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Database: UniProt
Entry: A0JWN0
LinkDB: A0JWN0
Original site: A0JWN0 
ID   UVRB_ARTS2              Reviewed;         693 AA.
AC   A0JWN0;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   12-DEC-2006, sequence version 1.
DT   31-JUL-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};
GN   OrderedLocusNames=Arth_2070;
OS   Arthrobacter sp. (strain FB24).
OC   Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Arthrobacter.
OX   NCBI_TaxID=290399;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FB24;
RX   PubMed=24501649; DOI=10.4056/sigs.4438185;
RA   Nakatsu C.H., Barabote R., Thompson S., Bruce D., Detter C.,
RA   Brettin T., Han C., Beasley F., Chen W., Konopka A., Xie G.;
RT   "Complete genome sequence of Arthrobacter sp. strain FB24.";
RL   Stand. Genomic Sci. 9:106-116(2013).
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; CP000454; ABK03450.1; -; Genomic_DNA.
DR   RefSeq; WP_011691916.1; NC_008541.1.
DR   SMR; A0JWN0; -.
DR   STRING; 290399.Arth_2070; -.
DR   PRIDE; A0JWN0; -.
DR   EnsemblBacteria; ABK03450; ABK03450; Arth_2070.
DR   KEGG; art:Arth_2070; -.
DR   eggNOG; ENOG4105CCW; Bacteria.
DR   eggNOG; COG0556; LUCA.
DR   HOGENOM; HOG000073580; -.
DR   KO; K03702; -.
DR   OMA; RYMHSEI; -.
DR   OrthoDB; 95696at2; -.
DR   Proteomes; UP000000754; 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: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; 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; Reference proteome; SOS response.
FT   CHAIN         1    693       UvrABC system protein B.
FT                                /FTId=PRO_1000077865.
FT   DOMAIN       35    188       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      438    604       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      648    683       UVR. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   NP_BIND      48     55       ATP. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   MOTIF       101    124       Beta-hairpin.
SQ   SEQUENCE   693 AA;  77898 MW;  C0CE374BE886F540 CRC64;
     MSLAQEINRV VAPFEVISEF KPAGDQPAAI AELTERIKNG EKDVVLLGAT GTGKSATTAW
     LIEQVQRPTL VMVQNKTLAA QLANEFRELL PNNAVEYFVS YYDYYQPEAY VAQTDTFIEK
     DSSVNEEVER LRHSATNALL TRRDVIVVAT VSCIYGLGTP EEYIAGMVTL RKGAEMNRDD
     LLRKFVSMQY ARNDMDFHRG TFRVRGDTVE IIPMYEELAI RIEFFGDEIE NIHTLHPLTG
     EVIRDEEEMY VFPASHYVAG PERMSRAIKR IEDELAERLQ VLESQNKLVE AQRLRMRTTY
     DLEMMQQMGF CNGIENYSSH IDGRARGTAP HCLLDYFPDD FLLVIDESHV TVPQIGAMYE
     GDMSRKRNLV DFGFRLPSAM DNRPLKWDEF QERVGQTVYL SATPGKYELG KSDGFVQQII
     RPTGLIDPEV VVKPTKGQID DLLGEIKTRT AKNERVLVTT LTKRMAEDLT DYLLGHGVKV
     EYLHSDVDTL RRVELLRELR MGVFDVLVGI NLLREGLDLP EVSLVSILDA DKEGFLRSST
     SLIQTIGRAA RNVSGQVHMY ADRITDSMAH AIDETNRRRA IQVAYNTEHG IDPQPLRKKI
     ADITDQLAKE DADTRELLAA SGKTRGKGKG ASTVRADGLA AAPAEDLVGL IEQLTEQMHA
     AAGELQFELA ARLRDEVGEL KKELRQMQAA GHA
//
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