RECA_GLUPO
ID RECA_GLUPO Reviewed; 348 AA.
AC Q08327;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 96.
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 Gluconacetobacter polyoxogenes (Acetobacter polyoxogenes).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Gluconacetobacter.
OX NCBI_TaxID=439;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=NBI1028;
RX PubMed=8486287; DOI=10.1016/0378-1119(93)90615-a;
RA Tayama K., Fukaya M., Takemura H., Okumura H., Kawamura Y., Horinouchi S.,
RA Beppu T.;
RT "Cloning and sequencing the recA+ genes of Acetobacter polyoxogenes and
RT Acetobacter aceti: construction of recA-mutants of by transformation-
RT mediated gene replacement.";
RL Gene 127:47-52(1993).
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; D13183; BAA02478.1; -; Genomic_DNA.
DR EMBL; S60629; AAC60438.1; -; Genomic_DNA.
DR PIR; JN0639; JN0639.
DR AlphaFoldDB; Q08327; -.
DR SMR; Q08327; -.
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..348
FT /note="Protein RecA"
FT /id="PRO_0000122630"
FT BINDING 69..76
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ SEQUENCE 348 AA; 37265 MW; B5632992C886982F CRC64;
MAQAPGIDKS KALEGALSQI ERAFGKGSIM RMGERPTEQV DVISTGSLGL DIALGIGGLP
RGRIIEIYGP ESSGKTTMAL HAIAEAQRKG GTCAFIDAEH ALDPGYARKL GVDVDNLLIS
QPDAGEQALE IADTLVRSGA VDVLVVDSVA ALVPRAELEG DMGDSHVGLH ARLMSQALRK
LTGSVSRSNT MLIFLNQIRL KIGVMFGSPE STTGGNALKF YASVRMDIRR IGSIKDKDEV
TGNQTRVKVV KNKMAPPFRQ VEFDIMYGEG ISKVGELIDL GVKAGIVEKS GAWFSCDSQR
IGQGRENAKQ FLRDHPEMAA DIERRVREQA GVVAEAMLVG PDEDGAEH
