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Database: UniProt
Entry: P72174
LinkDB: P72174
Original site: P72174 
ID   UVRB_PSEAE              Reviewed;         670 AA.
AC   P72174; P72147;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   08-DEC-2000, sequence version 2.
DT   31-JUL-2019, entry version 128.
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}; OrderedLocusNames=PA3138;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 /
OS   JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC   1C / PRS 101 / PAO1;
RX   PubMed=8808952; DOI=10.1128/jb.178.18.5550-5554.1996;
RA   Rivera E., Vila L., Barbe J.;
RT   "The uvrB gene of Pseudomonas aeruginosa is not DNA damage
RT   inducible.";
RL   J. Bacteriol. 178:5550-5554(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC   1C / PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T.,
RA   Reizer J., Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an
RT   opportunistic pathogen.";
RL   Nature 406:959-964(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-209.
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 /
RC   1C / PRS 101 / PAO1;
RX   PubMed=8939432; DOI=10.1046/j.1365-2958.1996.1351503.x;
RA   Burrows L.L., Charter D.F., Lam J.S.;
RT   "Molecular characterization of the Pseudomonas aeruginosa serotype O5
RT   (PAO1) B-band lipopolysaccharide gene cluster.";
RL   Mol. Microbiol. 22:481-495(1996).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC45869.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; X93486; CAA63759.1; -; Genomic_DNA.
DR   EMBL; AE004091; AAG06526.1; -; Genomic_DNA.
DR   EMBL; U50396; AAC45869.1; ALT_INIT; Genomic_DNA.
DR   PIR; A83255; A83255.
DR   RefSeq; NP_251828.1; NC_002516.2.
DR   RefSeq; WP_003104590.1; NZ_QZGE01000023.1.
DR   SMR; P72174; -.
DR   PaxDb; P72174; -.
DR   PRIDE; P72174; -.
DR   EnsemblBacteria; AAG06526; AAG06526; PA3138.
DR   GeneID; 882670; -.
DR   KEGG; pae:PA3138; -.
DR   PATRIC; fig|208964.12.peg.3290; -.
DR   PseudoCAP; PA3138; -.
DR   eggNOG; ENOG4105CCW; Bacteria.
DR   eggNOG; COG0556; LUCA.
DR   HOGENOM; HOG000073580; -.
DR   InParanoid; P72174; -.
DR   KO; K03702; -.
DR   OMA; RYMHSEI; -.
DR   PhylomeDB; P72174; -.
DR   BioCyc; PAER208964:G1FZ6-3198-MONOMER; -.
DR   Proteomes; UP000002438; 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; Reference proteome;
KW   SOS response.
FT   CHAIN         1    670       UvrABC system protein B.
FT                                /FTId=PRO_0000138418.
FT   DOMAIN       25    412       Helicase ATP-binding. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      429    582       Helicase C-terminal. {ECO:0000255|HAMAP-
FT                                Rule:MF_00204}.
FT   DOMAIN      631    666       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.
FT   CONFLICT    173    173       R -> Q (in Ref. 1; CAA63759).
FT                                {ECO:0000305}.
FT   CONFLICT    406    406       V -> I (in Ref. 1; CAA63759).
FT                                {ECO:0000305}.
SQ   SEQUENCE   670 AA;  76067 MW;  BD63D171E818E5BF CRC64;
     MDTFQLDSRF KPAGDQPEAI RQMVEGLEAG LSHQTLLGVT GSGKTFSIAN VIAQVQRPTL
     VLAPNKTLAA QLYGEFKTFF PHNSVEYFVS YYDYYQPEAY VPSSDTYIEK DSSINDHIEQ
     MRLSATKALL ERPDAIIVAT VSSIYGLGDP ASYLKMVLHL DRGDRIDQRE LLRRLTSLQY
     TRNDMDFARA TFRVRGDVID IFPAESDLEA IRVELFDDEV ESLSAFDPLT GEVIRKLPRF
     TFYPKSHYVT PRETLLEAVD QIKAELKERL DYLRNNNKLV EAQRLEQRTR FDLEMILELG
     YCNGIENYSR YLSGRAPGEP PPTLYDYLPA NSLLVIDESH VSVPQVGAMF KGDRSRKETL
     VEYGFRLPSA LDNRPLRFEE WEAVSPQTIF VSATPGPYEA EHAGRVIEQV VRPTGLVDPE
     IEVRPAMTQV DDLLSQIRQR VAKDERVLVT TLTKRMAEDL TDYLGDHDVR VRYLHSDIDT
     VERVEIIRDL RAGAFDVLVG INLLREGLDM PEVSLVAILD ADKEGFLRSE RSLIQTIGRA
     ARNLHGKAIL YADNVTGSMQ RAIDETERRR AKQIAFNEAH GIVPKGVRKD IKDILEGAVV
     PGARGKRKGV AKVAEESGRY ENELRSPSEI SKRIRQLEEK MYQLARDLEF EAAAQLRDEI
     QTLRERLVNV
//
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