RECA_CUTAC
ID RECA_CUTAC Reviewed; 348 AA.
AC P0CZ02; Q6A902;
DT 28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT 28-JUN-2011, sequence version 1.
DT 03-AUG-2022, entry version 52.
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 Cutibacterium acnes (Propionibacterium acnes).
OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC Cutibacterium.
OX NCBI_TaxID=1747;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=AT1, CK17, JMK9, JR2, L1958, LED2, MMG9, NCTC 737, P135, P136, P6,
RC P9, PV37, PV58, PV93, RM1, RM9, TON9, W1034, W1392, W1973, W1998, W513,
RC W633, W891, and WMK9;
RX PubMed=15634990; DOI=10.1128/jcm.43.1.326-334.2005;
RA McDowell A., Valanne S., Ramage G., Tunney M.M., Glenn J.V.,
RA McLorinan G.C., Bhatia A., Maisonneuve J.F., Lodes M., Persing D.H.,
RA Patrick S.;
RT "Propionibacterium acnes types I and II represent phylogenetically distinct
RT groups.";
RL J. Clin. Microbiol. 43:326-334(2005).
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; AY642055; AAT69987.1; -; Genomic_DNA.
DR EMBL; AY642056; AAT69988.1; -; Genomic_DNA.
DR EMBL; AY642059; AAT69991.1; -; Genomic_DNA.
DR EMBL; AY642060; AAT69992.1; -; Genomic_DNA.
DR EMBL; AY642063; AAT69995.1; -; Genomic_DNA.
DR EMBL; AY642068; AAT70000.1; -; Genomic_DNA.
DR EMBL; AY642070; AAT70002.1; -; Genomic_DNA.
DR EMBL; AY642071; AAT70003.1; -; Genomic_DNA.
DR EMBL; AY642072; AAT70004.1; -; Genomic_DNA.
DR EMBL; AY642073; AAT70005.1; -; Genomic_DNA.
DR EMBL; AY642074; AAT70006.1; -; Genomic_DNA.
DR EMBL; AY642075; AAT70007.1; -; Genomic_DNA.
DR EMBL; AY642076; AAT70008.1; -; Genomic_DNA.
DR EMBL; AY642077; AAT70009.1; -; Genomic_DNA.
DR EMBL; AY642078; AAT70010.1; -; Genomic_DNA.
DR EMBL; AY642079; AAT70011.1; -; Genomic_DNA.
DR EMBL; AY642080; AAT70012.1; -; Genomic_DNA.
DR EMBL; AY642081; AAT70013.1; -; Genomic_DNA.
DR EMBL; AY642082; AAT70014.1; -; Genomic_DNA.
DR EMBL; AY642086; AAT70018.1; -; Genomic_DNA.
DR EMBL; AY642092; AAT70024.1; -; Genomic_DNA.
DR EMBL; AY642093; AAT70025.1; -; Genomic_DNA.
DR EMBL; AY642094; AAT70026.1; -; Genomic_DNA.
DR EMBL; AY642095; AAT70027.1; -; Genomic_DNA.
DR EMBL; AY642096; AAT70028.1; -; Genomic_DNA.
DR EMBL; AY642097; AAT70029.1; -; Genomic_DNA.
DR RefSeq; WP_002515492.1; NZ_WOWJ01000002.1.
DR AlphaFoldDB; P0CZ02; -.
DR SMR; P0CZ02; -.
DR GeneID; 66621126; -.
DR OMA; DYGEQAL; -.
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_0000410487"
FT BINDING 67..74
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ SEQUENCE 348 AA; 37153 MW; 5AD390E0990469D6 CRC64;
MAATADREKA LATALQQIEK QHGKGSIMRL GEQETVKIAA IPTGSVALDV ALGVGGLPRG
RIVEIYGPES SGKTTVALHA IANAQAEGGI CAFIDAEHAL DPEYARKLGV DTDSLLVSQP
DNGEQALEIA DTLVRSGALE LIVVDSVAAL TPKAEIEGEM GDSHVGLQAR LMSQALRKMT
GALNAAGTTA IFINQLREKI GVMFGSPETT TGGRALKFYS SVRLDVRRVE TLKDGSEMVG
NRTRVKVAKN KVAPPFKQAE FDILYGQGIS REGSLIDMGV DCGIITKSGS WFSYNNEQLG
QGKENVRKFL RGNPDVANEI EDKILTHLGL REAEVPEGVD PRTGEVEF
