GenomeNet

Database: UniProt/TrEMBL
Entry: Q740L5_MYCPA
LinkDB: Q740L5_MYCPA
Original site: Q740L5_MYCPA 
ID   Q740L5_MYCPA            Unreviewed;       722 AA.
AC   Q740L5;
DT   05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2004, sequence version 1.
DT   01-MAY-2013, entry version 70.
DE   RecName: Full=UvrABC system protein B;
DE            Short=Protein UvrB;
DE   AltName: Full=Excinuclease ABC subunit B;
GN   Name=uvrB; OrderedLocusNames=MAP_1335;
OS   Mycobacterium paratuberculosis (strain ATCC BAA-968 / K-10).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC   Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D.,
RA   Banerji N., Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
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 (By similarity).
CC   -!- SUBUNIT: Forms a heterotetramer with UvrA during the search for
CC       lesions. Interacts with UvrC in an incision complex (By
CC       similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC   -!- DOMAIN: The beta-hairpin motif is involved in DNA binding (By
CC       similarity).
CC   -!- SIMILARITY: Belongs to the UvrB family.
CC   -!- SIMILARITY: Contains 1 UVR domain.
CC   -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC   -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution-NoDerivs License
CC   -----------------------------------------------------------------------
DR   EMBL; AE016958; AAS03652.1; -; Genomic_DNA.
DR   RefSeq; NP_960269.1; NC_002944.2.
DR   ProteinModelPortal; Q740L5; -.
DR   STRING; 262316.MAP1335; -.
DR   EnsemblBacteria; AAS03652; AAS03652; MAP_1335.
DR   GeneID; 2720724; -.
DR   KEGG; mpa:MAP1335; -.
DR   PATRIC; 17995157; VBIMycAvi108102_1408.
DR   KO; K03702; -.
DR   OMA; CIYGLGI; -.
DR   ProtClustDB; PRK05298; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR   GO; GO:0003677; F:DNA binding; IEA:HAMAP.
DR   GO; GO:0009381; F:excinuclease ABC activity; IEA:HAMAP.
DR   GO; GO:0004386; F:helicase activity; IEA:HAMAP.
DR   GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR   GO; GO:0006289; P:nucleotide-excision repair; IEA:HAMAP.
DR   GO; GO:0009432; P:SOS response; IEA:HAMAP.
DR   Gene3D; 4.10.860.10; -; 1.
DR   HAMAP; MF_00204; UvrB; 1; -.
DR   InterPro; IPR006935; Helicase/UvrB_dom.
DR   InterPro; IPR014001; Helicase_ATP-bd.
DR   InterPro; IPR001650; Helicase_C.
DR   InterPro; IPR001943; UVR_dom.
DR   InterPro; IPR004807; UvrB.
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   SMART; SM00487; DEXDc; 1.
DR   SMART; SM00490; HELICc; 1.
DR   SUPFAM; SSF46600; UvrB_C; 1.
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; Helicase; Hydrolase;
KW   Nucleotide-binding; SOS response.
FT   DOMAIN       53    213       Helicase ATP-binding (By similarity).
FT   DOMAIN      457    623       Helicase C-terminal (By similarity).
FT   DOMAIN      677    712       UVR (By similarity).
FT   NP_BIND      66     73       ATP (By similarity).
FT   MOTIF       119    142       Beta-hairpin (By similarity).
SQ   SEQUENCE   722 AA;  80921 MW;  208339B4571069BC CRC64;
     MAFATEHPVV AHSEYRPAEE AVEGLVRAGG RFEVVSPHAP AGDQPAAIDE LERRIRAGER
     DVVLLGATGT GKSATTAWLI ERLQRPTLVM APNKTLAAQL ANELREMLPH NAVEYFVSYY
     DYYQPEAYIA QTDTYIEKDS SINDDVERLR HSATSSLLSR RDVVVVASVS CIYGLGTPQS
     YLDRSVELRV GTEVPRDALL RLLVDVQYTR NDLSFTRGSF RVRGDTVEII PSYEELAVRI
     EFFGDEIEAL YYLHPLTGDV IRQVDSLRIF PATHYVAGPE RMAHAISTIE QELAERLAEL
     EGQGKLLEAQ RLRMRTNYDI EMMRQVGFCS GIENYSRHID GRGPGSPPAT LLDYFPEDFL
     LVIDESHVTV PQIGGMYEGD MSRKRNLVEY GFRLPSACDN RPLTWEEFAD RIGQTVYLSA
     TPGPYELSQT GGEFVEQVIR PTGLVDPKVV VKPTKGQIDD LIGEIRKRTE ADERVLVTTL
     TKKMAEDLTD YLLEMGIRVR YLHSEVDTLR RVELLRQLRL GEYDVLVGIN LLREGLDLPE
     VSLVAILDAD KEGFLRSARS LIQTIGRAAR NVSGEVHMYA DTITESMKEA IDETERRRAK
     QIAYNEAHGI DPQPLRKKIA DILDQVYREA DDTDTVEIGS GRSMSRGRRA QGEPGRAVSA
     GIVEGRDTTN MPRAELADLI KDLTAQMMAA ARDLQFELAA RFRDEIADLK KELRGMDAAG
     LK
//
DBGET integrated database retrieval system