UVRB_PSEAE
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 03-AUG-2022, entry version 138.
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 / JCM
OS 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 / 1C /
RC 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 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 / 1C /
RC 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., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT 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 / 1C /
RC 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 of 2
CC UvrA and 2 UvrB subunits scans DNA for abnormalities. Upon binding of
CC the UvrA(2)B(2) complex to a putative damaged site, the DNA wraps
CC around one UvrB monomer. DNA wrap is dependent on ATP binding by UvrB
CC and probably causes local melting of the DNA helix, facilitating
CC insertion of UvrB beta-hairpin between the DNA strands. Then UvrB
CC probes one DNA strand for the presence of a lesion. If a lesion is
CC found the UvrA subunits dissociate and the UvrB-DNA preincision complex
CC is formed. This complex is subsequently bound by UvrC and the second
CC UvrB is released. If no lesion is found, the DNA wraps around the other
CC UvrB subunit that will check the other stand for damage.
CC {ECO:0000255|HAMAP-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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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 AlphaFoldDB; P72174; -.
DR SMR; P72174; -.
DR STRING; 287.DR97_4791; -.
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 HOGENOM; CLU_009621_2_1_6; -.
DR InParanoid; P72174; -.
DR OMA; EYVDRMV; -.
DR PhylomeDB; P72174; -.
DR BioCyc; PAER208964:G1FZ6-3198-MON; -.
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:ATP hydrolysis 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 Gene3D; 3.40.50.300; -; 3.
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; Nucleotide-binding; Reference proteome; SOS response.
FT CHAIN 1..670
FT /note="UvrABC system protein B"
FT /id="PRO_0000138418"
FT DOMAIN 25..412
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 429..582
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 631..666
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT MOTIF 91..114
FT /note="Beta-hairpin"
FT BINDING 38..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT CONFLICT 173
FT /note="R -> Q (in Ref. 1; CAA63759)"
FT /evidence="ECO:0000305"
FT CONFLICT 406
FT /note="V -> I (in Ref. 1; CAA63759)"
FT /evidence="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
