DPRA_STRR6
ID DPRA_STRR6 Reviewed; 282 AA.
AC Q8DPI7;
DT 07-SEP-2016, integrated into UniProtKB/Swiss-Prot.
DT 07-SEP-2016, sequence version 2.
DT 25-MAY-2022, entry version 90.
DE RecName: Full=DNA processing protein DprA {ECO:0000303|PubMed:17803906};
GN Name=dprA {ECO:0000303|PubMed:12123453, ECO:0000303|PubMed:17803906};
GN Synonyms=cilB {ECO:0000303|PubMed:9535083},
GN dal {ECO:0000303|PubMed:10223974}, smf; OrderedLocusNames=spr1144;
OS Streptococcus pneumoniae (strain ATCC BAA-255 / R6).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=171101;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=11544234; DOI=10.1128/jb.183.19.5709-5717.2001;
RA Hoskins J., Alborn W.E. Jr., Arnold J., Blaszczak L.C., Burgett S.,
RA DeHoff B.S., Estrem S.T., Fritz L., Fu D.-J., Fuller W., Geringer C.,
RA Gilmour R., Glass J.S., Khoja H., Kraft A.R., Lagace R.E., LeBlanc D.J.,
RA Lee L.N., Lefkowitz E.J., Lu J., Matsushima P., McAhren S.M., McHenney M.,
RA McLeaster K., Mundy C.W., Nicas T.I., Norris F.H., O'Gara M., Peery R.B.,
RA Robertson G.T., Rockey P., Sun P.-M., Winkler M.E., Yang Y.,
RA Young-Bellido M., Zhao G., Zook C.A., Baltz R.H., Jaskunas S.R.,
RA Rosteck P.R. Jr., Skatrud P.L., Glass J.I.;
RT "Genome of the bacterium Streptococcus pneumoniae strain R6.";
RL J. Bacteriol. 183:5709-5717(2001).
RN [2]
RP PROTEIN SEQUENCE OF 1-6, FUNCTION, INTERACTION WITH RECA, SUBUNIT, AND
RP DNA-BINDING.
RC STRAIN=R6 / R800;
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 [3]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=9535083; DOI=10.1046/j.1365-2958.1998.00737.x;
RA Campbell E.A., Choi S.Y., Masure H.R.;
RT "A competence regulon in Streptococcus pneumoniae revealed by genomic
RT analysis.";
RL Mol. Microbiol. 27:929-939(1998).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=CP1500;
RX PubMed=10223974; DOI=10.1128/aem.65.5.1883-1890.1999;
RA Lee M.S., Dougherty B.A., Madeo A.C., Morrison D.A.;
RT "Construction and analysis of a library for random insertional mutagenesis
RT in Streptococcus pneumoniae: use for recovery of mutants defective in
RT genetic transformation and for identification of essential genes.";
RL Appl. Environ. Microbiol. 65:1883-1890(1999).
RN [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=R6 / R800;
RX PubMed=12123453; DOI=10.1046/j.1365-2958.2002.03013.x;
RA Berge M., Moscoso M., Prudhomme M., Martin B., Claverys J.P.;
RT "Uptake of transforming DNA in Gram-positive bacteria: a view from
RT Streptococcus pneumoniae.";
RL Mol. Microbiol. 45:411-421(2002).
RN [6]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=R6 / R800;
RX PubMed=14617176; DOI=10.1046/j.1365-2958.2003.03702.x;
RA Berge M., Mortier-Barriere I., Martin B., Claverys J.P.;
RT "Transformation of Streptococcus pneumoniae relies on DprA- and RecA-
RT dependent protection of incoming DNA single strands.";
RL Mol. Microbiol. 50:527-536(2003).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.70 ANGSTROMS), FUNCTION, SUBUNIT, DOMAIN,
RP MUTAGENESIS OF 235-GLN--ASP-243; 251-ILE--HIS-260 AND 260-HIS--LEU-269, AND
RP DNA-BINDING.
RC STRAIN=R6 / R800;
RX PubMed=22904190; DOI=10.1073/pnas.1205638109;
RA Quevillon-Cheruel S., Campo N., Mirouze N., Mortier-Barriere I.,
RA Brooks M.A., Boudes M., Durand D., Soulet A.L., Lisboa J., Noirot P.,
RA Martin B., van Tilbeurgh H., Noirot-Gros M.F., Claverys J.P., Polard P.;
RT "Structure-function analysis of pneumococcal DprA protein reveals that
RT dimerization is crucial for loading RecA recombinase onto DNA during
RT transformation.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:E2466-E2475(2012).
CC -!- FUNCTION: Protein that helps load RecA onto ssDNA during transformation
CC (PubMed:17803906, PubMed:22904190). Required for DNA transformation
CC (PubMed:9535083, PubMed:10223974, PubMed:12123453). Not required for
CC DNA uptake but for a later stage of transformation (PubMed:12123453).
CC Thought to interact at the cell pole with newly imported transforming
CC ssDNA which it binds cooperatively, protecting linear and circular
CC ssDNA from nuclease action (PubMed:14617176, PubMed:17803906). Forms
CC bridges between DNA segments (PubMed:17803906). Favors the loading of
CC RecA onto ssDNA and formation of RecA-DNA filaments, triggering RecA-
CC catalysis of ATP-driven homologous DNA pairing (PubMed:17803906).
CC {ECO:0000269|PubMed:10223974, ECO:0000269|PubMed:12123453,
CC ECO:0000269|PubMed:14617176, ECO:0000269|PubMed:17803906,
CC ECO:0000269|PubMed:22904190, ECO:0000269|PubMed:9535083}.
CC -!- SUBUNIT: Homodimer; forms tail-to-tail dimers, forms nucleoprotein
CC complex (NPC) which requires at least 30 nucleotides (nt) of ssDNA
CC becoming optimal with 50 nt (PubMed:22904190). Interacts with RecA,
CC forms mixed DprA-RecA-ssDNA filaments (PubMed:17803906).
CC {ECO:0000269|PubMed:22904190, ECO:0000305|PubMed:17803906}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P39813}.
CC Note=Localizes to the cell poles during competence (By similarity).
CC {ECO:0000250|UniProtKB:P39813}.
CC -!- INDUCTION: Expressed under conditions that induce DNA competence
CC (PubMed:9535083). {ECO:0000269|PubMed:9535083}.
CC -!- DOMAIN: The regions responsible for dimerization and for DprA-RecA
CC interaction partially overlap, it is suggested that when RecA interacts
CC with the DprA-ssDNA NPC it rearranges or disrupts the DprA dimer,
CC leading to nucleation of RecA on ssDNA (PubMed:22904190).
CC {ECO:0000305|PubMed:22904190}.
CC -!- DISRUPTION PHENOTYPE: Loss of transformation (PubMed:9535083,
CC PubMed:10223974, PubMed:12123453, PubMed:14617176). Imported DNA is
CC very rapidly degraded (PubMed:14617176). {ECO:0000269|PubMed:10223974,
CC ECO:0000269|PubMed:12123453, ECO:0000269|PubMed:14617176,
CC ECO:0000269|PubMed:9535083}.
CC -!- SIMILARITY: Belongs to the DprA/Smf family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAK99947.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE007317; AAK99947.1; ALT_INIT; Genomic_DNA.
DR PIR; A95147; A95147.
DR PIR; G98014; G98014.
DR RefSeq; NP_358737.1; NC_003098.1.
DR RefSeq; WP_000705306.1; NC_003098.1.
DR PDB; 3UQZ; X-ray; 2.70 A; A/B/C=1-282.
DR PDBsum; 3UQZ; -.
DR AlphaFoldDB; Q8DPI7; -.
DR SMR; Q8DPI7; -.
DR STRING; 171101.spr1144; -.
DR EnsemblBacteria; AAK99947; AAK99947; spr1144.
DR GeneID; 60232492; -.
DR KEGG; spr:spr1144; -.
DR PATRIC; fig|171101.6.peg.1242; -.
DR eggNOG; COG0758; Bacteria.
DR HOGENOM; CLU_029601_3_3_9; -.
DR Proteomes; UP000000586; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0030420; P:establishment of competence for transformation; IMP:UniProtKB.
DR InterPro; IPR003488; DprA.
DR InterPro; IPR041104; SAM_DrpA.
DR PANTHER; PTHR43022; PTHR43022; 1.
DR Pfam; PF02481; DNA_processg_A; 1.
DR Pfam; PF18255; SAM_DrpA; 1.
DR TIGRFAMs; TIGR00732; dprA; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Competence; Cytoplasm; Direct protein sequencing;
KW DNA-binding; Reference proteome.
FT CHAIN 1..282
FT /note="DNA processing protein DprA"
FT /id="PRO_0000437126"
FT MUTAGEN 235..265
FT /note="ERAMEEGRDVFAIPGSILDGLSDGCHHLIQE->QRAMEEGRNVFAIPGSILD
FT GLSDGCHHLIQQ: Forms dimers, forms NPC with ssDNA, 5-fold
FT decreased binding to RecA, 150-fold less efficient
FT transformation."
FT /evidence="ECO:0000269|PubMed:22904190"
FT MUTAGEN 235..243
FT /note="ERAMEEGRD->QRAMEEGRN: Forms dimers, forms
FT nucleoprotein complex with ssDNA (NPC), 1.5-fold decreased
FT binding to RecA, 8-fold less efficient transformation."
FT /evidence="ECO:0000269|PubMed:22904190"
FT MUTAGEN 251..260
FT /note="ILDGLSDGCH->VLDGLSDGCR: Partially able to dimerize,
FT 180-fold less efficient transformation, interacts with
FT RecA."
FT /evidence="ECO:0000269|PubMed:22904190"
FT MUTAGEN 260..269
FT /note="HHLIQEGAKL->AHLIQEGAKK: No longer dimerizes."
FT /evidence="ECO:0000269|PubMed:22904190"
FT MUTAGEN 260..269
FT /note="HHLIQEGAKL->AHLIQEGAKR: No longer dimerizes, 180-
FT fold less efficient transformation, interacts with RecA,
FT binds ssDNA but no longer forms NPC via dimerization."
FT /evidence="ECO:0000269|PubMed:22904190"
SQ SEQUENCE 282 AA; 31063 MW; 2468A80641FFE873 CRC64;
MKITNYEIYK LKKSGLTNQQ ILKVLEYGEN VDQELLLGDI ADISGCRNPA VFMERYFQID
DAHLSKEFQK FPSFSILDDC YPWDLSEIYD APVLLFYKGN LDLLKFPKVA VVGSRACSKQ
GAKSVEKVIQ GLENELVIVS GLAKGIDTAA HMAALQNGGK TIAVIGTGLD VFYPKANKRL
QDYIGNDHLV LSEYGPGEQP LKFHFPARNR IIAGLCRGVI VAEAKMRSGS LITCERAMEE
GRDVFAIPGS ILDGLSDGCH HLIQEGAKLV TSGQDVLAEF EF
