; HOG000073580; -.
DR KO; K03702; -.
DR OMA; CIYGLGI; -.
DR ProtClustDB; PRK05298; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0003677; F:DNA binding; IEA:HAMAP.
DR GO; GO:0009381; F:excinuclease ABC activity; IEA:HAMAP.
DR GO; GO:0004386; F:helicase activity; IEA:HAMAP.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:HAMAP.
DR GO; GO:0009432; P:SOS response; IEA:HAMAP.
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; 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; UvrB_C; 1.
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; SOS response.
FT CHAIN 1 696 UvrABC system protein B.
FT /FTId=PRO_0000227294.
FT DOMAIN 46 433 Helicase ATP-binding.
FT DOMAIN 450 616 Helicase C-terminal.
FT DOMAIN 647 682 UVR.
FT NP_BIND 59 66 ATP (Potential).
FT MOTIF 112 135 Beta-hairpin.
SQ SEQUENCE 696 AA; 79428 MW; F276C194D2005000 CRC64;
MSEHHSDTRD DLDESKFVTF EGSPFQLYQP YPPSGDQPTA IATLVEGVED GLSFQTLLGV
TGSGKTYTMA NTIARLGRPA IVFAPNKTLA AQLYAEFREF FPRNAVEYFV SYYDYYQPEA
YVPQRDLFIE KDSSINEHIE QMRLSATKSL MERRDVVIVA TVSAIYGIGN PSEYHQMILT
LRTGDKIGQR EVIARLIAMQ YTRNEQDFQR GTFRVRGDTI DIFPAEHAEM AVRVELFDDE
VDTLHLFDPL TGRVRQKIPR FTVYPSSHYV TPRETVMRAV ETIKDELRER LEFFHRDGKL
VEAQRLEQRT RFDLEMLQEL GFCKGIENYS RHFSGAAPGE PPPTLVDYLP PDALMLLDES
HVLIGQLNGM YNGDRARKEN LVDYGFRLPS ALDNRPLKFP EFERKMRQVV FVSATPADYE
QRVSGQTAEQ VVRPTGLVDP QIEVRPASTQ VDDVLSEITE RVKANERVLI TVLTKRMAEQ
LTEFLADHGV KVRYLHSDID TVERVEIIRD LRLGTFDVLV GINLLREGLD IPEVSLVAIL
DADKEGFLRA ERSLIQTIGR AARNVNGKAL LYADRITDSM RRAIDETERR RAKQIAYNEK
MGITPRGVVK RIKDIIDGVY NADEARAELK EAQQRAKFED MSEKQIAKEI KRLEKQMADY
AKNLEFEKAA QTRDQLALLR ERVFGANVGD HVSGGE
//
