RECA_THEAQ
ID RECA_THEAQ Reviewed; 340 AA.
AC P48296;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, 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 Thermus aquaticus.
OC Bacteria; Deinococcus-Thermus; Deinococci; Thermales; Thermaceae; Thermus.
OX NCBI_TaxID=271;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 25104 / DSM 625 / JCM 10724 / NBRC 103206 / NCIMB 11243 / YT-1;
RX PubMed=8113181; DOI=10.1128/jb.176.5.1405-1412.1994;
RA Angov E., Camerini-Otero R.D.;
RT "The recA gene from the thermophile Thermus aquaticus YT-1: cloning,
RT expression, and characterization.";
RL J. Bacteriol. 176:1405-1412(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7929298; DOI=10.1016/s0021-9258(18)47335-8;
RA Wetmur J.G., Wong D.M., Ortiz B., Tong J., Reichert F., Gelfand D.H.;
RT "Cloning, sequencing, and expression of RecA proteins from three distantly
RT related thermophilic eubacteria.";
RL J. Biol. Chem. 269:25928-25935(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.
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; L20680; AAA19796.1; -; Unassigned_DNA.
DR EMBL; L20095; AAA27502.1; -; Genomic_DNA.
DR PIR; A53378; A53378.
DR AlphaFoldDB; P48296; -.
DR SMR; P48296; -.
DR DIP; DIP-61165N; -.
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..340
FT /note="Protein RecA"
FT /id="PRO_0000122879"
FT BINDING 65..72
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ SEQUENCE 340 AA; 36454 MW; 0411D8437623A7AA CRC64;
MEENKRKSLE NALKTIEKEF GKGAVMRLGE MPKLQVDVIP TGSLGLDLAL GIGGIPRGRV
TEIFGPESGG KTTLALTIIA QAQKGGGVAA FVDAEHALDP LYAKKLGVDV QELLVSQPDT
GEQALEIVEL LARSGAVDVI VVDSVAALVP KAEIEGEMGD QHVGLQARLM SQALRKLTAV
LSKSNTAAIF INQVREKVGV MYGNPETTPG GRALKFYSSV RLDVRKSGQP IKVGNEAVGI
KVKVKVVKNK LAPPFREAEL EIYFGRGLDP VMDLVNVAVA AGVIEKAGSW FSYGEHRLGQ
GKEKAAEYLR ERPELLEEIR AKVLERADKV VLAAGEEEGE