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Database: UniProt
Entry: A9IR19
LinkDB: A9IR19
Original site: A9IR19 
ID   UVRB_BORPD              Reviewed;         675 AA.
AC   A9IR19;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   11-DEC-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}; OrderedLocusNames=Bpet2780;
OS   Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=340100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448;
RX   PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA   Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H.,
RA   Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA   Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA   Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA   Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T.,
RA   Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA   Martinez-Arias R.;
RT   "The missing link: Bordetella petrii is endowed with both the metabolic
RT   versatility of environmental bacteria and virulence traits of pathogenic
RT   Bordetellae.";
RL   BMC Genomics 9:449-449(2008).
CC   -!- FUNCTION: The UvrABC repair system catalyzes the recognition and
CC       processing of DNA lesions. A damage recognition complex composed of 2
CC       UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of
CC       the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps
CC       around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB
CC       and probably causes local melting of the DNA helix, facilitating
CC       insertion of UvrB beta-hairpin between the DNA strands. Then UvrB
CC       probes one DNA strand for the presence of a lesion. If a lesion is
CC       found the UvrA subunits dissociate and the UvrB-DNA preincision complex
CC       is formed. This complex is subsequently bound by UvrC and the second
CC       UvrB is released. If no lesion is found, the DNA wraps around the other
CC       UvrB subunit that will check the other stand for damage.
CC       {ECO:0000255|HAMAP-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; AM902716; CAP43122.1; -; Genomic_DNA.
DR   SMR; A9IR19; -.
DR   STRING; 94624.Bpet2780; -.
DR   EnsemblBacteria; CAP43122; CAP43122; Bpet2780.
DR   KEGG; bpt:Bpet2780; -.
DR   eggNOG; ENOG4105CCW; Bacteria.
DR   eggNOG; COG0556; LUCA.
DR   HOGENOM; HOG000073580; -.
DR   KO; K03702; -.
DR   OMA; TEYHQMI; -.
DR   Proteomes; UP000001225; 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; Cytoplasm; DNA damage; DNA excision; DNA repair;
KW   Excision nuclease; Helicase; Hydrolase; Nucleotide-binding;
KW   Reference proteome; SOS response.
FT   CHAIN           1..675
FT                   /note="UvrABC system protein B"
FT                   /id="PRO_1000099539"
FT   DOMAIN          35..192
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT   DOMAIN          439..605
FT                   /note="Helicase C-terminal"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT   DOMAIN          633..668
FT                   /note="UVR"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT   NP_BIND         48..55
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT   MOTIF           101..124
FT                   /note="Beta-hairpin"
SQ   SEQUENCE   675 AA;  75938 MW;  0CC38986C598EAF1 CRC64;
     MTAPGFVDFP DSPFHLYQPY PPAGDQPAAI EGLAQGMRDG LMYQTLLGVT GSGKTYTMAN
     IIARLGRPAL VLAPNKTLAA QLYAEMREFF PKNAVEYFVS YYDYYQPEAY VPTRDLFIEK
     DSSINEHIEQ MRLSATKSLL ERRDTVIVGT VSCIYGIGNP GDYHAMVLIL RAGDRISRRE
     VLARLVAMQY TRNDADFARG TFRVRGETLD IFPAESPELA LRLTLFDDEI ESLELFDPLT
     GRVRQKVPRF TVYPGSHYVT PRDTVLRAIE TIKEELRDRL KLLTAEGKLV EAQRLEQRTR
     FDLEMLQELG FCKGIENYSR HLSGAAPGEP PPTLIDYLPA DALMFIDESH VTMGQLGGMY
     RGDRARKETL VQYGFRLPSA LDNRPLRLEE FEARMRQCVF VSATPAAYEQ EHSDNVVEQV
     VRPTGLVDPQ VEVRPARTQV DDLLGEIKLR VAAQERVLVT TLTKRMAEDL TDFLAEHGVR
     VRYLHSDIDT VERVEIIRDL RLGTFDVLVG INLLREGLDI PEVSLVAILD ADKEGFLRSE
     RSLIQTIGRA ARNLNGHAIL YADAITASMR RAMDETERRR TKQLAFNAEH GITARGVNKA
     VRELIDGIVA PARHDTLESA IAPEVLADEK SVAREIRRLE KLMTDHARNL EFEQAAAARD
     ALNALKQRVL LDGAA
//
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