(data stored in SCRATCH zone)

SWISSPROT: Q5LVZ9_RUEPO

ID   Q5LVZ9_RUEPO            Unreviewed;       732 AA.
AC   Q5LVZ9;
DT   01-FEB-2005, integrated into UniProtKB/TrEMBL.
DT   01-FEB-2005, sequence version 1.
DT   08-MAY-2019, entry version 117.
DE   RecName: Full=UvrABC system protein B {ECO:0000256|HAMAP-Rule:MF_00204, ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS01081106};
DE            Short=Protein UvrB {ECO:0000256|HAMAP-Rule:MF_00204};
DE   AltName: Full=Excinuclease ABC subunit B {ECO:0000256|HAMAP-Rule:MF_00204};
GN   Name=uvrB {ECO:0000256|HAMAP-Rule:MF_00204,
GN   ECO:0000313|EMBL:AAV93861.1};
GN   OrderedLocusNames=SPO0545 {ECO:0000313|EMBL:AAV93861.1};
OS   Ruegeria pomeroyi (strain ATCC 700808 / DSM 15171 / DSS-3)
OS   (Silicibacter pomeroyi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Ruegeria.
OX   NCBI_TaxID=246200 {ECO:0000313|EMBL:AAV93861.1, ECO:0000313|Proteomes:UP000001023};
RN   [1] {ECO:0000313|EMBL:AAV93861.1, ECO:0000313|Proteomes:UP000001023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=15602564; DOI=10.1038/nature03170;
RA   Moran M.A., Buchan A., Gonzalez J.M., Heidelberg J.F., Whitman W.B.,
RA   Kiene R.P., Henriksen J.R., King G.M., Belas R., Fuqua C., Brinkac L.,
RA   Lewis M., Johri S., Weaver B., Pai G., Eisen J.A., Rahe E.,
RA   Sheldon W.M., Ye W., Miller T.R., Carlton J., Rasko D.A.,
RA   Paulsen I.T., Ren Q., Daugherty S.C., Deboy R.T., Dodson R.J.,
RA   Durkin A.S., Madupu R., Nelson W.C., Sullivan S.A., Rosovitz M.J.,
RA   Haft D.H., Selengut J., Ward N.;
RT   "Genome sequence of Silicibacter pomeroyi reveals adaptations to the
RT   marine environment.";
RL   Nature 432:910-913(2004).
RN   [2] {ECO:0000313|EMBL:AAV93861.1, ECO:0000313|Proteomes:UP000001023}
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 700808 / DSM 15171 / DSS-3
RC   {ECO:0000313|Proteomes:UP000001023};
RX   PubMed=25780504; DOI=10.1186/1944-3277-9-11;
RA   Rivers A.R., Smith C.B., Moran M.A.;
RT   "An updated genome annotation for the model marine bacterium Ruegeria
RT   pomeroyi DSS-3.";
RL   Stand. Genomic Sci. 9:11-11(2014).
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:0000256|HAMAP-
CC       Rule:MF_00204, ECO:0000256|SAAS:SAAS01081113}.
CC   -!- SUBUNIT: Forms a heterotetramer with UvrA during the search for
CC       lesions. Interacts with UvrC in an incision complex.
CC       {ECO:0000256|HAMAP-Rule:MF_00204, ECO:0000256|RuleBase:RU003587,
CC       ECO:0000256|SAAS:SAAS01081110}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00204,
CC       ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS01144535}.
CC   -!- DOMAIN: The beta-hairpin motif is involved in DNA binding.
CC       {ECO:0000256|HAMAP-Rule:MF_00204}.
CC   -!- SIMILARITY: Belongs to the UvrB family. {ECO:0000256|HAMAP-
CC       Rule:MF_00204, ECO:0000256|RuleBase:RU003587,
CC       ECO:0000256|SAAS:SAAS01081111}.
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DR   EMBL; CP000031; AAV93861.1; -; Genomic_DNA.
DR   RefSeq; WP_011046302.1; NC_003911.12.
DR   STRING; 246200.SPO0545; -.
DR   EnsemblBacteria; AAV93861; AAV93861; SPO0545.
DR   KEGG; sil:SPO0545; -.
DR   eggNOG; ENOG4105CCW; Bacteria.
DR   eggNOG; COG0556; LUCA.
DR   HOGENOM; HOG000073580; -.
DR   KO; K03702; -.
DR   OMA; RYMHSEI; -.
DR   OrthoDB; 95696at2; -.
DR   BioCyc; RPOM246200:G1G48-552-MONOMER; -.
DR   Proteomes; UP000001023; 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   CDD; cd00079; HELICc; 1.
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;
DR   PRODOM; Q5LVZ9.
DR   SWISS-2DPAGE; Q5LVZ9.
KW   ATP-binding {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|SAAS:SAAS01144540}; Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001023};
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|SAAS:SAAS01144521};
KW   DNA damage {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS01144538};
KW   DNA excision {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS01081119};
KW   DNA repair {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS01144510};
KW   Excision nuclease {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS01081136};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|SAAS:SAAS01144519};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001023};
KW   SOS response {ECO:0000256|HAMAP-Rule:MF_00204,
KW   ECO:0000256|RuleBase:RU003587, ECO:0000256|SAAS:SAAS01081129}.
FT   DOMAIN       53    199       Helicase ATP-binding.
FT                                {ECO:0000259|PROSITE:PS51192}.
FT   DOMAIN      458    624       Helicase C-terminal.
FT                                {ECO:0000259|PROSITE:PS51194}.
FT   DOMAIN      651    686       UVR. {ECO:0000259|PROSITE:PS50151}.
FT   NP_BIND      66     73       ATP. {ECO:0000256|HAMAP-Rule:MF_00204}.
FT   COILED      291    311       {ECO:0000256|SAM:Coils}.
FT   COILED      654    674       {ECO:0000256|SAM:Coils}.
FT   MOTIF       119    142       Beta-hairpin. {ECO:0000256|HAMAP-Rule:
FT                                MF_00204}.
SQ   SEQUENCE   732 AA;  82284 MW;  09C76EF9AD95C03A CRC64;
     MPDAHSDKSA ALMHAPAPDV KARPKLEGGR RFVMQTEFQP AGDQPTAIAE LTQGVNEGER
     NQVLLGATGT GKTFTMAKVI EETQRPAIIL APNKTLAAQL YGEFKGFFPD NAVEYFVSFY
     DYYQPEAYVA RSDTYIEKES QINEQIDRMR HSATRALLER DDVIIIASVS CIYGIGSVET
     YGAMTQDLKV GGEYDQRQIM ADLVAQQYKR NDQAFQRGSF RVRGDSLEVW PAHLEDRAWK
     LSFFGEELEA ITEFDPLTGQ KTDTFDQIRV YANSHYVTPK PTMQQAIIGI KQELRQRLDQ
     LVGEGKLLEA QRLEQRTNFD LEMLEATGVC NGIENYSRYL TGRAPGEPPP TLFEFIPDHA
     IVFADESHVS VPQIGGMYRG DYRRKFTLAE HGFRLPSCMD NRPLKFEEWD AMRPQSVFVS
     ATPAAWEMEQ SGGVFTEQVI RPTGLLDPQV EIRPVEMQVD DLLDEVRKMA DQGFRTLVTT
     LTKRMAEDLT EYLHEQGIKV RYMHSDIDTL ERIEILRDLR LGAFDVLVGI NLLREGLDIP
     ECGLVAILDA DKEGFLRSET SLIQTIGRAA RNAEGRVIMY ADRITGSMER ALGETDRRRA
     KQIAYNEEHG ITPATVKKNV EDVLAGLYKG DTDMSRVTAK IDKPLHGGNL EAVLDGLRAD
     MRKAAENLEF EEAARLRDEV KRLEAVDLAV SDDPMARQWA VESASEQAVK SRGRSTAGRP
     GQRGGNVKRR GR
//

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