ID UVRB_NITEU Reviewed; 695 AA.
AC Q82WA9;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 01-MAY-2013, entry version 64.
DE RecName: Full=UvrABC system protein B;
DE Short=Protein UvrB;
DE AltName: Full=Excinuclease ABC subunit B;
GN Name=uvrB; OrderedLocusNames=NE0785;
OS Nitrosomonas europaea (strain ATCC 19718 / NBRC 14298).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Nitrosomonadaceae; Nitrosomonas.
OX NCBI_TaxID=228410;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 19718 / NBRC 14298;
RX PubMed=12700255; DOI=10.1128/JB.185.9.2759-2773.2003;
RA Chain P., Lamerdin J.E., Larimer F.W., Regala W., Lao V., Land M.L.,
RA Hauser L., Hooper A.B., Klotz M.G., Norton J., Sayavedra-Soto L.A.,
RA Arciero D.M., Hommes N.G., Whittaker M.M., Arp D.J.;
RT "Complete genome sequence of the ammonia-oxidizing bacterium and
RT obligate chemolithoautotroph Nitrosomonas europaea.";
RL J. Bacteriol. 185:2759-2773(2003).
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; AL954747; CAD84696.1; -; Genomic_DNA.
DR RefSeq; NP_840859.1; NC_004757.1.
DR ProteinModelPortal; Q82WA9; -.
DR SMR; Q82WA9; 8-600.
DR STRING; 228410.NE0785; -.
DR EnsemblBacteria; CAD84696; CAD84696; NE0785.
DR GeneID; 1081724; -.
DR KEGG; neu:NE0785; -.
DR PATRIC; 22712554; VBINitEur56163_0880.
DR eggNOG; COG0556; -.
DR HOGENOM; HOG000073580; -.
DR KO; K03702; -.
DR OMA; CIYGLGI; -.
DR ProtClustDB; PRK05298; -.
DR BioCyc; NEUR228410:GJNO-806-MONOMER; -.
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 1 695 UvrABC system protein B.
FT /FTId=PRO_0000227334.
FT DOMAIN 31 414 Helicase ATP-binding.
FT DOMAIN 435 601 Helicase C-terminal.
FT DOMAIN 632 667 UVR.
FT NP_BIND 44 51 ATP (Potential).
FT MOTIF 97 120 Beta-hairpin.
SQ SEQUENCE 695 AA; 79423 MW; 62BD4D26765A0251 CRC64;
MIITFPGSPY KLNQAFQPAG DQPEAIRILV EGIESGLSFQ TLLGVTGSGK TFTIANMIAR
LGRPAIIMAP NKTLAAQLYA EMREFFPENA VEYFVSYYDY YQPEAYVPSR DLFIEKDSSI
NEHIEQMRLS ATKSLLERED AIIVATVSCI YGIGDPVDYH GMILHVREHE KISQRDIIQR
LTGMQYQRNE FEFARGTFRV RGDVLDVFPA ENSETALRIS LFDDEVESMT LFDPLTGQTR
QKVSRYTVYP SSHYVTPRST TLRAIETIKT ELTGRLNYFH ENHKLVEAQR LEQRTRFDLE
MLNELGFCKG IENYSRHLSG RQPGDPPPTL IDYLPDNALM IIDESHVTVP QIGGMYKGDR
SRKENLVAYG FRLPSALDNR PLRFEEFEKL MPQTIFVSAT PADYEIQRSG QIAEQVVRPT
GLVDPVIIIR PVTTQVDDLM SEVSLRAAQN ERVLVTTLTK RMAEDLTDYF SDHGIRVRYL
HSDIDTVERV EIIRDLRLGK FDVLVGINLL REGLDIPEVS LVGILDADKE GFLRSERSLI
QTMGRAARHV NGTVILYADK ITNSMRRAID ETERRRNKQK LFNQQNNITP RGVNKRIKDL
IDGVYDSENA AEHRKVAQIQ ARYAAMDEAQ LAKEIQRLEK SMLEAARNME FEQAAQYRDE
IKNLRSKLFI GIIDPDEIRE VPQTAGKKSR RKAGR
//
