RECA_ACIFI
ID RECA_ACIFI Reviewed; 346 AA.
AC P16238;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 1.
DT 03-AUG-2022, entry version 105.
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 Acidithiobacillus ferridurans.
OC Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=1232575;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33020 / DSM 29468 / JCM 18981 / 11Fe;
RX PubMed=2504646; DOI=10.1016/0378-1119(89)90308-9;
RA Ramesar R.S., Abratt V., Woods D.R., Rawlings D.E.;
RT "Nucleotide sequence and expression of a cloned Thiobacillus ferrooxidans
RT recA gene in Escherichia coli.";
RL Gene 78:1-8(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 297-346.
RC STRAIN=ATCC 33020 / DSM 29468 / JCM 18981 / 11Fe;
RX PubMed=9245807; DOI=10.1099/00221287-143-7-2179;
RA Guiliani N., Bengrine A., Borne F., Chippaux M., Bonnefoy V.;
RT "Alanyl-tRNA synthetase gene of the extreme acidophilic
RT chemolithoautotrophic Thiobacillus ferrooxidans is highly homologous to
RT alaS genes from all living kingdoms but cannot be transcribed from its
RT promoter in Escherichia coli.";
RL Microbiology 143:2179-2187(1997).
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.
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; M26933; AAA27385.1; -; Genomic_DNA.
DR EMBL; X95571; CAA64816.1; -; Genomic_DNA.
DR PIR; JU0051; RQBCAT.
DR AlphaFoldDB; P16238; -.
DR SMR; P16238; -.
DR STRING; 380394.Lferr_1050; -.
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..346
FT /note="Protein RecA"
FT /id="PRO_0000122884"
FT BINDING 66..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ SEQUENCE 346 AA; 37096 MW; 2FAC69A491EBDC22 CRC64;
MDEQRSKGLS AALSQIDKQF GKGAVMRLGD HNAIKDIEVY STGSLGLDLA LGVGGLPRGR
VVEIYGPESS GKTTLTLHAI ASCQAAGGTA AFIDAEHALD PGYAHKLGVD LENLLISQPD
TGEQALEIAD MLVRSGAVDL IVIDSVAALT PKAEIEGEMG DSHVGLQARL MSQALRNLTA
NISRSNTLVI FINQIRMKIG VMYGSPETTT GGNALKFYAS VRLDIRRIGA IKKSDEVVGN
DTRVKVVKNK VAPPFREAEF AIYYGEGISR LSELVDLGVK FDIVEKSGAW YSYQGHRIGQ
GKDNARQYLK VHPELAANIE QRIRAAAAGH PLAFAEEVES PQRSAS