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Database: UniProt
Entry: P58174
LinkDB: P58174
Original site: P58174 
ID   UVRB_MYCPU              Reviewed;         657 AA.
AC   P58174;
DT   20-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   20-JUN-2001, sequence version 1.
DT   31-JUL-2019, entry version 115.
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=MYPU_0960;
OS   Mycoplasma pulmonis (strain UAB CTIP).
OC   Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX   NCBI_TaxID=272635;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAB CTIP;
RX   PubMed=11353084; DOI=10.1093/nar/29.10.2145;
RA   Chambaud I., Heilig R., Ferris S., Barbe V., Samson D., Galisson F.,
RA   Moszer I., Dybvig K., Wroblewski H., Viari A., Rocha E.P.C.,
RA   Blanchard A.;
RT   "The complete genome sequence of the murine respiratory pathogen
RT   Mycoplasma pulmonis.";
RL   Nucleic Acids Res. 29:2145-2153(2001).
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; AL445563; CAC13269.1; -; Genomic_DNA.
DR   PIR; H90523; H90523.
DR   RefSeq; WP_010924900.1; NC_002771.1.
DR   SMR; P58174; -.
DR   STRING; 272635.MYPU_0960; -.
DR   PRIDE; P58174; -.
DR   EnsemblBacteria; CAC13269; CAC13269; CAC13269.
DR   KEGG; mpu:MYPU_0960; -.
DR   eggNOG; ENOG4105CCW; Bacteria.
DR   eggNOG; COG0556; LUCA.
DR   HOGENOM; HOG000073580; -.
DR   KO; K03702; -.
DR   OMA; RYMHSEI; -.
DR   OrthoDB; 95696at2; -.
DR   BioCyc; MPUL272635:G1GT6-95-MONOMER; -.
DR   Proteomes; UP000000528; 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:ATPase 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   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; Nucleotide-binding; Reference proteome;
KW   SOS response.
FT   CHAIN         1    657       UvrABC system protein B.
FT                                /FTId=PRO_0000138410.
FT   DOMAIN       23    412       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      428    581       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      621    656       UVR. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   NP_BIND      36     43       ATP. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   MOTIF        89    112       Beta-hairpin.
SQ   SEQUENCE   657 AA;  76354 MW;  B9B2166809870554 CRC64;
     MFKLHSNYSP SGDQPRAIQE LAEDIEKNKK HLVLQGVTGS GKTFTIANLI AKFNRTTLVL
     SHNKTLASQL YSELKEFFPE NRVEYFVSYF DFYRPEAYLP STDTYIDKTS KTNNELDAMR
     MSSLNALLTR KDTIVVSSVA AIYGAFNPQE YQKNFFSIEV GQELKRKDFF LDLVKRHYKR
     NDVNLVPGSF SAKGDVVEIA PAWTSDFAIR VEFFGDEIEA IATIDPLNKT LKKRHKNYLI
     FPANAYSTNK DIVSRVVLQV KEELIDRLDY FEKNNKLLEM QRLEQRVKSD MDSLEEFGIC
     SGIENYARYI DGREQGEKPY TLLDYLPEEA LVFIDESHMM VPQLNAMFNG DRSRKQNLVD
     YGFRLPSALD NRPLTFSEFE EYKFPKIYIS ATPSEYEIEK ADQKITKMII RPTGLLDPII
     ETRSKTNQVE DIYDELQKQK AKNERTLILT TTKRFSEELT RYFQEKGEKV AYIHSDHKTF
     ERNEILRKLR KGVYDLVIGI NLLREGIDLP EVSLVIILDA DKESFLRNTK SLIQIVGRAS
     RNSSGKVIFY ADFVSKSMRE TIEDNFEKRQ IQIQYNKEHG IVPQTIIKDI PEPIEGHGFE
     HSIEYFLSNE KKSKAQLKEK EKLILDLKKQ MLEASQKMNY ERAIHLRDLL IELGEKL
//
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