ID A8CT60_9BURK Unreviewed; 317 AA.
AC A8CT60;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 77.
DE RecName: Full=Protein RecA {ECO:0000256|ARBA:ARBA00015553, ECO:0000256|RuleBase:RU000526};
DE AltName: Full=Recombinase A {ECO:0000256|RuleBase:RU000526};
DE Flags: Fragment;
GN Name=recA {ECO:0000313|EMBL:ABV44564.1};
OS Burkholderia cenocepacia.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=95486 {ECO:0000313|EMBL:ABV44564.1};
RN [1] {ECO:0000313|EMBL:ABV44564.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=P207 {ECO:0000313|EMBL:ABV44564.1};
RX PubMed=17855569; DOI=10.1128/JCM.01606-07;
RA Pimentel J.D., Dubedat S.M., Dodds E.L., Benn R.A.;
RT "Identification of isolates within the Burkholderia cepacia complex by a
RT multiplex recA and 16S rRNA gene real-time PCR assay.";
RL J. Clin. Microbiol. 45:3853-3854(2007).
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:0000256|ARBA:ARBA00025580}.
CC -!- SIMILARITY: Belongs to the RecA family. {ECO:0000256|ARBA:ARBA00009391,
CC ECO:0000256|RuleBase:RU004527}.
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DR EMBL; EF427802; ABV44564.1; -; Genomic_DNA.
DR AlphaFoldDB; A8CT60; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0140664; F:ATP-dependent DNA damage sensor activity; IEA:InterPro.
DR GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR GO; GO:0006310; P:DNA recombination; IEA:UniProtKB-KW.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-KW.
DR CDD; cd00983; RecA; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR049261; RecA-like_C.
DR InterPro; IPR049428; RecA-like_N.
DR InterPro; IPR020588; RecA_ATP-bd.
DR InterPro; IPR023400; RecA_C_sf.
DR InterPro; IPR020587; RecA_monomer-monomer_interface.
DR NCBIfam; TIGR02012; tigrfam_recA; 1.
DR PANTHER; PTHR45900:SF1; MITOCHONDRIAL DNA REPAIR PROTEIN RECA HOMOLOG-RELATED; 1.
DR PANTHER; PTHR45900; RECA; 1.
DR Pfam; PF00154; RecA; 1.
DR Pfam; PF21096; RecA_C; 1.
DR PRINTS; PR00142; RECA.
DR SMART; SM00382; AAA; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF54752; RecA protein, C-terminal domain; 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 {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU004527};
KW DNA damage {ECO:0000256|ARBA:ARBA00022763, ECO:0000256|RuleBase:RU004527};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172,
KW ECO:0000256|RuleBase:RU004527};
KW DNA repair {ECO:0000256|ARBA:ARBA00023204, ECO:0000256|RuleBase:RU000526};
KW DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|RuleBase:RU004527};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU004527};
KW SOS response {ECO:0000256|RuleBase:RU000526}.
FT DOMAIN 20..179
FT /note="RecA family profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50162"
FT DOMAIN 184..257
FT /note="RecA family profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50163"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ABV44564.1"
FT NON_TER 317
FT /evidence="ECO:0000313|EMBL:ABV44564.1"
SQ SEQUENCE 317 AA; 34271 MW; EDF09A2B5926C26B CRC64;
EKQFGKGSIM RMGDGEAAEN IQVVSTGSLG LDIALGVGGL PRGRVVEIYG PESSGKTTLT
LQVIAELQKI GGTAAFIDAE HALDVQYASK LGVNVPELLI SQPDTGEQAL EITDALVRSG
SIDMIVIDSV AALVPKAEIE GEMGDSLPGL QARLMSQALR KLTGTIKRTN CLVIFINQIR
MKIGVMFGNP ETTTGGNALK FYSSVRLDIR RIGSIKKNDE VIGNETRVKV VKNKVSPPFR
EAIFDILYGE SISRQGEIID LGVQAKIVDK AGAWYSYNGE KIGQGKDNAR EFLRENPEIA
REIENRIRES LGVVSMP
//
