RECA_ENTFC
ID RECA_ENTFC Reviewed; 349 AA.
AC Q6KCJ6;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
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};
OS Enterococcus faecium (Streptococcus faecium).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1352;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 19434 / DSM 20477 / JCM 5804 / LMG 11423 / NBRC 100485 / NCTC
RC 7171 / WDCM 00010;
RA Torriani S., Felis G.E., Knijff E., Girelli D., Castioni A., Dellaglio F.;
RT "Taxonomic re-evaluation of the genus Enterococcus.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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. It interacts with LexA causing its activation and leading to its
CC autocatalytic cleavage. {ECO:0000255|HAMAP-Rule:MF_00268}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00268}.
CC -!- SIMILARITY: Belongs to the RecA family. {ECO:0000255|HAMAP-
CC Rule:MF_00268}.
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DR EMBL; AJ621707; CAF21832.1; -; Genomic_DNA.
DR RefSeq; WP_002287328.1; NZ_WVTH01000006.1.
DR AlphaFoldDB; Q6KCJ6; -.
DR SMR; Q6KCJ6; -.
DR STRING; 1352.AL014_13320; -.
DR GeneID; 66455535; -.
DR eggNOG; COG0468; Bacteria.
DR OMA; DYGEQAL; -.
DR OrthoDB; 1080436at2; -.
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: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 3: Inferred from homology;
KW ATP-binding; Cytoplasm; DNA damage; DNA recombination; DNA repair;
KW DNA-binding; Nucleotide-binding; SOS response.
FT CHAIN 1..349
FT /note="Protein RecA"
FT /id="PRO_0000122710"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ SEQUENCE 349 AA; 37514 MW; BAEC98F9B4D4D901 CRC64;
MADDRKAALD AALKKIEKSY GKGSIMKLGE KIDQQISTIP SGSLALDVAL GVGGYPRGRI
IEVYGPESSG KTTVALHAIA EVQKNGGTAA FIDAEHALDP QYAQKLGVNI DELLLSQPDT
GEQGLEIADA LVSSGAVDIV VVDSVAALVP RAEIDGEMGD SHVGLQARLM SQALRKLSGS
INKTKTIAIF INQIREKVGV MFGNPEITPG GRALKFYATI RLEVRRAEQL KQGTDIVGNR
TKIKVVKNKV APPFKIAEVD VMYGLGISQE GELLDMAVEK DIVDKSGAWY SYKEDRIGQG
RENAKIYMAN HPEMMAEVSA LVRAAYGIGE EVAVPEDEKG QEELPLVEE
