GenomeNet

Database: UniProt
Entry: A7FYY1
LinkDB: A7FYY1
Original site: A7FYY1 
ID   UVRB_CLOB1              Reviewed;         662 AA.
AC   A7FYY1;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   11-SEP-2007, sequence version 1.
DT   31-JUL-2019, entry version 79.
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=CLB_3443;
OS   Clostridium botulinum (strain ATCC 19397 / Type A).
OC   Bacteria; Firmicutes; Clostridia; Clostridiales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=441770;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 19397 / Type A;
RX   PubMed=18060065; DOI=10.1371/journal.pone.0001271;
RA   Smith T.J., Hill K.K., Foley B.T., Detter J.C., Munk A.C., Bruce D.C.,
RA   Doggett N.A., Smith L.A., Marks J.D., Xie G., Brettin T.S.;
RT   "Analysis of the neurotoxin complex genes in Clostridium botulinum A1-
RT   A4 and B1 strains: BoNT/A3, /Ba4 and /B1 clusters are located within
RT   plasmids.";
RL   PLoS ONE 2:E1271-E1271(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}.
DR   EMBL; CP000726; ABS33225.1; -; Genomic_DNA.
DR   RefSeq; WP_003357634.1; NC_009697.1.
DR   SMR; A7FYY1; -.
DR   PRIDE; A7FYY1; -.
DR   EnsemblBacteria; ABS33225; ABS33225; CLB_3443.
DR   KEGG; cba:CLB_3443; -.
DR   HOGENOM; HOG000073580; -.
DR   KO; K03702; -.
DR   OMA; RYMHSEI; -.
DR   OrthoDB; 95696at2; -.
DR   BioCyc; CBOT441770:G1G96-3451-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    662       UvrABC system protein B.
FT                                /FTId=PRO_1000099541.
FT   DOMAIN       25    182       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      429    595       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      622    657       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   662 AA;  76217 MW;  1FD4227E7741CC74 CRC64;
     MNQFKVISKF NPTGDQPKAI KSIAKGIEKR EKFQTLIGVT GSGKTFTMAN IIEKVQKPTL
     VLAHNKTLAA QLCSEFREFF PNNAVEYFVS YYDYYQPEAY VAQSDTYIEK DASINDEIDK
     LRHSATSALF ERKDVIIVAS VSCIYGLGNP EEYKKLTISL REGMEKDRDE IIKKLVEIQY
     ERNDIDFSRG TFRVKGDVLD IFPASSSSKA VRVEFFGDEI DRIKEFDVLT GETITKLKHI
     SIFPASHFAT SKDRLEVAIK DIEEELEERV KELVSQDKIL EAQRLKQRTN FDIEMMREVG
     YCTGIENYSR VLDGRAKGTP PQTLLDYFPQ DFLLFIDESH VTLPQVKAMQ AGDKSRKDSL
     VEYGFRLPCA YDNRPLTFKE FENKLNQVVF VSATPAKYEL EYSTNTAEQV IRPTGLLDPE
     IIVKPVKGQI DDLYTSIQET IKRGFRILVT TLTKKMAEDL TDYLKEMGVK TRYLHSDIDT
     IERMKIIHDL RKGEFHVLVG INLLREGLDI PEVALVTILD ADKEGFLRSE TSLIQTVGRA
     ARNSESKVIM YGDVITKSME KTIKETNRRR KIQMEYNEEH GIVPKTIIKD IREVIQISDI
     AEERKEYDNL NEALKSYNND IDKLIEKYEE EMKEAAQNLQ FEKAAHLRDV IYKLKKDKET
     EL
//
DBGET integrated database retrieval system