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Database: UniProt
Entry: B8ZJQ9
LinkDB: B8ZJQ9
Original site: B8ZJQ9 
ID   UVRB_STRPJ              Reviewed;         662 AA.
AC   B8ZJQ9;
DT   28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT   03-MAR-2009, sequence version 1.
DT   18-SEP-2019, entry version 69.
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=SPN23F11340;
OS   Streptococcus pneumoniae (strain ATCC 700669 / Spain 23F-1).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=561276;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700669 / Spain 23F-1;
RX   PubMed=19114491; DOI=10.1128/jb.01343-08;
RA   Croucher N.J., Walker D., Romero P., Lennard N., Paterson G.K.,
RA   Bason N.C., Mitchell A.M., Quail M.A., Andrew P.W., Parkhill J.,
RA   Bentley S.D., Mitchell T.J.;
RT   "Role of conjugative elements in the evolution of the multidrug-
RT   resistant pandemic clone Streptococcus pneumoniae Spain23F ST81.";
RL   J. Bacteriol. 191:1480-1489(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; FM211187; CAR68943.1; -; Genomic_DNA.
DR   RefSeq; WP_000607027.1; NC_011900.1.
DR   SMR; B8ZJQ9; -.
DR   EnsemblBacteria; CAR68943; CAR68943; SPN23F11340.
DR   KEGG; sne:SPN23F11340; -.
DR   KO; K03702; -.
DR   OMA; RYMHSEI; -.
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    662       UvrABC system protein B.
FT                                /FTId=PRO_1000200554.
FT   DOMAIN       31    188       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      626    661       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   662 AA;  75734 MW;  C2EB617ED537BDD1 CRC64;
     MINHITDNQF KLVSKYQPSG DQPQAIEQLV DNIEGGEKAQ ILMGATGTGK TYTMSQVISK
     VNKPTLVIAH NKTLAGQLYG EFKEFFPENA VEYFVSYYDY YQPEAYVPSS DTYIEKDSSV
     NDEIDKLRHS ATSALLERND VIVVASVSCI YGLGSPKEYA DSVVSLRPGL EISRDKLLND
     LVDIQFERND IDFQRGRFRV RGDVVEIFPA SRDEHAFRVE FFGDEIDRIR EVEALTGQVL
     GEVDHLAIFP ATHFVTNDDH MEVAIAKIQA ELEEQLAVFE KEGKLLEAQR LKQRTEYDIE
     MLREMGYTNG VENYSRHMDG RSEGEPPYTL LDFFPDDFLI MIDESHMTIG QIKGMYNGDR
     SRKEMLVNYG FRLPSALDNR PLRREEFESH VHQIVYVSAT PGDYENEQTE TVIEQIIRPT
     GLLDPEVEVR PTMGQIDDLL GEINARVEKN ERTFITTLTK KMAEDLTDYF KEMGIKVKYM
     HSDIKTLERT EIIRDLRLGV FDVLVGINLL REGIDVPEVS LVAILDADKE GFLRNERGLI
     QTIGRAARNS EGHVIMYADT VTQSMQRAID ETARRRKIQM AYNEEHGIVP QTIKKEIRDL
     IAVTKAVAKE EDKEVDINSL NKQERKELVK KLEKQMQEAV EVLDFELAAQ IRDMMLEVKA
     LD
//
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