ID   A1IGB7_PHOPO            Unreviewed;       675 AA.
AC   A1IGB7;
DT   06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2007, sequence version 1.
DT   16-APR-2014, entry version 42.
DE   RecName: Full=UvrABC system protein B;
DE            Short=Protein UvrB;
DE   AltName: Full=Excinuclease ABC subunit B;
GN   Name=uvrB;
OS   Photobacterium phosphoreum.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales;
OC   Vibrionaceae; Photobacterium.
OX   NCBI_TaxID=659;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=IFO 13896;
RA   Kasai S.;
RT   "Identification of luxO in Photobacterium phosphoreum IFO 13896.";
RL   Submitted (JAN-2003) to the EMBL/GenBank/DDBJ databases.
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 UVR domain.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -!- SIMILARITY: Contains UVR domain.
CC   -!- SIMILARITY: Contains helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains helicase C-terminal domain.
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DR   EMBL; AB101000; BAF43690.1; -; Genomic_DNA.
DR   ProteinModelPortal; A1IGB7; -.
DR   SMR; A1IGB7; 5-597.
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; Cytoplasm; DNA damage; DNA excision; DNA repair;
KW   Excision nuclease; Helicase; Hydrolase; Nucleotide-binding;
KW   SOS response.
FT   DOMAIN       26    181       Helicase ATP-binding (By similarity).
FT   DOMAIN      432    598       Helicase C-terminal (By similarity).
FT   DOMAIN      635    670       UVR (By similarity).
FT   NP_BIND      39     46       ATP (By similarity).
FT   MOTIF        92    115       Beta-hairpin (By similarity).
SQ   SEQUENCE   675 AA;  76639 MW;  4F58FAA7DD96A344 CRC64;
     MSKLFNLVSD YSPAGDQPTA IEQLMDGLDS GLAQQTLLGV TGSGKTFTIA NVIAQANRPT
     LIMAPNKTLA AQLYGEMRDF FPDNAVEYFV SYYDYYQPEA YVPTTDTFIE KDASVNAHIE
     QMRLSATKAL MERRDVIIIA SVSAIYGLGD PESYLKMMLH VRRGDVLDQR DILRRLAELQ
     YKRNDAVFER GTFRVRGEVI DIFPAESEKE AIRLELFDGE VEVISSFDPL TGAIIQRNLA
     RTTIYPKTHY VTPREKILDA IEGIKLELTQ RKQQLLDNNK LVEEQRISQR TQFDIEMMNE
     LGFCSGIENY SRYLSGRTEG EPPPTLFDYL PADGLLIIDE SHVTVSQIGA MFRGDRSRKE
     NLVEYGFRLP SALDNRPMKF EEFESLAPQT IYVSATPGNY EIEKSGGDIA EQVVRPTGLL
     DPEIEVRPVA TQVDDLLSEI HIRSAKQERV LVTTLTKRMS EDLTEYLTEH GVKVRYLHSD
     IDTVERVEII RDLRLGKFDV LVGINLLREG LDIPEVSLVA ILDADKEGFL RSERSLIQTM
     GRAARNIEGK AILYGDRITG SMERAINETQ RRREKQIIYN LEHNIIPQKL NKKIGDLLEL
     GAPSGRSKSR NKAADLHKVA ESKGTYSVLT PQQLELEIQR LEKQMYDFAQ NLEFEQAADT
     RDKIHQLRQQ FIANS
//