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Database: UniProt
Entry: A2RE43
LinkDB: A2RE43
Original site: A2RE43 
ID   UVRB_STRPG              Reviewed;         663 AA.
AC   A2RE43;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   18-SEP-2019, entry version 87.
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=SpyM50790;
OS   Streptococcus pyogenes serotype M5 (strain Manfredo).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=160491;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Manfredo;
RX   PubMed=17012393; DOI=10.1128/jb.01227-06;
RA   Holden M.T.G., Scott A., Cherevach I., Chillingworth T., Churcher C.,
RA   Cronin A., Dowd L., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA   Moule S., Mungall K., Quail M.A., Price C., Rabbinowitsch E.,
RA   Sharp S., Skelton J., Whitehead S., Barrell B.G., Kehoe M.,
RA   Parkhill J.;
RT   "Complete genome of acute rheumatic fever-associated serotype M5
RT   Streptococcus pyogenes strain Manfredo.";
RL   J. Bacteriol. 189:1473-1477(2007).
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; AM295007; CAM30118.1; -; Genomic_DNA.
DR   RefSeq; WP_011888826.1; NC_009332.1.
DR   SMR; A2RE43; -.
DR   KEGG; spf:SpyM50790; -.
DR   HOGENOM; HOG000073580; -.
DR   KO; K03702; -.
DR   OMA; RYMHSEI; -.
DR   BioCyc; SPYO160491:G1G1P-862-MONOMER; -.
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; Cytoplasm; DNA damage; DNA excision; DNA repair;
KW   Excision nuclease; Helicase; Hydrolase; Nucleotide-binding;
KW   SOS response.
FT   CHAIN         1    663       UvrABC system protein B.
FT                                /FTId=PRO_1000077930.
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;  75647 MW;  B7976780B191A215 CRC64;
     MIDKRDDKPF KLKSKYKPSG DQPQAIESLV DNIEGGEKAQ ILLGATGTGK TYTMSQVISK
     VNKPTLVIAH NKTLAGQLYG EFKEFFPDNA VEYFVSYYDY YQPEAYVPSS DTYIEKDSSV
     NDEIDKLRHS ATSSLLERND VIVVASVSCI YGLGSPKEYA DSAVSLRPGQ EISRDTLLNQ
     LVDIQFERND IDFQRGCFRV RGDVVEVFPA SRDEHAFRVE FFGDEIDRIC EIESLTGKTI
     GEVDHLVLFP ATHFVTNDEH MEQSIAKIQA ELAEQLQLFE SEGKLLEAQR LRQRTEYDIE
     MLREMGYTSG VENYSRHMDG RSPGEPPYTL LDFFPEDFLI MIDESHMTMG QIKGMYNGDQ
     ARKQMLVDYG FRLPSALDNR PLRREEFESH VHQIVYVSAT PGEYEMSQTN TIIEQIIRPT
     GLLDPEIDVR PSMGQIDDLL GEINQRVARD ERTFITTLTK KMAEDLTDYL KEMGVKVKYM
     HSDIKTLERT EIIRDLRLGV FDVLIGINLL REGIDVPEVS LVAILDADKE GFLRNERGLI
     QTIGRAARNV DGHVIMYADK MTDSMQRAID ETARRREIQI AYNKAHGIVP QTIKKDIRGL
     ISISKTSHND ISKEEMDYES MSRGERKEAI NALQKQMQEA AELLDFELAA QMRDLILELK
     LMD
//
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