ID UVRB_MYCPN Reviewed; 657 AA.
AC P75558;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 27-MAR-2024, entry version 132.
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=MPN_211;
GN ORFNames=MP620;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129 / Subtype 1)
OS (Mycoplasmoides pneumoniae).
OC Bacteria; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC Mycoplasmoides.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129 / Subtype 1;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
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 ---------------------------------------------------------------------------
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; U00089; AAB96268.1; -; Genomic_DNA.
DR PIR; S73946; S73946.
DR RefSeq; NP_109899.1; NC_000912.1.
DR RefSeq; WP_010874568.1; NZ_OU342337.1.
DR AlphaFoldDB; P75558; -.
DR SMR; P75558; -.
DR IntAct; P75558; 1.
DR STRING; 272634.MPN_211; -.
DR EnsemblBacteria; AAB96268; AAB96268; MPN_211.
DR GeneID; 66609143; -.
DR KEGG; mpn:MPN_211; -.
DR PATRIC; fig|272634.6.peg.230; -.
DR HOGENOM; CLU_009621_2_1_14; -.
DR OrthoDB; 9806651at2; -.
DR BioCyc; MPNE272634:G1GJ3-341-MONOMER; -.
DR Proteomes; UP000000808; 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..657
FT /note="UvrABC system protein B"
FT /id="PRO_0000138409"
FT DOMAIN 29..416
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 435..597
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 615..650
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"
SQ SEQUENCE 657 AA; 75193 MW; 5D367BEFB3F04618 CRC64;
MKSPTKDSKL FHLKSNFAPT GDQPAAIAKL AEFQTNEQVL LGATGTGKTF TIANVIQKVQ
LPTVVIAHNK TLAGQLYQEL KELFPNNAVE YFISYFDFYQ PEAYLPAKGV YIEKSATVNE
EIKRLRVSTL HSLSTRKDVI VVGSVASIYP TSSPADFAQY SLWLVVGKEY GLSELKTQLI
HLNYVVNKQQ LTPGKFRFQG DVVEVFPGYA QDYVLRLSFF DQQLEQIARI DPLTNKVLET
LNSFKLGPAD EYIVNQNDLG VALDTIKAEL KDRLKYFERL NFPERAQRLQ TITEHDLADL
KAWGVCSGVE NYARHLEHRP PHSKPYNIFD YFTKGEWLLV VDESHQTLPQ IKGMYNTDIS
RKQSLIEYGF RLPSALDNRP LSYEEFRQGI NKVIYVSATP REEEIQLSHN NVVEQLVRPT
YLLDPEVIVK PKDNQVEDLV SEIINQRKHN GRTFVTVLTI KMAENLTDFL KERNIKVAYI
HKDIKALERL ILLTDLRKGE YECLVGINLL REGLDVPEVS LVAIFDADIP GLPRDERSLI
QIIGRAARNV HGRVIMYANT ISEQMDKAIK ETQRRRTIQM AYNEQHHKTP MTVQKPITLN
QPIKLKTKSS EQQKAALIKQ LTKEMKQAAA NQNYELAIEI RDSIFELEKQ FRGKIKS
//
