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Database: UniProt
Entry: A2C5B3
LinkDB: A2C5B3
Original site: A2C5B3 
ID   UVRB_PROM1              Reviewed;         678 AA.
AC   A2C5B3;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   31-JUL-2019, entry version 80.
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=NATL1_21171;
OS   Prochlorococcus marinus (strain NATL1A).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochloraceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=167555;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NATL1A;
RX   PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA   Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L.,
RA   Rodrigue S., Chen F., Lapidus A., Ferriera S., Johnson J.,
RA   Steglich C., Church G.M., Richardson P., Chisholm S.W.;
RT   "Patterns and implications of gene gain and loss in the evolution of
RT   Prochlorococcus.";
RL   PLoS Genet. 3:2515-2528(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; CP000553; ABM76673.1; -; Genomic_DNA.
DR   RefSeq; WP_011824617.1; NC_008819.1.
DR   SMR; A2C5B3; -.
DR   STRING; 167555.NATL1_21171; -.
DR   PRIDE; A2C5B3; -.
DR   EnsemblBacteria; ABM76673; ABM76673; NATL1_21171.
DR   KEGG; pme:NATL1_21171; -.
DR   eggNOG; ENOG4105CCW; Bacteria.
DR   eggNOG; COG0556; LUCA.
DR   HOGENOM; HOG000073580; -.
DR   KO; K03702; -.
DR   OMA; RYMHSEI; -.
DR   BioCyc; PMAR167555:G1G7Z-1952-MONOMER; -.
DR   Proteomes; UP000002592; 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    678       UvrABC system protein B.
FT                                /FTId=PRO_1000077909.
FT   DOMAIN       25    176       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   678 AA;  76771 MW;  677F11BDF606FFE2 CRC64;
     MPEYKLQAPY TPKGDQPAAI KGLVGGVNDG EKFQTLLGAT GTGKTFTIAN LIAQTGRPAL
     VLAHNKTLAA QLCNELREFF PDNAVEYFIS YYDYYQPEAY VPVSDTYIAK TSSINEEIDM
     LRHSATRSLF ERDDVIVVAS ISCIYGLGIP SEYLKASVKF QVGQSIDLRS CLRSLVSNQY
     TRNDIEISRG RFRVRGDVLE IGPAYDDRLV RLELFGDEVE SISYVDPTTG EILNKLDSIN
     IYPAKHFVTP KDRLDSAIKA IKKELKDRLE FLNQEGKLLE AQRLEQRTIY DLEMLKEVGY
     CNGVENYARH LSGREPGSAP ECLIDYFPKD WLLLIDESHV TCPQLRAMYN GDQARKKVLI
     DHGFRLPSAA DNRPLKDIEF WNKAKQTVFI SATPGDWELS QSTKNIVEQV IRPTGVLDPL
     VEVRPTHGQV DDLLFEIRKR ASKNQRILVT TLTKRMAEDL TDYLSENKIR VRYLHSEIHS
     IERIEIIQDL RLGEYDVLVG VNLLREGLDL PEVSLVVILD ADKEGFLRAQ RSLIQTIGRA
     ARHVEGLALL YADKMTDSMA KAISETERRR EIQNIYNIEH GITPKPAGKK ASNSILSFLE
     ISRRLNQDGS TDDFVDIADK LIEHSAKDSD SGVSLESLPE LIEKLESKMK IKAKDLDFEK
     AAILRDRIKK LRHRLVGR
//
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