UVRB_ZYMMO
ID UVRB_ZYMMO Reviewed; 740 AA.
AC Q56998; Q5NQL8; Q8GM48;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 15-FEB-2005, sequence version 2.
DT 03-AUG-2022, entry version 131.
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=ZMO0362;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RA Beletsiotis E.A., Oikonomou I., Typas M.A.;
RT "Isolation and characterization of the uvrA, uvrB and uvrD genes from the
RT ethanol producing bacterium Zymomonas mobilis strain CP4.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 457-740.
RA Reuter K.K.H., Ficner R.;
RL Submitted (JUN-1994) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; AY083905; AAM12395.1; -; Genomic_DNA.
DR EMBL; AE008692; AAV88986.1; -; Genomic_DNA.
DR EMBL; L33777; AAA27703.1; -; Genomic_DNA.
DR PIR; T46897; T46897.
DR RefSeq; WP_011240284.1; NZ_CP035711.1.
DR AlphaFoldDB; Q56998; -.
DR SMR; Q56998; -.
DR STRING; 264203.ZMO0362; -.
DR EnsemblBacteria; AAV88986; AAV88986; ZMO0362.
DR GeneID; 58026212; -.
DR KEGG; zmo:ZMO0362; -.
DR eggNOG; COG0556; Bacteria.
DR HOGENOM; CLU_009621_2_1_5; -.
DR OMA; EYVDRMV; -.
DR OrthoDB; 95696at2; -.
DR Proteomes; UP000001173; 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..740
FT /note="UvrABC system protein B"
FT /id="PRO_0000138452"
FT DOMAIN 56..444
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 461..627
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT DOMAIN 651..686
FT /note="UVR"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 687..740
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 122..145
FT /note="Beta-hairpin"
FT COMPBIAS 10..35
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 704..740
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 69..76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00204"
FT CONFLICT 304..337
FT /note="FKAEGKLLEAQRLEERTEFDLEMMAATGACSGIE -> SKLKVNYWKRRFGK
FT AHRIRSGNDGCNRCLFRYS (in Ref. 1)"
FT /evidence="ECO:0000305"
FT CONFLICT 419
FT /note="T -> N (in Ref. 1; AAM12395)"
FT /evidence="ECO:0000305"
FT CONFLICT 457..465
FT /note="PIEEQVDNL -> RPQLTLTKG (in Ref. 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 740 AA; 83724 MW; DEB679FA5C466EB0 CRC64;
MTIAIRTTLD EPENHSDFVP HRPSRPEKTE PSKPFRLVSD YEPAGDQPQA ISALCKDIQK
GERDQVLLGV TGSGKTFTMA KVIEKLQRPS LILAPNKILA AQLYGEFKRF FPENAVEFFV
SYYDYYQPEA YVPRTDTYIE KDSAINEAID RMRHAATRSL LEREDVIIVA SVSCLYGIGS
VDTYSSMTFR LLKGQLVDQR EIIRRLVALQ YKRNEVAFGR GSFRVKGDTL EIFPSHYEDM
AWRISFFGDE IEEISEFDPL TGVKIAKLDQ IKIYANSHYV TPEPTLKAAN NAIRRELDNR
LREFKAEGKL LEAQRLEERT EFDLEMMAAT GACSGIENYS RFLTGRAPGE PPPTLFEYLP
DNALLFVDES HQTIPQINGM SRGDYRRKTT LADYGFRLPS CIDNRPLRFE EWNAMRPQTV
YVSATPGPWE LEQTGGVFVE QIIRPTGLVD PAIEVRPIEE QVDNLIFEAK KTAAAGWRSL
VTTLTKRMAE DLTEYMYEAG LKVRYMHSDV ETIERIELIR DLRLGVYDVL IGINLLREGL
DIPECGLVAV LDADKEGFLR SETSLIQTIG RAARNAEGRV ILYGDKITGS MARAMAETER
RRIKQIAWNK AHNITPATVK RQVDDIVGHF GVVNSSEAAA TIENHDPKVL ARSISETEKE
MLEAAANLEF EKAAQLRDVL HQLKRQELGL PPEKSSEIQG RSEAGRPGTR KTRSDKAREA
KASKRVKQEA GEKLLRSRGH
