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Database: UniProt
Entry: Q5M3D5
LinkDB: Q5M3D5
Original site: Q5M3D5 
ID   UVRB_STRT2              Reviewed;         668 AA.
AC   Q5M3D5;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   31-JUL-2019, entry version 101.
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=stu1497;
OS   Streptococcus thermophilus (strain ATCC BAA-250 / LMG 18311).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=264199;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-250 / LMG 18311;
RX   PubMed=15543133; DOI=10.1038/nbt1034;
RA   Bolotin A., Quinquis B., Renault P., Sorokin A., Ehrlich S.D.,
RA   Kulakauskas S., Lapidus A., Goltsman E., Mazur M., Pusch G.D.,
RA   Fonstein M., Overbeek R., Kyprides N., Purnelle B., Prozzi D.,
RA   Ngui K., Masuy D., Hancy F., Burteau S., Boutry M., Delcour J.,
RA   Goffeau A., Hols P.;
RT   "Complete sequence and comparative genome analysis of the dairy
RT   bacterium Streptococcus thermophilus.";
RL   Nat. Biotechnol. 22:1554-1558(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; CP000023; AAV61100.1; -; Genomic_DNA.
DR   SMR; Q5M3D5; -.
DR   STRING; 264199.stu1497; -.
DR   EnsemblBacteria; AAV61100; AAV61100; stu1497.
DR   KEGG; stl:stu1497; -.
DR   eggNOG; ENOG4105CCW; Bacteria.
DR   eggNOG; COG0556; LUCA.
DR   HOGENOM; HOG000073580; -.
DR   KO; K03702; -.
DR   OMA; RYMHSEI; -.
DR   Proteomes; UP000001170; 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; Reference proteome;
KW   SOS response.
FT   CHAIN         1    668       UvrABC system protein B.
FT                                /FTId=PRO_0000227369.
FT   DOMAIN       36    423       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      440    606       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      632    667       UVR. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   NP_BIND      49     56       ATP. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   MOTIF       102    125       Beta-hairpin.
SQ   SEQUENCE   668 AA;  76645 MW;  5C0812E06E47BE3B CRC64;
     MKGKTMIDRK EDNQFHLVSK YEPSGDQPQA IETLVDNIKG GEKAQILKGA TGTGKTYTMS
     QVIQRVNKPT LVIAHNKTLA GQLYGEFKEF FPDNAVEYFV SYYDYYQPEA YVPSSDTYIE
     KDSSINDEID KLRHSATSAL LERNDVIVVA SVSCIYGLGS PKEYADSAVS LRPGQEISRD
     KLLNDLVDIQ FERNDIDFQR GKFRVRGDVV EIFPASRDEN AFRVEFFGDE IDRICEIESL
     TGRNLGEVEH LVLFPATHFM TNEEHMEEAI KNIMEEMEVQ VNQFEAEGKL IEAQRIRQRT
     EYDVEMLREM GYTNGIENYS RHMDGRKEGE PPFTLLDFFP EDFLIMIDES HMTMGQIKGM
     YNGDQARKKM LVDYGFRLPS ALDNRPLRRE EFESHVHQIV YVSATPGDYE MEQTETVVEQ
     IIRPTGLLDP EVEVRPTMGQ MDDLLGEINA RTEKGERVFV TTLTKKMAED LTDYLKEMGV
     KVKYMHSDIK TLERTEIIRD LRLGVFDVLI GINLLREGID VPEVSLVAIL DADKEGFLRN
     ERGLIQTIGR AARNSDGHVI MYADKITESM QKAMDETARR REIQMAYNKE HGITPQTIKK
     EIRDLISITK TNEAEVAEDT VNYSAMNKKE RQEAIKKLQK QMHEAAELLD FELAAQIRDM
     VLELKSMD
//
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