UVRB_MYCMO
ID UVRB_MYCMO Reviewed; 659 AA.
AC Q6KH72;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 104.
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=MMOB5720;
OS Mycoplasma mobile (strain ATCC 43663 / 163K / NCTC 11711) (Mesomycoplasma
OS mobile).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mesomycoplasma.
OX NCBI_TaxID=267748;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43663 / 163K / NCTC 11711;
RX PubMed=15289470; DOI=10.1101/gr.2674004;
RA Jaffe J.D., Stange-Thomann N., Smith C., DeCaprio D., Fisher S., Butler J.,
RA Calvo S., Elkins T., FitzGerald M.G., Hafez N., Kodira C.D., Major J.,
RA Wang S., Wilkinson J., Nicol R., Nusbaum C., Birren B., Berg H.C.,
RA Church G.M.;
RT "The complete genome and proteome of Mycoplasma mobile.";
RL Genome Res. 14:1447-1461(2004).
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}.
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DR EMBL; AE017308; AAT28058.1; -; Genomic_DNA.
DR RefSeq; WP_011265092.1; NC_006908.1.
DR AlphaFoldDB; Q6KH72; -.
DR SMR; Q6KH72; -.
DR STRING; 267748.MMOB5720; -.
DR EnsemblBacteria; AAT28058; AAT28058; MMOB5720.
DR KEGG; mmo:MMOB5720; -.
DR eggNOG; COG0556; Bacteria.
DR HOGENOM; CLU_009621_2_1_14; -.
DR OMA; EYVDRMV; -.
DR OrthoDB; 95696at2; -.
DR Proteomes; UP000009072; 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..659
FT /note="UvrABC system protein B"
FT /id="PRO_0000227329"
FT DOMAIN 27..414
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 432..594
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 624..659
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT MOTIF 93..116
FT /note="Beta-hairpin"
FT BINDING 40..47
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
SQ SEQUENCE 659 AA; 76420 MW; 021FA017096F38B0 CRC64;
MENKGFELVS TYKPTGDQPR AIQELIEGLE QNKKSQVLLG VTGSGKTFTI ANVIKAANRP
VLLLSHNKTL ASQLYSELKD FFPNNRVEYF VSYFDYYRPE AYMPNTDTYI DKTTKSNWDL
EEMRMSTLNS ISTKRDTIVV ASVASIYGAL KPKEYWSAFY NISIAQKISR KEFLLDLVQR
GYKRNNVASE PGSFNAKGDF VDIIPAWTKG FHIRVEFFGD EIEKISTIDS NNKITIEKFK
EYLIFPASAY TAPTGTIEAA VLRIREELHQ RLEYFEKEGK LLEKQRLEDR TRNDLESLEE
FGFCPGIENY SRHVDGRAEG EQPFTLFDYL PNDALLIIDE SHMMIPQLNG MYNGDRARKL
NLVNYGFRLP SALDNRPLQF HEFEKYEFQK IYISATPSDY EINQAHGEIV KQIIRPTGLL
DPLIEIRREQ NQVEDMFDEI QKQKAKKQRT LILATTKKVS EELTRYFQEK KEKVAYIHSD
YTTFERNEIL RKLRKGVYDT VIGINLLREG IDLPEVSLIM VLDANKESFF RSKKSLIQIV
GRAARNVNGR VIFYANNISK SMEETIYDNL DKRKIQMDYN KKHNIIPKTI IKPITEAIED
KKLNESLISF MSHSKTKKSI KEKEALVKDL RNQMLDASKQ LNFERAAELR DIILELEAN
