ID E3UK10_9BURK Unreviewed; 313 AA.
AC E3UK10;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
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:ADO21594.1};
OS Burkholderia arboris.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=488730 {ECO:0000313|EMBL:ADO21594.1};
RN [1] {ECO:0000313|EMBL:ADO21594.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=HP56 {ECO:0000313|EMBL:ADO21601.1}, HT12
RC {ECO:0000313|EMBL:ADO21604.1}, HT28 {ECO:0000313|EMBL:ADO21619.1},
RC HT59 {ECO:0000313|EMBL:ADO21605.1}, HT70
RC {ECO:0000313|EMBL:ADO21617.1}, HT86 {ECO:0000313|EMBL:ADO21609.1},
RC YP14 {ECO:0000313|EMBL:ADO21610.1}, YP17
RC {ECO:0000313|EMBL:ADO21614.1}, YP19 {ECO:0000313|EMBL:ADO21618.1},
RC YT10 {ECO:0000313|EMBL:ADO21606.1}, YT12
RC {ECO:0000313|EMBL:ADO21608.1}, YT16 {ECO:0000313|EMBL:ADO21602.1},
RC YT18 {ECO:0000313|EMBL:ADO21611.1}, YT21
RC {ECO:0000313|EMBL:ADO21612.1}, YT22 {ECO:0000313|EMBL:ADO21603.1},
RC YT23 {ECO:0000313|EMBL:ADO21613.1}, YT35
RC {ECO:0000313|EMBL:ADO21615.1}, YT44 {ECO:0000313|EMBL:ADO21600.1}, ZP7
RC {ECO:0000313|EMBL:ADO21594.1}, ZP8 {ECO:0000313|EMBL:ADO21595.1}, ZT10
RC {ECO:0000313|EMBL:ADO21616.1}, ZT29 {ECO:0000313|EMBL:ADO21607.1},
RC ZT37 {ECO:0000313|EMBL:ADO21596.1}, ZT54
RC {ECO:0000313|EMBL:ADO21597.1}, ZT55 {ECO:0000313|EMBL:ADO21598.1}, and
RC ZT78 {ECO:0000313|EMBL:ADO21599.1};
RX PubMed=20882285; DOI=10.1007/s00284-010-9758-3;
RA Lou M., Fang Y., Zhang G., Xie G., Zhu B., Ibrahim M.;
RT "Diversity of Burkholderia cepacia complex from the Moso bamboo
RT (Phyllostachys edulis) rhizhosphere soil.";
RL Curr. Microbiol. 62:650-658(2011).
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; HM446283; ADO21594.1; -; Genomic_DNA.
DR EMBL; HM446284; ADO21595.1; -; Genomic_DNA.
DR EMBL; HM446285; ADO21596.1; -; Genomic_DNA.
DR EMBL; HM446286; ADO21597.1; -; Genomic_DNA.
DR EMBL; HM446287; ADO21598.1; -; Genomic_DNA.
DR EMBL; HM446288; ADO21599.1; -; Genomic_DNA.
DR EMBL; HM446289; ADO21600.1; -; Genomic_DNA.
DR EMBL; HM446290; ADO21601.1; -; Genomic_DNA.
DR EMBL; HM446291; ADO21602.1; -; Genomic_DNA.
DR EMBL; HM446292; ADO21603.1; -; Genomic_DNA.
DR EMBL; HM446293; ADO21604.1; -; Genomic_DNA.
DR EMBL; HM446294; ADO21605.1; -; Genomic_DNA.
DR EMBL; HM446295; ADO21606.1; -; Genomic_DNA.
DR EMBL; HM446296; ADO21607.1; -; Genomic_DNA.
DR EMBL; HM446297; ADO21608.1; -; Genomic_DNA.
DR EMBL; HM446298; ADO21609.1; -; Genomic_DNA.
DR EMBL; HM446299; ADO21610.1; -; Genomic_DNA.
DR EMBL; HM446300; ADO21611.1; -; Genomic_DNA.
DR EMBL; HM446301; ADO21612.1; -; Genomic_DNA.
DR EMBL; HM446302; ADO21613.1; -; Genomic_DNA.
DR EMBL; HM446303; ADO21614.1; -; Genomic_DNA.
DR EMBL; HM446304; ADO21615.1; -; Genomic_DNA.
DR EMBL; HM446305; ADO21616.1; -; Genomic_DNA.
DR EMBL; HM446306; ADO21617.1; -; Genomic_DNA.
DR EMBL; HM446307; ADO21618.1; -; Genomic_DNA.
DR EMBL; HM446308; ADO21619.1; -; Genomic_DNA.
DR AlphaFoldDB; E3UK10; -.
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 16..175
FT /note="RecA family profile 1"
FT /evidence="ECO:0000259|PROSITE:PS50162"
FT DOMAIN 180..253
FT /note="RecA family profile 2"
FT /evidence="ECO:0000259|PROSITE:PS50163"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ADO21594.1"
FT NON_TER 313
FT /evidence="ECO:0000313|EMBL:ADO21594.1"
SQ SEQUENCE 313 AA; 33693 MW; 96A58D27829BFD86 CRC64;
GKGSIMRMGD GEAAENIQVV STGSLGLDIA LGVGGLPRGR VVEIYGPESS GKTTLTLQVI
AELQKLGGTA AFIDAEHALD VQYAAKLGVN VPELLISQPD TGEQALEITD ALVRSGSIDM
IVIDSVAALV PKAEIEGEMG DSLPGLQARL MSQALRKLTG TIKRTNCLVI FINQIRMKIG
VMFGNPETTT GGNALKFYSS VRLDIRRIGS IKKNDEVIGN ETRVKVVKNK VSPPFREAIF
DILYGEGISR QGEIIDLGVQ AKIVDKAGAW YSYNGEKIGQ GKDNAREFLR ENPEIAREIE
NRIRESLGVV SMP
//
