RADA_STRR6
ID RADA_STRR6 Reviewed; 420 AA.
AC Q8DRP0;
DT 13-APR-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=DNA repair protein RadA {ECO:0000255|HAMAP-Rule:MF_01498};
DE EC=3.6.4.- {ECO:0000255|HAMAP-Rule:MF_01498};
DE AltName: Full=Branch migration protein RadA {ECO:0000255|HAMAP-Rule:MF_01498};
GN Name=radA {ECO:0000255|HAMAP-Rule:MF_01498}; OrderedLocusNames=spr0025;
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 FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC BAA-255 / R6;
RX PubMed=17631629; DOI=10.1128/jb.00573-07;
RA Burghout P., Bootsma H.J., Kloosterman T.G., Bijlsma J.J., de Jongh C.E.,
RA Kuipers O.P., Hermans P.W.;
RT "Search for genes essential for pneumococcal transformation: the RADA DNA
RT repair protein plays a role in genomic recombination of donor DNA.";
RL J. Bacteriol. 189:6540-6550(2007).
CC -!- FUNCTION: Plays a role in repairing double-strand DNA breaks, probably
CC involving stabilizing or processing branched DNA or blocked replication
CC forks (By similarity). Required for efficient transformation with
CC chromosomal (linear) DNA, but not for replicative plasmid DNA. Its
CC increased sensitivity to a DNA damaging agent suggests it may be
CC required for DNA repair (PubMed:17631629). {ECO:0000255|HAMAP-
CC Rule:MF_01498, ECO:0000269|PubMed:17631629}.
CC -!- DOMAIN: The middle region has homology to RecA with ATPase motifs
CC including the RadA KNRFG motif, while the C-terminus is homologous to
CC Lon protease (By similarity). Unlike most bacteria many S.pneumoniae do
CC not have the N-terminal putative zinc-finger. {ECO:0000255|HAMAP-
CC Rule:MF_01498, ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Natural transformation efficiency with
CC chromosomal DNA decreases to 10%; uptake of replicating plasmid DNA is
CC unaffected. Increased sensitivity to methyl methanesulfonate but not UV
CC light (PubMed:17631629). {ECO:0000269|PubMed:17631629}.
CC -!- SIMILARITY: Belongs to the RecA family. RadA subfamily.
CC {ECO:0000255|HAMAP-Rule:MF_01498}.
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DR EMBL; AE007317; AAK98829.1; -; Genomic_DNA.
DR PIR; A97875; A97875.
DR RefSeq; NP_357619.1; NC_003098.1.
DR PDB; 5LKM; X-ray; 3.50 A; A/B/C=1-419.
DR PDB; 5LKQ; X-ray; 2.50 A; A/B=244-419.
DR PDBsum; 5LKM; -.
DR PDBsum; 5LKQ; -.
DR AlphaFoldDB; Q8DRP0; -.
DR SMR; Q8DRP0; -.
DR STRING; 171101.spr0025; -.
DR MEROPS; S16.A04; -.
DR EnsemblBacteria; AAK98829; AAK98829; spr0025.
DR KEGG; spr:spr0025; -.
DR PATRIC; fig|171101.6.peg.27; -.
DR eggNOG; COG1066; Bacteria.
DR HOGENOM; CLU_018264_0_1_9; -.
DR OMA; FELMRLA; -.
DR Proteomes; UP000000586; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003684; F:damaged DNA binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000725; P:recombinational repair; IBA:GO_Central.
DR Gene3D; 3.30.230.10; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_01498; RadA_bact; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR004504; DNA_repair_RadA.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020588; RecA_ATP-bd.
DR InterPro; IPR020568; Ribosomal_S5_D2-typ_fold.
DR InterPro; IPR014721; Ribosomal_S5_D2-typ_fold_subgr.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54211; SSF54211; 1.
DR TIGRFAMs; TIGR00416; sms; 1.
DR PROSITE; PS50162; RECA_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; DNA damage; DNA repair; DNA-binding; Hydrolase;
KW Metal-binding; Nucleotide-binding; Reference proteome; Stress response.
FT CHAIN 1..420
FT /note="DNA repair protein RadA"
FT /id="PRO_0000435882"
FT REGION 317..420
FT /note="Lon-protease-like"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT MOTIF 218..222
FT /note="RadA KNRFG motif"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT BINDING 62..69
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01498"
FT HELIX 26..28
FT /evidence="ECO:0007829|PDB:5LKM"
FT HELIX 42..47
FT /evidence="ECO:0007829|PDB:5LKM"
FT STRAND 50..52
FT /evidence="ECO:0007829|PDB:5LKM"
FT STRAND 54..62
FT /evidence="ECO:0007829|PDB:5LKM"
FT HELIX 68..79
FT /evidence="ECO:0007829|PDB:5LKM"
FT TURN 80..82
FT /evidence="ECO:0007829|PDB:5LKM"
FT STRAND 85..92
FT /evidence="ECO:0007829|PDB:5LKM"
FT HELIX 94..104
FT /evidence="ECO:0007829|PDB:5LKM"
FT STRAND 108..114
FT /evidence="ECO:0007829|PDB:5LKM"
FT HELIX 119..129
FT /evidence="ECO:0007829|PDB:5LKM"
FT STRAND 132..137
FT /evidence="ECO:0007829|PDB:5LKM"
FT HELIX 139..141
FT /evidence="ECO:0007829|PDB:5LKM"
FT HELIX 157..170
FT /evidence="ECO:0007829|PDB:5LKM"
FT STRAND 174..180
FT /evidence="ECO:0007829|PDB:5LKM"
FT HELIX 194..196
FT /evidence="ECO:0007829|PDB:5LKM"
FT STRAND 197..204
FT /evidence="ECO:0007829|PDB:5LKM"
FT STRAND 210..222
FT /evidence="ECO:0007829|PDB:5LKM"
FT STRAND 227..232
FT /evidence="ECO:0007829|PDB:5LKM"
FT STRAND 234..239
FT /evidence="ECO:0007829|PDB:5LKM"
FT HELIX 245..250
FT /evidence="ECO:0007829|PDB:5LKQ"
FT STRAND 257..265
FT /evidence="ECO:0007829|PDB:5LKQ"
FT STRAND 268..280
FT /evidence="ECO:0007829|PDB:5LKQ"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:5LKQ"
FT STRAND 288..293
FT /evidence="ECO:0007829|PDB:5LKQ"
FT HELIX 295..309
FT /evidence="ECO:0007829|PDB:5LKQ"
FT STRAND 316..322
FT /evidence="ECO:0007829|PDB:5LKQ"
FT HELIX 323..325
FT /evidence="ECO:0007829|PDB:5LKQ"
FT HELIX 331..333
FT /evidence="ECO:0007829|PDB:5LKQ"
FT HELIX 334..346
FT /evidence="ECO:0007829|PDB:5LKQ"
FT STRAND 354..356
FT /evidence="ECO:0007829|PDB:5LKQ"
FT STRAND 364..367
FT /evidence="ECO:0007829|PDB:5LKQ"
FT HELIX 372..381
FT /evidence="ECO:0007829|PDB:5LKQ"
FT STRAND 385..390
FT /evidence="ECO:0007829|PDB:5LKQ"
FT HELIX 391..393
FT /evidence="ECO:0007829|PDB:5LKQ"
FT TURN 394..396
FT /evidence="ECO:0007829|PDB:5LKQ"
FT STRAND 403..408
FT /evidence="ECO:0007829|PDB:5LKQ"
FT HELIX 411..418
FT /evidence="ECO:0007829|PDB:5LKQ"
SQ SEQUENCE 420 AA; 45806 MW; AB6BC4EB8DA25D42 CRC64;
MEEVEVAEVK NARVSLTGEK TKPMKLAEVT SINVNRTKTE MEEFNRVLGG GVVPGSLVLI
GGDPGIGKST LLLQVSTQLS QVGTVLYVSG EESAQQIKLR AERLGDIDSE FYLYAETNMQ
SVRAEVERIQ PDFLIIDSIQ TIMSPEISGV QGSVSQVREV TAELMQLAKT NNIAIFIVGH
VTKEGTLAGP RMLEHMVDTV LYFEGERHHT FRILRAVKNR FGSTNEIGIF EMQSGGLVEV
LNPSQVFLEE RLDGATGSSI VVTMEGTRPI LAEVQALVTP TMFGNAKRTT TGLDFNRASL
IMAVLEKRAG LLLQNQDAYL KSAGGVKLDE PAIDLAVAVA IASSYKDKPT NPQECFVGEL
GLTGEIRRVN RIEQRINEAA KLGFTKIYVP KNSLTGITLP KEIQVIGVTT IQEVLKKVFA
