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Database: UniProt
Entry: Q5X0E6
LinkDB: Q5X0E6
Original site: Q5X0E6 
ID   UVRB_LEGPL              Reviewed;         663 AA.
AC   Q5X0E6;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   31-JUL-2019, entry version 97.
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=lpl0074;
OS   Legionella pneumophila (strain Lens).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=297245;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lens;
RX   PubMed=15467720; DOI=10.1038/ng1447;
RA   Cazalet C., Rusniok C., Brueggemann H., Zidane N., Magnier A., Ma L.,
RA   Tichit M., Jarraud S., Bouchier C., Vandenesch F., Kunst F.,
RA   Etienne J., Glaser P., Buchrieser C.;
RT   "Evidence in the Legionella pneumophila genome for exploitation of
RT   host cell functions and high genome plasticity.";
RL   Nat. Genet. 36:1165-1173(2004).
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; CR628337; CAH14304.1; -; Genomic_DNA.
DR   RefSeq; WP_011214362.1; NC_006369.1.
DR   SMR; Q5X0E6; -.
DR   EnsemblBacteria; CAH14304; CAH14304; lpl0074.
DR   KEGG; lpf:lpl0074; -.
DR   LegioList; lpl0074; -.
DR   HOGENOM; HOG000073580; -.
DR   KO; K03702; -.
DR   OMA; TEYHQMI; -.
DR   Proteomes; UP000002517; 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; SOS response.
FT   CHAIN         1    663       UvrABC system protein B.
FT                                /FTId=PRO_0000227324.
FT   DOMAIN       26    414       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      430    596       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      624    659       UVR. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   NP_BIND      39     46       ATP. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   MOTIF        92    115       Beta-hairpin.
SQ   SEQUENCE   663 AA;  75620 MW;  8D70FD36703CA543 CRC64;
     MKDLFKIYSN YQPAGDQPTA IASLIDGLES GLAKQTLLGV TGSGKTFTIA HVIQAMKRPT
     LIMAPNKTLA AQLYGEFKAF FPDNAVEYFV SYYDYYQPEA YVPASDTFIE KDASINEHIE
     QMRLSATKAL IERKDAIIVA TVSAIYGLGD PDSYLRMLLH LSRGEQSDQR KILKRLAEMQ
     YTRTNLSLER GQFRVNGDVI DIFPADSEKE AIRIELFDDE VDNIARFDPL TGEILQRLPR
     VTIFPKTHYV TPRERILETV EKVKVELQER LAELNAQNKL VEAQRLEQRT CFDIEMMLEL
     GYCSGIENYS RYLSNREAGE APPTLFDYLP PEALLIIDES HVTVPQIGGM YRGDRARKET
     LVNYGFRLPS ALDNRPLRFE EFEERSPQTI YISATPGPYE QEHSDNVAEQ VVRPTGLIDP
     EVEIRPVKTQ VDDLMSEIRQ VIAQGSRILV TTLTKRMAED LTEYLSEHGI KVRYLHSDVD
     TVERMEIIRD LRLGEFDVLV GINLLREGLD MPEVALVAIL DADKEGFLRS ERSLIQTIGR
     AARNVKGRAI LYADNITGSM QRALTETERR REKQKAFNLK HGITPKGINK SVEDILEGAY
     IGKRKTMVAE QAPRYTHWSP QELAKQINAL EKQMYAHAQN MEFELAAKIR DEYLLLKEQL
     MKI
//
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