(data stored in ACNUC7421 zone)

SWISSPROT: UVRB_LEGPC

ID   UVRB_LEGPC              Reviewed;         663 AA.
AC   A5I9P3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-JUN-2007, sequence version 1.
DT   11-DEC-2019, entry version 82.
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=LPC_0094;
OS   Legionella pneumophila (strain Corby).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales;
OC   Legionellaceae; Legionella.
OX   NCBI_TaxID=400673;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Corby;
RA   Gloeckner G., Albert-Weissenberger C., Weinmann E., Jacobi S., Schunder E.,
RA   Steinert M., Buchrieser C., Hacker J., Heuner K.;
RT   "Identification and characterization of a new conjugation/ type IVA
RT   secretion system (trb/tra) of L. pneumophila Corby localized on a mobile
RT   genomic island.";
RL   Submitted (NOV-2006) to the EMBL/GenBank/DDBJ databases.
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}.
DR   EMBL; CP000675; ABQ54093.1; -; Genomic_DNA.
DR   RefSeq; WP_011945277.1; NC_009494.2.
DR   SMR; A5I9P3; -.
DR   PRIDE; A5I9P3; -.
DR   EnsemblBacteria; ABQ54093; ABQ54093; LPC_0094.
DR   KEGG; lpc:LPC_0094; -.
DR   HOGENOM; HOG000073580; -.
DR   KO; K03702; -.
DR   OMA; TEYHQMI; -.
DR   BioCyc; LPNE400673:LPC_RS00430-MONOMER; -.
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:0003677; F:DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0009381; F:excinuclease ABC activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
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; 2.
DR   PROSITE; PS51194; HELICASE_CTER; 1.
DR   PROSITE; PS50151; UVR; 1.
PE   3: Inferred from homology;
DR   PRODOM; A5I9P3.
DR   SWISS-2DPAGE; A5I9P3.
KW   ATP-binding; Cytoplasm; DNA damage; DNA excision; DNA repair;
KW   Excision nuclease; Helicase; Hydrolase; Nucleotide-binding; SOS response.
FT   CHAIN           1..663
FT                   /note="UvrABC system protein B"
FT                   /id="PRO_1000077901"
FT   DOMAIN          26..183
FT                   /note="Helicase ATP-binding"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT   DOMAIN          430..596
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   NP_BIND         39..46
FT                   /note="ATP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT   MOTIF           92..115
FT                   /note="Beta-hairpin"
SQ   SEQUENCE   663 AA;  75637 MW;  D11E71BA46CE933E CRC64;
     MKDLFKIYSN YQPAGDQPTA IASLIDGLES GLAKQTLLGV TGSGKTFTIA HVIQAMKRPT
     LIMAPNKTLA AQLYGEFKAF FPDNAVEYFV SYYDYYQPEA YVPASDTFIE KDASINEHIE
     QMRLSATKAL IERKDAIIVA TVSAIYGLGD PDSYLRMLLH LSRGEQSDQR KILKRLAEMQ
     YTRTNLSLER GQFRVHGDVI DIFPADSEKE AIRIELFDDE VDNIARFDPL TGEILQRLPR
     VTIFPKTHYV TPRERILETV EKVKAELQER LAELNAQNKL VEAQRLEQRT CFDIEMMLEL
     GYCSGIENYS RYLSNREAGE APPTLFDYLP PDALLIIDES HVTVPQIGGM YRGDRARKET
     LVNYGFRLPS ALDNRPLRFE EFEERSPQTI YISATPGPYE QEHSDNVAEQ VVRPTGLIDP
     EVEIRPVKTQ VDDLMSEIRQ VIAQGSRILV TTLTKRMAED LTEYLSEHGI KVRYLHSDVD
     TVERMEIIRD LRLGEFDVLV GINLLREGLD MPEVALVAIL DADKEGFLRS ERSLIQTIGR
     AARNVKGRAI LYADTMTGSM QRALMETERR REKQKAFNLK HGITPKGINK SVEDILEGAY
     IGKRKTMVAE QAPRYTHWSP QELAKQINAL EKQMYAHAQN MEFELAAKIR DEYLLLKEQL
     MKI
//

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