ID A0A086_9BURK Unreviewed; 347 AA.
AC A0A086;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 24-JAN-2024, entry version 80.
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:ABJ74752.1};
OS Burkholderia sp. M317.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia.
OX NCBI_TaxID=406779 {ECO:0000313|EMBL:ABJ74752.1};
RN [1] {ECO:0000313|EMBL:ABJ74752.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=M317 {ECO:0000313|EMBL:ABJ74752.1};
RA Zhang L.X., Xie G.L.;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABJ74752.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=M317 {ECO:0000313|EMBL:ABJ74752.1};
RX PubMed=17233735; DOI=10.1111/j.1574-6968.2006.00530.x;
RA Zhang L., Xie G.;
RT "Diversity and distribution of Burkholderia cepacia complex in the
RT rhizosphere of rice and maize.";
RL FEMS Microbiol. Lett. 266:231-235(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; DQ989511; ABJ74752.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A086; -.
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|RuleBase:RU004527};
KW DNA recombination {ECO:0000256|ARBA:ARBA00023172,
KW ECO:0000256|RuleBase:RU004527}; DNA repair {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 36..195
FT /note="RecA family profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50162"
FT DOMAIN 200..273
FT /note="RecA family profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50163"
FT NON_TER 347
FT /evidence="ECO:0000313|EMBL:ABJ74752.1"
SQ SEQUENCE 347 AA; 37315 MW; 4F5CAA9E6EF1517C CRC64;
MTAEKSKALA AALAQIEKQF GKGSIMRMGD GEAAENIQVV STGSPGLDIA LGVGGLPRGR
VVEIYGPESS GKTTLTLQVI AELQKIGGTA AFIDAEHALD VQYASKLGVN VPELLISQPD
TGEQALEITD ALVRSGSIDM IVIDSVAALV PKAEIEGEMG DSLPGLQARL MSQALRKLTG
TIKRTNCLVI FINQIRMKIG VMFGNPETTT GGNALKFYSS VRLDIRRIGS IKKNDEVIGN
ETRVKVVKNK VSPPFREAIF DILYGEGISR QGEIIDLGVQ AKIVDKAGAW YSYNGEKIGQ
GKDNAREFLR ENPEIAREIE NRIRESLGVV SMPDGVANEA EAMDEEE
//