GenomeNet

Database: UniProt
Entry: Q7UA24
LinkDB: Q7UA24
Original site: Q7UA24 
ID   UVRB_SYNPX              Reviewed;         677 AA.
AC   Q7UA24;
DT   07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   13-NOV-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=SYNW0077;
OS   Synechococcus sp. (strain WH8102).
OC   Bacteria; Cyanobacteria; Synechococcales; Synechococcaceae;
OC   Synechococcus; unclassified Synechococcus.
OX   NCBI_TaxID=84588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH8102;
RX   PubMed=12917641; DOI=10.1038/nature01943;
RA   Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L.,
RA   Chain P., Lamerdin J.E., Regala W., Allen E.E., McCarren J.,
RA   Paulsen I.T., Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT   "The genome of a motile marine Synechococcus.";
RL   Nature 424:1037-1042(2003).
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; BX569689; CAE06592.1; -; Genomic_DNA.
DR   RefSeq; WP_011126955.1; NC_005070.1.
DR   SMR; Q7UA24; -.
DR   STRING; 84588.SYNW0077; -.
DR   EnsemblBacteria; CAE06592; CAE06592; SYNW0077.
DR   KEGG; syw:SYNW0077; -.
DR   eggNOG; ENOG4105CCW; Bacteria.
DR   eggNOG; COG0556; LUCA.
DR   HOGENOM; HOG000073580; -.
DR   KO; K03702; -.
DR   OMA; RYMHSEI; -.
DR   OrthoDB; 95696at2; -.
DR   Proteomes; UP000001422; 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; SOS response.
FT   CHAIN         1    677       UvrABC system protein B.
FT                                /FTId=PRO_0000227376.
FT   DOMAIN       25    412       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      429    591       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      639    674       UVR. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   NP_BIND      38     45       ATP. {ECO:0000255|HAMAP-Rule:MF_00204}.
FT   MOTIF        91    114       Beta-hairpin.
SQ   SEQUENCE   677 AA;  75985 MW;  03AA7C70D698F089 CRC64;
     MPAYDLTAPY TPKGDQPTAI KQLVQGVNGG ERYQTLLGAT GTGKTFTMAN VIAQTGRPAL
     VLAHNKTLAA QLCNELREFF PENAVEYFIS YYDYYQPEAY VPVSDTYIAK TASINEEIDM
     LRHSATRSLF ERRDVIVVAS ISCIYGLGIP SEYLKAAVKF EVGETLNIRS QLRELVNNQY
     SRNDTEIARG RFRMKGDVLE IGPAYEDRLV RIELFGDEVE AIRYVDPTTG EILQSLETVN
     IYPAKHFVTP KDRLDSAIGE IRQELRDRLD FLNGEGKLLE AQRLEQRTKY DLEMLGQVGY
     CNGVENYARH LAGREEGTPP ECLIDYFPKD WLLIVDESHV TCSQLQAMYN GDQARKKVLI
     EHGFRLPSAA DNRPLKGEEF WEKAHQTVFV SATPGNWELE VSGGEVAQQV IRPTGVLDPI
     VEVRPTTGQV DDLLGEIRDR ASKQQRVLVT TLTKRMAEDL TDYLAENEVR VRYLHSEIHS
     IERIEIIQDL RLGEYDVLVG VNLLREGLDL PEVSLVAILD ADKEGFLRAE RSLIQTIGRA
     ARHVEGVALL YADNMTESMA KAISETERRR KIQQTYNEKH GIVPTAAGKK ASNSILSFLE
     LSRKLKQDGP DADLVQVAGK AAQALEEDPD AGLALEALPE LIDQLEGKMK EAAKKLDFED
     AANLRDRIKQ LRQKMAG
//
DBGET integrated database retrieval system