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Database: UniProt
Entry: A0PP48
LinkDB: A0PP48
Original site: A0PP48 
ID   UVRB_MYCUA              Reviewed;         701 AA.
AC   A0PP48;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   09-JAN-2007, sequence version 1.
DT   31-JUL-2019, entry version 84.
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=MUL_1616;
OS   Mycobacterium ulcerans (strain Agy99).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=362242;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Agy99;
RX   PubMed=17210928; DOI=10.1101/gr.5942807;
RA   Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA   Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L.,
RA   Ryan J., Johnson P.D.R., Davies J.K., Jenkin G.A., Small P.L.C.,
RA   Jones L.M., Tekaia F., Laval F., Daffe M., Parkhill J., Cole S.T.;
RT   "Reductive evolution and niche adaptation inferred from the genome of
RT   Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL   Genome Res. 17:192-200(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; CP000325; ABL04117.1; -; Genomic_DNA.
DR   SMR; A0PP48; -.
DR   STRING; 362242.MUL_1616; -.
DR   EnsemblBacteria; ABL04117; ABL04117; MUL_1616.
DR   KEGG; mul:MUL_1616; -.
DR   HOGENOM; HOG000073580; -.
DR   KO; K03702; -.
DR   OMA; RYMHSEI; -.
DR   Proteomes; UP000000765; 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    701       UvrABC system protein B.
FT                                /FTId=PRO_1000077907.
FT   DOMAIN       28    188       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      432    598       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      656    691       UVR. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   NP_BIND      41     48       ATP. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   MOTIF        94    117       Beta-hairpin.
SQ   SEQUENCE   701 AA;  78352 MW;  A4F13DAB3A99BA24 CRC64;
     MRTGASFEVI SPHDPAGDQP AAINELERRI RAGERDVVLL GATGTGKSAT TAWLIERLQR
     PTLVMAPNKT LAAQLANELR EMLPHNAVEY FVSYYDYYQP EAYIAQTDTY IEKDSSINDD
     VERLRHSATS ALLSRRDVVV VASVSCIYGL GTPQSYLDRS VELQVGTDVP RDGLLRLLVD
     VQYTRNDLSF TRGSFRVRGD TVEIIPSYED LAVRIEFFGD GIEALYYLHP LTGDVVRQVD
     SLRIFPATHY VAGPERMAQA ISTIEEELAE RLAELEGHGK LLEAHRLRMR TNYDIEMMRQ
     VGFCSGIENY SRHIDGRPAG SAPATLLDYF PEDFLLVIDE SHVTVPQIGG MYEGDISRKR
     NLVEFGFRLP SAVDNRPLQW EEFADRIGQT VYLSATPGPY ELSQSGGEFV EQVIRPTGLV
     DPKVVVKPTK GQIDDLIGEI RQRAEVDQRV LVTTLTKKMA EDLTDYLLEM GIRVRYLHSE
     VDTLRRVELL RQLRLGEYDV LVGINLLREG LDLPEVSLVA ILDADKEGFL RSARSLIQTI
     GRAARNVSGE VHMYADKITD SMKEAIDETE RRRAKQVAYN EANGIDPQPL RKKIADILDQ
     VYREADDTEA AESVPIGGSG RNSSRGRRAQ GEPGRAVSAG VFEGRDTSTM PRAELADLIK
     DLTSQMMVAA RDLQFELAAR FRDEIADLKK ELRGMDAAGL N
//
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