ID UVRB_PROMA Reviewed; 677 AA.
AC Q7V9M1;
DT 07-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2003, sequence version 1.
DT 01-MAY-2013, entry version 65.
DE RecName: Full=UvrABC system protein B;
DE Short=Protein UvrB;
DE AltName: Full=Excinuclease ABC subunit B;
GN Name=uvrB; OrderedLocusNames=Pro_1809;
OS Prochlorococcus marinus (strain SARG / CCMP1375 / SS120).
OC Bacteria; Cyanobacteria; Prochlorales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167539;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SARG / CCMP1375 / SS120;
RX PubMed=12917486; DOI=10.1073/pnas.1733211100;
RA Dufresne A., Salanoubat M., Partensky F., Artiguenave F., Axmann I.M.,
RA Barbe V., Duprat S., Galperin M.Y., Koonin E.V., Le Gall F.,
RA Makarova K.S., Ostrowski M., Oztas S., Robert C., Rogozin I.B.,
RA Scanlan D.J., Tandeau de Marsac N., Weissenbach J., Wincker P.,
RA Wolf Y.I., Hess W.R.;
RT "Genome sequence of the cyanobacterium Prochlorococcus marinus SS120,
RT a nearly minimal oxyphototrophic genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:10020-10025(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 (By similarity).
CC -!- SUBUNIT: Forms a heterotetramer with UvrA during the search for
CC lesions. Interacts with UvrC in an incision complex (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity).
CC -!- DOMAIN: The beta-hairpin motif is involved in DNA binding (By
CC similarity).
CC -!- SIMILARITY: Belongs to the UvrB family.
CC -!- SIMILARITY: Contains 1 helicase ATP-binding domain.
CC -!- SIMILARITY: Contains 1 helicase C-terminal domain.
CC -!- SIMILARITY: Contains 1 UVR domain.
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DR EMBL; AE017126; AAQ00853.1; -; Genomic_DNA.
DR RefSeq; NP_876200.1; NC_005042.1.
DR ProteinModelPortal; Q7V9M1; -.
DR SMR; Q7V9M1; 3-590.
DR STRING; 167539.Pro1809; -.
DR EnsemblBacteria; AAQ00853; AAQ00853; Pro_1809.
DR GeneID; 1463192; -.
DR KEGG; pma:Pro1809; -.
DR PATRIC; 23030471; VBIProMar8617_1911.
DR eggNOG; COG0556; -.
DR KO; K03702; -.
DR OMA; CIYGLGI; -.
DR ProtClustDB; PRK05298; -.
DR BioCyc; PMAR167539:GJN2-1853-MONOMER; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:HAMAP.
DR GO; GO:0003677; F:DNA binding; IEA:HAMAP.
DR GO; GO:0009381; F:excinuclease ABC activity; IEA:HAMAP.
DR GO; GO:0004386; F:helicase activity; IEA:HAMAP.
DR GO; GO:0090305; P:nucleic acid phosphodiester bond hydrolysis; IEA:GOC.
DR GO; GO:0006289; P:nucleotide-excision repair; IEA:HAMAP.
DR GO; GO:0009432; P:SOS response; IEA:HAMAP.
DR Gene3D; 4.10.860.10; -; 1.
DR HAMAP; MF_00204; UvrB; 1; -.
DR InterPro; IPR006935; Helicase/UvrB_dom.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR001943; UVR_dom.
DR InterPro; IPR004807; UvrB.
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 SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SUPFAM; SSF46600; UvrB_C; 1.
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; Reference proteome;
KW SOS response.
FT CHAIN 1 677 UvrABC system protein B.
FT /FTId=PRO_0000227341.
FT DOMAIN 25 412 Helicase ATP-binding.
FT DOMAIN 429 591 Helicase C-terminal.
FT DOMAIN 639 674 UVR.
FT NP_BIND 38 45 ATP (Potential).
FT MOTIF 91 114 Beta-hairpin.
SQ SEQUENCE 677 AA; 77240 MW; 3AF1E0DA4996F5F8 CRC64;
MSKYYLKAPY QPKGDQPKAI TKLVDGVNSG REYQTLLGAT GTGKTFTIAN VIAKTGRPAL
VLAHNKTLAA QLCNELREFF PNNAVEYFIS YYDYYQPEAY VPVSDTYIAK TSSINEEIDM
LRHSATRSLF ERDDVIVVAS ISCIYGLGIP SEYLKASVKF KVGNEINLRK SLRELVANQY
FRNDFDIGRG KFRVKGDVLE IGPAYDDRLV RIELFGDEIE AIRYVDPITG EILDSLNCIS
IYPAKHFVTP KERLVTAIDD IQKELKEQLD FFNKEGKLLE AQRLEQRTKY DLEMLREVGY
CNGVENYARH LSGREAGSPP ECLIDYFPKD WLLVIDESHV TCSQLLAMYN GDQSRKKVLI
EHGFRLPSAA DNRPLKSQEF WNKANQTVFI SATPGNWELE ISSGAIIEQV IRPTGVLDPL
VEVRPTKGQV EDLLDEIRER SRKKQRVLIT TLTKRMAEDL TDYLSENDVR VRYLHSEIHS
IERIEIIQDL RMGEYDVLVG VNLLREGLDL PEVSLVVILD ADKEGFLRAE RSLIQTIGRA
ARHIEGKALL YADNFTDSMK KAIEETERRR AIQESYNQQN NIVPMPAGKK ANNSILSFLE
LSRRVQKDGI DNDLVEIAGN VVDEFKFNNN SELAIENLPQ LIDELETKMK KSAKDLDFEN
AAKLRDKIHQ LRKKLIR
//
