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Database: UniProt
Entry: C6DDU0
LinkDB: C6DDU0
Original site: C6DDU0 
ID   UVRB_PECCP              Reviewed;         670 AA.
AC   C6DDU0;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   01-SEP-2009, sequence version 1.
DT   31-JUL-2019, entry version 66.
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=PC1_1509;
OS   Pectobacterium carotovorum subsp. carotovorum (strain PC1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Pectobacteriaceae; Pectobacterium.
OX   NCBI_TaxID=561230;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PC1;
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H.,
RA   Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C.,
RA   Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Mikhailova N., Balakrishnan V., Glasner J., Perna N.T.;
RT   "Complete sequence of Pectobacterium carotovorum subsp. carotovorum
RT   PC1.";
RL   Submitted (JUL-2009) 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
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; CP001657; ACT12552.1; -; Genomic_DNA.
DR   RefSeq; WP_015839778.1; NC_012917.1.
DR   SMR; C6DDU0; -.
DR   STRING; 561230.PC1_1509; -.
DR   PRIDE; C6DDU0; -.
DR   EnsemblBacteria; ACT12552; ACT12552; PC1_1509.
DR   GeneID; 29706008; -.
DR   KEGG; pct:PC1_1509; -.
DR   eggNOG; ENOG4105CCW; Bacteria.
DR   eggNOG; COG0556; LUCA.
DR   HOGENOM; HOG000073580; -.
DR   KO; K03702; -.
DR   OMA; RYMHSEI; -.
DR   OrthoDB; 95696at2; -.
DR   BioCyc; PCAR561230:G1GF8-1537-MONOMER; -.
DR   Proteomes; UP000002736; 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; SOS response.
FT   CHAIN         1    670       UvrABC system protein B.
FT                                /FTId=PRO_1000204138.
FT   DOMAIN       26    183       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      431    597       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      630    665       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   670 AA;  75858 MW;  B1C67F93A7C0267B CRC64;
     MSKVFTLNSD FKPAGDQPEA IRRLKEGLED GLAHQTLLGV TGSGKTFTIA NVIADLNRPT
     MMLAPNKTLA AQLYGEMKEF FPDNAVEYFV SYYDYYQPEA YVPSSDTFIE KDASVNEHIE
     QMRLSATKAL LERRDVIVVA SVSAIYGLGD PDLYLKMMLH LTQGMLIDQR AILRRLAELQ
     YSRNDQAFQR GTFRVRGEVI DIFPAESDEI ALRVELFDEE VERLSLFDPL TGHVLQTVPR
     YTIYPKTHYV TPRERILQAM EDIKVELADR RKVLLANDKL VEEQRLSQRT QFDLEMMNEL
     GYCSGIENYS RYLSGRGPGE PPPTLFDYLP ADGLLVIDES HVTVPQIGGM YRGDRARKET
     LVEYGFRLPS ALDNRPMKFE EFEALAPQTI YVSATPGNYE LEKSGGEVID QVVRPTGLLD
     PLIEVRPVAT QVDDLLSEIR QRAAVNERVL VTTLTKRMAE DLTEYLEEHG ERVRYLHSDI
     DTVERVEIIR DLRLGEFDVL VGINLLREGL DMPEVSLVAI LDADKEGFLR SERSLIQTIG
     RAARNLRGKA ILYGDKITPS MAKAIGETER RREKQEAYNT EHGIVPQGLN KKISDILQLG
     QPTNRGKGRG NRKAAEPAAR YELMTPKALE LKIRELESKM LTHAQNLEFE EAAALRDELQ
     ALRAQFIAAS
//
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