GenomeNet

Database: UniProt
Entry: A3N031
LinkDB: A3N031
Original site: A3N031 
ID   UVRB_ACTP2              Reviewed;         673 AA.
AC   A3N031;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   03-APR-2007, sequence version 1.
DT   13-NOV-2019, entry version 86.
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=APL_0667;
OS   Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=416269;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L20;
RX   PubMed=18065534; DOI=10.1128/jb.01845-07;
RA   Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA   Nash J.H.E.;
RT   "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT   (serotype 5b).";
RL   J. Bacteriol. 190:1495-1496(2008).
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; CP000569; ABN73767.1; -; Genomic_DNA.
DR   RefSeq; WP_009874701.1; NC_009053.1.
DR   SMR; A3N031; -.
DR   STRING; 416269.APL_0667; -.
DR   PRIDE; A3N031; -.
DR   EnsemblBacteria; ABN73767; ABN73767; APL_0667.
DR   GeneID; 4849100; -.
DR   KEGG; apl:APL_0667; -.
DR   PATRIC; fig|416269.6.peg.698; -.
DR   eggNOG; ENOG4105CCW; Bacteria.
DR   eggNOG; COG0556; LUCA.
DR   HOGENOM; HOG000073580; -.
DR   KO; K03702; -.
DR   OMA; RYMHSEI; -.
DR   BioCyc; APLE416269:G1G87-699-MONOMER; -.
DR   Proteomes; UP000001432; Chromosome.
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; Complete proteome; Cytoplasm; DNA damage; DNA excision;
KW   DNA repair; Excision nuclease; Helicase; Hydrolase;
KW   Nucleotide-binding; SOS response.
FT   CHAIN         1    673       UvrABC system protein B.
FT                                /FTId=PRO_1000077862.
FT   DOMAIN       29    188       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      434    600       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      634    669       UVR. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   NP_BIND      42     49       ATP. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   MOTIF        95    118       Beta-hairpin.
SQ   SEQUENCE   673 AA;  76678 MW;  9B1241721972051C CRC64;
     MSKQGKPFIL HSPFKPSGDQ PSAIAKLTEG LNDGLAHQTL LGVTGSGKTF TIANVIAQLN
     RPAMLLAPNK TLAAQLYAEM KAFFPENAVE YFVSYYDYYQ PEAYVPSSDT FIEKDASINE
     QIEQMRLSAT KSFLERRDTI VVASVSAIYG LGDVDAYMQM MLHLQLGAII DQREILARLA
     ELQYTRNDQA FQRSTFRVRG EVIDIFPAES DEIALRVELF DDEIESLSLF DPLTGHSLGK
     VPRYTIYPKT HYVTPRERIL NAIEEIKQEL VERREYFIKE NKLLEEQRIT QRTQFDIEMM
     NELGYCSGIE NYSRYLSGRK EGEPPPTLFD YMPADGLLII DESHVTVPQI GGMYRGDRAR
     KETLVQYGFR LPSALDNRPL RFEEFERLAP QTIYVSATPG NYELEKSNGD VVDQVVRPTG
     LLDPIIEVRP VATQVDDVLS EIHKRVAVDE RVLITTLTKK MAEDLTDYLD EHGVRVRYLH
     SDIDTVERVE IIHDLRMGMF DVLVGINLLR EGLDMPEVSL VAILDADKEG FLRSERSLIQ
     TIGRAARNLN GKAILYGDRI TNSMQKAITE TERRREKQQK YNEEHGITPQ ALNKKVGELL
     DIGQTDKPKR GKQAVKVEEK SANTYKPKSR KELEKELKQL EQQMRDFAKD LEFEKAAAVR
     DKIGQLKAVL LEV
//
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