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Database: UniProt
Entry: C0MBD7
LinkDB: C0MBD7
Original site: C0MBD7 
ID   UVRB_STRE4              Reviewed;         663 AA.
AC   C0MBD7;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-MAY-2009, sequence version 1.
DT   31-JUL-2019, entry version 70.
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=SEQ_1454;
OS   Streptococcus equi subsp. equi (strain 4047).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=553482;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=4047;
RX   PubMed=19325880; DOI=10.1371/journal.ppat.1000346;
RA   Holden M.T.G., Heather Z., Paillot R., Steward K.F., Webb K.,
RA   Ainslie F., Jourdan T., Bason N.C., Holroyd N.E., Mungall K.,
RA   Quail M.A., Sanders M., Simmonds M., Willey D., Brooks K.,
RA   Aanensen D.M., Spratt B.G., Jolley K.A., Maiden M.C.J., Kehoe M.,
RA   Chanter N., Bentley S.D., Robinson C., Maskell D.J., Parkhill J.,
RA   Waller A.S.;
RT   "Genomic evidence for the evolution of Streptococcus equi: host
RT   restriction, increased virulence, and genetic exchange with human
RT   pathogens.";
RL   PLoS Pathog. 5:E1000346-E1000346(2009).
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; FM204883; CAW94344.1; -; Genomic_DNA.
DR   SMR; C0MBD7; -.
DR   EnsemblBacteria; CAW94344; CAW94344; SEQ_1454.
DR   KEGG; seu:SEQ_1454; -.
DR   HOGENOM; HOG000073580; -.
DR   KO; K03702; -.
DR   OMA; RYMHSEI; -.
DR   OrthoDB; 95696at2; -.
DR   Proteomes; UP000001365; 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    663       UvrABC system protein B.
FT                                /FTId=PRO_1000200552.
FT   DOMAIN       31    271       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      435    601       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      627    662       UVR. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   NP_BIND      44     51       ATP. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   MOTIF        97    120       Beta-hairpin.
SQ   SEQUENCE   663 AA;  75606 MW;  2DCFCAF773339911 CRC64;
     MIDKRDFKAF KLVSKYAPSG DQPQAIETLV DNIEGGEKAQ ILLGATGTGK TYTMSQVISK
     VNKPTLVVAH NKTLAGQLYG EFKEFFPENA VEYFVSYYDY YQPEAYVPSS DTYIEKDSSV
     NDEIDKLRHS ATSSLLERND VIVVASVSCI YGLGSPKEYA DSAVSLRPGQ EISRDQLLNA
     LVDIQFERND IDFQRGRFRV RGDVVEVFPA SRDEHAFRIE FFGDEIDRIR EIESLTGKVL
     GDADHLVLFP ATHFVTNDEH MEQSISKIQA ELADQLKLFE AEGKLLEAQR LRQRTEYDIE
     MLREMGYTNG VENYSRHMDG RSAGEPPYTL LDFFPDDFLI MIDESHMTMG QIKGMYNGDK
     ARKQMLVDYG FRLPSALDNR PLRREEFESH VHQIVYVSAT PGDYEMEQTD TIVEQIIRPT
     GLLDPEVEVR PSMGQMDDLL GEINLRVERG ERTFITTLTK KMAEDLTDYL KEMGVKVKYM
     HSDIKTLERT EIIRDLRLGV FDVLIGINLL REGIDVPEVS LVAILDADKE GFLRNERGLI
     QTIGRAARNA DGHVIMYADR MTDSMQRAID ETARRRAIQM AYNEEHGIIP QTIKKDIRDL
     ISISRAVEAK ATEAETNYES MTRSERQEAI KQLQKNMQEA AELLDFELAA QLRDLILELK
     AMD
//
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