RECA_STRR6
ID RECA_STRR6 Reviewed; 388 AA.
AC P0A452; P30758;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Protein RecA {ECO:0000255|HAMAP-Rule:MF_00268};
DE AltName: Full=Recombinase A {ECO:0000255|HAMAP-Rule:MF_00268};
GN Name=recA {ECO:0000255|HAMAP-Rule:MF_00268}; OrderedLocusNames=spr1757;
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 NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11, AND INDUCTION.
RX PubMed=7798154; DOI=10.1128/jb.177.1.86-93.1995;
RA Pearce B.J., Naughton A.M., Campbell E.A., Masure H.R.;
RT "The rec locus, a competence-induced operon in Streptococcus pneumoniae.";
RL J. Bacteriol. 177:86-93(1995).
RN [3]
RP FUNCTION, PROTEIN LEVEL, 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 [4]
RP FUNCTION, INTERACTION WITH DPRA, SUBUNIT, AND 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).
CC -!- FUNCTION: Can catalyze the hydrolysis of ATP in the presence of single-
CC stranded DNA, the ATP-dependent uptake of single-stranded DNA by duplex
CC DNA, and the ATP-dependent hybridization of homologous single-stranded
CC DNAs (By similarity). It interacts with LexA causing its activation and
CC leading to its autocatalytic cleavage (By similarity). Required for DNA
CC transformation; protects transforming DNA from degradation, possibly in
CC combination with DprA (PubMed:14617176, PubMed:17803906). Present at
CC 15,000-30,000 monomers per competent cell (PubMed:14617176).
CC {ECO:0000255|HAMAP-Rule:MF_00268, ECO:0000269|PubMed:14617176,
CC ECO:0000305|PubMed:17803906}.
CC -!- SUBUNIT: Interacts with DprA; probably forms mixed DprA-RecA-ssDNA
CC filaments (PubMed:17803906). {ECO:0000269|PubMed:17803906}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00268}.
CC -!- INDUCTION: By competence and DNA damage (PubMed:7798154).
CC {ECO:0000269|PubMed:7798154}.
CC -!- DISRUPTION PHENOTYPE: Loss of DNA transformation; incoming DNA is very
CC rapidly degraded (PubMed:14617176). {ECO:0000269|PubMed:14617176}.
CC -!- SIMILARITY: Belongs to the RecA family. {ECO:0000255|HAMAP-
CC Rule:MF_00268}.
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DR EMBL; AE007317; AAL00560.1; -; Genomic_DNA.
DR EMBL; L36131; AAC09383.1; -; Genomic_DNA.
DR PIR; C98091; C98091.
DR RefSeq; NP_359349.1; NC_003098.1.
DR RefSeq; WP_001085462.1; NC_003098.1.
DR AlphaFoldDB; P0A452; -.
DR SMR; P0A452; -.
DR STRING; 171101.spr1757; -.
DR EnsemblBacteria; AAL00560; AAL00560; spr1757.
DR GeneID; 60233092; -.
DR GeneID; 66807012; -.
DR KEGG; spr:spr1757; -.
DR PATRIC; fig|171101.6.peg.1898; -.
DR eggNOG; COG0468; Bacteria.
DR HOGENOM; CLU_040469_3_2_9; -.
DR OMA; DYGEQAL; -.
DR PHI-base; PHI:4702; -.
DR Proteomes; UP000000586; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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:UniProtKB-UniRule.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:UniProtKB-UniRule.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-UniRule.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-UniRule.
DR GO; GO:0030420; P:establishment of competence for transformation; IMP:UniProtKB.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR CDD; cd00983; recA; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00268; RecA; 1.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR013765; DNA_recomb/repair_RecA.
DR InterPro; IPR020584; DNA_recomb/repair_RecA_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR020588; RecA_ATP-bd.
DR InterPro; IPR023400; RecA_C.
DR InterPro; IPR020587; RecA_monomer-monomer_interface.
DR PANTHER; PTHR45900; PTHR45900; 1.
DR Pfam; PF00154; RecA; 1.
DR PRINTS; PR00142; RECA.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54752; SSF54752; 1.
DR TIGRFAMs; TIGR02012; tigrfam_recA; 1.
DR PROSITE; PS00321; RECA_1; 1.
DR PROSITE; PS50162; RECA_2; 1.
DR PROSITE; PS50163; RECA_3; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Competence; Cytoplasm; DNA damage; DNA recombination;
KW DNA repair; DNA-binding; Nucleotide-binding; Reference proteome;
KW SOS response.
FT CHAIN 1..388
FT /note="Protein RecA"
FT /id="PRO_0000122860"
FT REGION 347..388
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 374..388
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 79..86
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ SEQUENCE 388 AA; 41950 MW; 40F5DA5F15E1BCB3 CRC64;
MAKKPKKLEE ISKKFGAERE KALNDALKLI EKDFGKGSIM RLGERAEQKV QVMSSGSLAL
DIALGSGGYP KGRIIEIYGP ESSGKTTVAL HAVAQAQKEG GIAAFIDAEH ALDPAYAAAL
GVNIDELLLS QPDSGEQGLE IAGKLIDSGA VDLVVVDSVA ALVPRAEIDG DIGDSHVGLQ
ARMMSQAMRK LGASINKTKT IAIFINQLRE KVGVMFGNPE TTPGGRALKF YASVRLDVRG
NTQIKGTGDQ KETNVGKETK IKVVKNKVAP PFKEAVVEIM YGEGISKTGE LLKIASDLDI
IKKAGAWYSY KDEKIGQGSE NAKKYLAEHP EIFDEIDKQV RSKFGLIDGE EVSEQDTENK
KDEPKKEEAV NEEVPLDLGD ELEIEIEE
