UVRB_MYCGE
ID UVRB_MYCGE Reviewed; 656 AA.
AC P47319; Q49254; Q49446; Q49506;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 139.
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=MG073;
OS Mycoplasma genitalium (strain ATCC 33530 / DSM 19775 / NCTC 10195 / G37)
OS (Mycoplasmoides genitalium).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=243273;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=7569993; DOI=10.1126/science.270.5235.397;
RA Fraser C.M., Gocayne J.D., White O., Adams M.D., Clayton R.A.,
RA Fleischmann R.D., Bult C.J., Kerlavage A.R., Sutton G.G., Kelley J.M.,
RA Fritchman J.L., Weidman J.F., Small K.V., Sandusky M., Fuhrmann J.L.,
RA Nguyen D.T., Utterback T.R., Saudek D.M., Phillips C.A., Merrick J.M.,
RA Tomb J.-F., Dougherty B.A., Bott K.F., Hu P.-C., Lucier T.S.,
RA Peterson S.N., Smith H.O., Hutchison C.A. III, Venter J.C.;
RT "The minimal gene complement of Mycoplasma genitalium.";
RL Science 270:397-403(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-78; 102-231 AND 414-528.
RC STRAIN=ATCC 33530 / DSM 19775 / NCTC 10195 / G37;
RX PubMed=8253680; DOI=10.1128/jb.175.24.7918-7930.1993;
RA Peterson S.N., Hu P.-C., Bott K.F., Hutchison C.A. III;
RT "A survey of the Mycoplasma genitalium genome by using random sequencing.";
RL J. Bacteriol. 175:7918-7930(1993).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD10554.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L43967; AAC71291.1; -; Genomic_DNA.
DR EMBL; U01743; AAD10554.1; ALT_INIT; Genomic_DNA.
DR EMBL; U02119; AAD12393.1; -; Genomic_DNA.
DR EMBL; U01698; AAB01010.1; -; Genomic_DNA.
DR PIR; A64208; A64208.
DR RefSeq; WP_010869318.1; NC_000908.2.
DR AlphaFoldDB; P47319; -.
DR SMR; P47319; -.
DR STRING; 243273.MG_073; -.
DR EnsemblBacteria; AAC71291; AAC71291; MG_073.
DR KEGG; mge:MG_073; -.
DR eggNOG; COG0556; Bacteria.
DR HOGENOM; CLU_009621_2_1_14; -.
DR OMA; EYVDRMV; -.
DR OrthoDB; 95696at2; -.
DR BioCyc; MGEN243273:G1GJ2-85-MON; -.
DR Proteomes; UP000000807; 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:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:UniProtKB-UniRule.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 3.
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; Nucleotide-binding; Reference proteome; SOS response.
FT CHAIN 1..656
FT /note="UvrABC system protein B"
FT /id="PRO_0000138407"
FT DOMAIN 29..414
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 434..596
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 614..649
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT MOTIF 95..118
FT /note="Beta-hairpin"
FT BINDING 42..49
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT CONFLICT 45
FT /note="G -> A (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 102..107
FT /note="EAYLPS -> KLTYPD (in Ref. 2; AAD12393)"
FT /evidence="ECO:0000305"
FT CONFLICT 432..433
FT /note="DN -> IT (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 656 AA; 75202 MW; 59488ADF5D283493 CRC64;
MKNQTKSNSL FQLSTNYIPT GDQPEAIKKL SEFKTKQQVL LGATGTGKTF TIANVIQNSQ
LPTVVIAHNK TLAGQLFNEL KQLFPKNAVE YFISYFDFYQ PEAYLPSKGI YIEKSATVNE
AIKRLRVSTL HSLSTRKDVI VVGSVASIYP TSSPSDFVKY CLWFVVGKDY DLKTIKDRLV
SLNYVVNKQQ LTPGKFRFQG DVLEVFPGYS DAFVIRISFF DTKVEQICQI DPLTNKILNQ
LFEIKIGPAD EYVVNQSDLD IAIKNIKQEL QERVNYFNKQ NLVERAQRLA TITNHDLNDL
KAWGFCSGVE NYARHLELRM ANSTPYSIFD YFKGDWLLVI DESHQTLPQL NGMYNTDLSR
KQSLIDYGFR LPSALDNRPL SFAELQQKMQ KVIYVSATPR DKEISLSQNN VIEQLVRPTY
LVDPIIVVKP KDNQVEDLIE EIINQRQNNT RTFVTVLTIK MAENLTEYLK ERKIKVAYIH
KDIKALERLL LINDLRRGEY ECLVGINLLR EGLDVPEVAL VCIFDADIPG LPRDERSLIQ
IIGRAARNEH GRVVMYANHV TEQMQKAIDE TKRRRTVQME YNKLHNKTPK TVVKPLTFVQ
PIKLKAKSNA EKNAALIKQL TKEMKKAAAN QNYELAIEIR DSIFELEKEI GSKIKV
