RECA_STRLI
ID RECA_STRLI Reviewed; 374 AA.
AC P48294;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 1.
DT 03-AUG-2022, entry version 100.
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 Streptomyces lividans.
OC Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC Streptomyces.
OX NCBI_TaxID=1916;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=TK24;
RX PubMed=8013883; DOI=10.1111/j.1574-6968.1994.tb06803.x;
RA Nussbaumer B., Wohlleben W.;
RT "Identification, isolation and sequencing of the recA gene of Streptomyces
RT lividans TK24.";
RL FEMS Microbiol. Lett. 118:57-63(1994).
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; X76076; CAA53674.1; -; Genomic_DNA.
DR PIR; S38674; S38674.
DR AlphaFoldDB; P48294; -.
DR SMR; P48294; -.
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..374
FT /note="Protein RecA"
FT /id="PRO_0000122856"
FT REGION 327..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 66..73
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ SEQUENCE 374 AA; 39552 MW; 53FB852B09BA5AC8 CRC64;
MAGTDREKAL DAALAQIERQ FGKGAVMRMG DRTNEPIEVI PTGSTALDVA LGVGGIPRGR
VVEVYGPESS GKTTLTLHAV ANAQKAGGQV AFVDAEHALD PEYAKKLGVD IDNLILSQPD
NGEQALEIVD MLVRSGALDL IVIDSVAALV PRAEIEGEMG DSHVGLQARL MSQALRKITS
ALNQSKTTAI FINQLREKIG VMFGSPETTT GGRALKFYAS VRLDIRRIET LKDGTDAVGN
RTRVKVVKNK VAPPFKQAEF DILYGQGISR EGGLIDMGVE NGFVRKAGAW YTYEGDQLGQ
GKENARNFLK DNPDLANEIE KKIKQKLGVG VHPEESATEP GADAASAAPA DAAPAVPAPT
TAKATKSKAA AAKS
