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Database: UniProt
Entry: Q62CK6
LinkDB: Q62CK6
Original site: Q62CK6 
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   29-OCT-2014, entry version 70.
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=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. {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}.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC       {ECO:0000255|HAMAP-Rule:MF_00204}.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC       {ECO:0000255|HAMAP-Rule:MF_00204}.
CC   -!- SIMILARITY: Contains 1 UVR domain. {ECO:0000255|HAMAP-
CC       Rule:MF_00204}.
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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; LEKQMHE; -.
DR   OrthoDB; EOG6B360R; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-HAMAP.
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: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   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. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      450    616       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      647    682       UVR. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   NP_BIND      59     66       ATP. {ECO:0000255|HAMAP-Rule:MF_00204}.
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
//
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