DPRA_BACSU
ID DPRA_BACSU Reviewed; 297 AA.
AC P39813; O34494;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=DNA processing protein DprA {ECO:0000303|PubMed:17630974};
DE AltName: Full=Protein Smf;
GN Name=dprA {ECO:0000303|PubMed:17630974}; Synonyms=smf;
GN OrderedLocusNames=BSU16110;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RA Foulger D., Errington J.;
RT "Cloning and sequencing 7.5 Kbp of DNA from Bacillus subtilis upstream of
RT the codV gene.";
RL Submitted (OCT-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 138-297.
RC STRAIN=168 / 8G5;
RA de Jong S.;
RT "Cloning and sequencing of the TopI gene, the gene encoding B. subtilis DNA
RT topoisomerase I.";
RL Submitted (AUG-1994) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168;
RX PubMed=11918817; DOI=10.1046/j.1365-2958.2002.02833.x;
RA Berka R.M., Hahn J., Albano M., Draskovic I., Persuh M., Cui X., Sloma A.,
RA Widner W., Dubnau D.;
RT "Microarray analysis of the Bacillus subtilis K-state: genome-wide
RT expression changes dependent on ComK.";
RL Mol. Microbiol. 43:1331-1345(2002).
RN [5]
RP INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=168 / CU741;
RX PubMed=11948146; DOI=10.1128/jb.184.9.2344-2351.2002;
RA Ogura M., Yamaguchi H., Kobayashi K., Ogasawara N., Fujita Y., Tanaka T.;
RT "Whole-genome analysis of genes regulated by the Bacillus subtilis
RT competence transcription factor ComK.";
RL J. Bacteriol. 184:2344-2351(2002).
RN [6]
RP GENE NAME, SUBCELLULAR LOCATION, AND DEVELOPMENTAL STAGE.
RC STRAIN=168;
RX PubMed=17630974; DOI=10.1111/j.1365-2958.2007.05799.x;
RA Kramer N., Hahn J., Dubnau D.;
RT "Multiple interactions among the competence proteins of Bacillus
RT subtilis.";
RL Mol. Microbiol. 65:454-464(2007).
RN [7]
RP FUNCTION, INTERACTION WITH RECA, SUBUNIT, AND DNA-BINDING.
RC STRAIN=168;
RX PubMed=17803906; DOI=10.1016/j.cell.2007.07.038;
RA Mortier-Barriere I., Velten M., Dupaigne P., Mirouze N., Pietrement O.,
RA McGovern S., Fichant G., Martin B., Noirot P., Le Cam E., Polard P.,
RA Claverys J.P.;
RT "A key presynaptic role in transformation for a widespread bacterial
RT protein: DprA conveys incoming ssDNA to RecA.";
RL Cell 130:824-836(2007).
RN [8]
RP FUNCTION.
RX PubMed=25138221; DOI=10.1074/jbc.m114.577924;
RA Yadav T., Carrasco B., Serrano E., Alonso J.C.;
RT "Roles of Bacillus subtilis DprA and SsbA in RecA-mediated genetic
RT recombination.";
RL J. Biol. Chem. 289:27640-27652(2014).
CC -!- FUNCTION: Protein that helps load RecA onto ssDNA during transformation
CC (PubMed:17803906, PubMed:25138221). Binds cooperatively to circular
CC ssDNA, is able to bridge different segments of DNA (PubMed:17803906).
CC Favors the loading of RecA onto SsbA- or SsbB-coated ssDNA and
CC formation of RecA-DNA filaments (PubMed:25138221). RecA-ATP cannot
CC catalyze homologous DNA strand exchange; SsbA and DprA activate strand
CC exchange by RecA-ATP (PubMed:25138221). {ECO:0000269|PubMed:17803906,
CC ECO:0000269|PubMed:25138221}.
CC -!- SUBUNIT: Interacts with RecA (PubMed:17803906).
CC {ECO:0000269|PubMed:17803906}.
CC -!- INTERACTION:
CC P39813; P16971: recA; NbExp=3; IntAct=EBI-1535559, EBI-1535844;
CC -!- SUBCELLULAR LOCATION: Cytoplasm. Note=Localizes mostly to the cell
CC poles during the development of competence (PubMed:17630974). During
CC competence a number of proteins (at least CoiA, ComFA, ComGA, DprA,
CC RecA and SsbB) are thought to colocalize at the cell pole, in a
CC disruption of ssbB DprA no longer accumulates (PubMed:17630974).
CC {ECO:0000269|PubMed:17630974}.
CC -!- DEVELOPMENTAL STAGE: Preferentially expressed in cells competent for
CC DNA transformation; that is 5-15% of the population (PubMed:17630974).
CC {ECO:0000269|PubMed:17630974}.
CC -!- INDUCTION: Expression activated by ComK (PubMed:11918817,
CC PubMed:11948146). {ECO:0000269|PubMed:11918817,
CC ECO:0000269|PubMed:11948146}.
CC -!- DISRUPTION PHENOTYPE: Transformation efficiency drops 50- to 100-fold
CC (PubMed:11918817, PubMed:11948146). {ECO:0000269|PubMed:11918817,
CC ECO:0000269|PubMed:11948146}.
CC -!- SIMILARITY: Belongs to the DprA/Smf family. {ECO:0000305}.
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DR EMBL; AJ000975; CAA04421.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB13484.1; -; Genomic_DNA.
DR EMBL; L27797; AAA22762.1; -; Genomic_DNA.
DR PIR; H69708; H69708.
DR RefSeq; NP_389493.1; NC_000964.3.
DR RefSeq; WP_003245871.1; NZ_JNCM01000035.1.
DR AlphaFoldDB; P39813; -.
DR SMR; P39813; -.
DR IntAct; P39813; 1.
DR STRING; 224308.BSU16110; -.
DR PaxDb; P39813; -.
DR PRIDE; P39813; -.
DR DNASU; 940135; -.
DR EnsemblBacteria; CAB13484; CAB13484; BSU_16110.
DR GeneID; 940135; -.
DR KEGG; bsu:BSU16110; -.
DR PATRIC; fig|224308.179.peg.1751; -.
DR eggNOG; COG0758; Bacteria.
DR InParanoid; P39813; -.
DR OMA; YSKQHTI; -.
DR PhylomeDB; P39813; -.
DR BioCyc; BSUB:BSU16110-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:1990814; F:DNA/DNA annealing activity; IDA:CACAO.
DR GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR InterPro; IPR003488; DprA.
DR PANTHER; PTHR43022; PTHR43022; 1.
DR Pfam; PF02481; DNA_processg_A; 1.
DR TIGRFAMs; TIGR00732; dprA; 1.
PE 1: Evidence at protein level;
KW Competence; Cytoplasm; DNA-binding; Reference proteome.
FT CHAIN 1..297
FT /note="DNA processing protein DprA"
FT /id="PRO_0000209155"
FT CONFLICT 262
FT /note="A -> P (in Ref. 3; AAA22762)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 297 AA; 32935 MW; A2E369AAC4D158CB CRC64;
MDQAAVCLTI CRINQLLSPS LLLKWWKADP SMSLTSPVLQ TVTRDQIKAA ALKNEIEQFY
PKLPRVLAAY REQGINTIPI SSKQYPFWLK SIYDPPAVLF AKGDMTLLSK GRKIGIVGTR
NPTAYGKQVV NHLTKEICRK GWVIVSGLAS GIDGMSHAAS IKAKGRTIGV IAGGFQHIYP
RENLQLADHM AKHHILLSEH PPETKPQKWH FPMRNRIISG LSEGVIVVQG KEKSGSLITA
YQALEQGREV FAVPGSLFDP YAGGPIKLIQ QGAKAIWSAE DIFEELPERN VQYTEPF
