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Database: UniProt
Entry: Q2JRR3
LinkDB: Q2JRR3
Original site: Q2JRR3 
ID   UVRB_SYNJA              Reviewed;         695 AA.
AC   Q2JRR3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   07-MAR-2006, sequence version 1.
DT   01-OCT-2014, entry version 62.
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=CYA_2564;
OS   Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium
OS   Yellowstone A-Prime).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Synechococcus.
OX   NCBI_TaxID=321327;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JA-3-3Ab;
RX   PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA   Bhaya D., Grossman A.R., Steunou A.-S., Khuri N., Cohan F.M.,
RA   Hamamura N., Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT   "Population level functional diversity in a microbial community
RT   revealed by comparative genomic and metagenomic analyses.";
RL   ISME J. 1:703-713(2007).
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; CP000239; ABD00683.1; -; Genomic_DNA.
DR   RefSeq; WP_011431356.1; NC_007775.1.
DR   RefSeq; YP_475946.1; NC_007775.1.
DR   ProteinModelPortal; Q2JRR3; -.
DR   SMR; Q2JRR3; 4-616.
DR   STRING; 321327.CYA_2564; -.
DR   EnsemblBacteria; ABD00683; ABD00683; CYA_2564.
DR   GeneID; 3899899; -.
DR   KEGG; cya:CYA_2564; -.
DR   PATRIC; 23813386; VBISynSp90045_2518.
DR   eggNOG; COG0556; -.
DR   HOGENOM; HOG000073580; -.
DR   KO; K03702; -.
DR   OMA; LEKQMHE; -.
DR   OrthoDB; EOG6B360R; -.
DR   BioCyc; SSP321327:GHFX-2556-MONOMER; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; Helicase; Hydrolase;
KW   Nucleotide-binding; SOS response.
FT   CHAIN         1    695       UvrABC system protein B.
FT                                /FTId=PRO_1000077934.
FT   DOMAIN       25    176       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      454    617       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      652    687       UVR. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   NP_BIND      38     45       ATP. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   MOTIF        91    114       Beta-hairpin.
SQ   SEQUENCE   695 AA;  79027 MW;  28C6FCE2217E5E56 CRC64;
     MSEFQLVSSY QPTGDQPKAI AGLVKSILEG HRFQTLLGAT GTGKTFTIAH TIQQVGRPTL
     VMAPNKTLAA QLCNELRELF PYNAVEYFIS YYDYYQPEAY VPSTDTYIAK SSSINDEIDM
     LRHSATRSLF ERRDVIVVAS VSCIYGLGMP EEYLKASIPF QVGQEINQRE VLRDLAGIQY
     ERNDLELARG RFRVKGDVLE IVPAYEDRVI RIEFFGDEIE AIRLIDPVTG EILTSLSALR
     VYPARHFVTP EAQLQQAILN IEQELEEQLA FFRKQGKLLE AQRLEQRTRY DLEMLREVGY
     CNGIENYSRH LTGRKEGEPP ACLVDYFKAN DWLLVVDESH VTVPQIRGMY NGDRARKQVL
     VDHGFRLPSA LDNRPLKAEE FWAKVHQCVF VSATPGNWEL EQSGAQFETV VENGKTLKFY
     VPGTGRVIEQ VIRPTGVVDP EVHVRPTAGQ VEDLLGEIYL RLERSQQGLP ERVIVTTLTK
     RMAEDLTEYL QERGIRVRYL HSEISSIERI EILQDFREGA FDVLVGVNLL REGLDLPEVS
     LVAILDADKE GFLRAERSLI QMIGRAARNV RGTVVMYADT LTGSMARAIA ETQRRREIQL
     QYNRQHNITP KPIIKKNSNA ILSFLAISRK LNSQDLEKAF PVADEIPLSE IPELIGQLEL
     KMKAAAKNLE FEEAAQLRDQ IKKLRQRLLG HHQST
//
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