ID UVRB_MYCMS Reviewed; 671 AA.
AC Q6MS38;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 111.
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=MSC_0944;
OS Mycoplasma mycoides subsp. mycoides SC (strain PG1).
OC Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272632;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PG1;
RX PubMed=14762060; DOI=10.1101/gr.1673304;
RA Westberg J., Persson A., Holmberg A., Goesmann A., Lundeberg J.,
RA Johansson K.-E., Pettersson B., Uhlen M.;
RT "The genome sequence of Mycoplasma mycoides subsp. mycoides SC type strain
RT PG1T, the causative agent of contagious bovine pleuropneumonia (CBPP).";
RL Genome Res. 14:221-227(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; BX293980; CAE77553.1; -; Genomic_DNA.
DR RefSeq; NP_975911.1; NC_005364.2.
DR AlphaFoldDB; Q6MS38; -.
DR SMR; Q6MS38; -.
DR STRING; 272632.MSC_0944; -.
DR KEGG; mmy:MSC_0944; -.
DR PATRIC; fig|272632.4.peg.1026; -.
DR eggNOG; COG0556; Bacteria.
DR HOGENOM; CLU_009621_2_1_14; -.
DR Proteomes; UP000001016; 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 CDD; cd17916; DEXHc_UvrB; 1.
DR CDD; cd18790; SF2_C_UvrB; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 3.
DR Gene3D; 4.10.860.10; UVR domain; 1.
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 NCBIfam; TIGR00631; uvrb; 1.
DR PANTHER; PTHR24029; UVRABC SYSTEM PROTEIN B; 1.
DR PANTHER; PTHR24029:SF0; UVRABC SYSTEM PROTEIN B; 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; C-terminal UvrC-binding domain of UvrB; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
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..671
FT /note="UvrABC system protein B"
FT /id="PRO_0000227330"
FT DOMAIN 35..423
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 440..602
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 632..667
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT MOTIF 101..124
FT /note="Beta-hairpin"
FT BINDING 48..55
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
SQ SEQUENCE 671 AA; 77354 MW; FF1E901406FA297E CRC64;
MLWEKVMFIA NNKYKLVTKY KPSGDQNQAI EKLNKAIIEN KKHQVLLGAT GTGKTFTIAN
IIAKHNKQAL VIAHNKTLAM QLYYELKEMF PENRVEYFVS NFDFFQPEAY IPSKDLYIDK
DSRQNMELDM MRLSACNALL TRNDTIVVAS VAALFALQNP LEYSSAFIEL KVGQKIKRNE
LLTWLVRSGY TRNDIENQLG SFSAKGDVVK IVPGWVNNIM FRISLFDDEI ESIHTLNTIT
NSILDNITTV TIHPAQSYIT PQDKLKTICN NIRNELVQRL AELQSENKLL EAQRLEQRTK
YDLESLEEFG FCSGIENYSS HLDFRSKGQR PYVLLDYFNN DFITIVDESH ITLPQIRGMY
NTDRSRKLTL VEYGFRLPSA LDNRPLNFDE FNSLIKQVIY TSATPGDYEL DLVNHQVVQQ
IIRPTGLLDP QIEIRKTTNQ IDDIINEIHL RKLQNERVFI TTLTIRMSED LTAFLQEKNI
KVAYLHSELK TLERSEILND LRKGVYDVVV GVNLLREGLD LPEVSLVCIL DADKQGFLRN
YRSLIQTIGR VARNVNGKAI MYADTVSQAM DEAIKETNRR RKIQEEFNKK HNIVPKTISK
AISESILSEQ TKKTLAKAKK IKDKKQKLQT IQQTIDNLRQ EMLQAAKELD FERAAILRDT
IIELENEKNT N
//
