RECA_BRUA2
ID RECA_BRUA2 Reviewed; 361 AA.
AC Q2YRU7; Q04761; Q57CT9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
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}; OrderedLocusNames=BAB1_1224;
OS Brucella abortus (strain 2308).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=2308;
RX PubMed=8321120; DOI=10.1006/mpat.1993.1018;
RA Tatum F.M., Morfitt D.C., Halling S.M.;
RT "Construction of a Brucella abortus RecA mutant and its survival in mice.";
RL Microb. Pathog. 14:177-185(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308;
RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
RN [3]
RP FUNCTION, INDUCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=2308;
RX PubMed=16816190; DOI=10.1128/jb.01994-05;
RA Roux C.M., Booth N.J., Bellaire B.H., Gee J.M., Roop R.M. II, Kovach M.E.,
RA Tsolis R.M., Elzer P.H., Ennis D.G.;
RT "RecA and RadA proteins of Brucella abortus do not perform overlapping
RT protective DNA repair functions following oxidative burst.";
RL J. Bacteriol. 188:5187-5195(2006).
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 (By similarity). Interacts with LexA causing LexA activation and
CC leading to its autocatalytic cleavage (PubMed:16816190). High basal
CC expression of RecA may be important in slowly-dividing Brucella for
CC intracellular survival in its hostile host (PubMed:16816190).
CC {ECO:0000255|HAMAP-Rule:MF_00268, ECO:0000305|PubMed:16816190}.
CC -!- FUNCTION: Confers methyl methanesulfonate (MMS) resistance to an E.coli
CC recA deletion mutant (PubMed:8321120). This protein is constitutively
CC activated; its expression in an E.coli recA deletion leads to
CC constitutive expression from a recA reporter gene. Presumably it
CC constitutively activates LexA autocleavage, but no data was published
CC (PubMed:16816190). {ECO:0000269|PubMed:16816190,
CC ECO:0000269|PubMed:8321120}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00268}.
CC -!- INDUCTION: Constitutively expressed at a high level with 2-fold further
CC induction by mitomycin C treatment. Positively autoregulated.
CC {ECO:0000269|PubMed:16816190}.
CC -!- DISRUPTION PHENOTYPE: Greatly increased sensitivity to MMS, decreased
CC bacterial load in BALB/c mice, but bacteria still persist 100 days
CC after peritoneal injection (PubMed:8321120). Increased sensitivity to
CC UV light (but considerably less than expected compared to E.coli),
CC hypersensitivity to MMS, slightly increased sensitivity to H(2)O(2).
CC Loss of mitomycin C-induced expression from a recA promoter. 4-fold
CC less survival in mouse macrophages, where the bacteria has to survive
CC an extremely hostile environment (PubMed:16816190).
CC {ECO:0000269|PubMed:16816190, ECO:0000269|PubMed:8321120}.
CC -!- SIMILARITY: Belongs to the RecA family. {ECO:0000255|HAMAP-
CC Rule:MF_00268}.
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DR EMBL; L00679; AAA22999.1; -; Genomic_DNA.
DR EMBL; AM040264; CAJ11180.1; -; Genomic_DNA.
DR PIR; I40347; I40347.
DR RefSeq; WP_002964332.1; NZ_KN046823.1.
DR AlphaFoldDB; Q2YRU7; -.
DR SMR; Q2YRU7; -.
DR STRING; 359391.BAB1_1224; -.
DR EnsemblBacteria; CAJ11180; CAJ11180; BAB1_1224.
DR GeneID; 45124571; -.
DR GeneID; 55590878; -.
DR KEGG; bmf:BAB1_1224; -.
DR PATRIC; fig|359391.11.peg.123; -.
DR HOGENOM; CLU_040469_3_2_5; -.
DR OMA; DYGEQAL; -.
DR PRO; PR:Q2YRU7; -.
DR Proteomes; UP000002719; Chromosome I.
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 2: Evidence at transcript level;
KW ATP-binding; Cytoplasm; DNA damage; DNA recombination; DNA repair;
KW DNA-binding; Nucleotide-binding; Reference proteome; SOS response.
FT CHAIN 1..361
FT /note="Protein RecA"
FT /id="PRO_1000047893"
FT BINDING 77..84
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
FT CONFLICT 121
FT /note="D -> H (in Ref. 1; AAA22999)"
FT /evidence="ECO:0000305"
FT CONFLICT 131
FT /note="D -> I (in Ref. 1; AAA22999)"
FT /evidence="ECO:0000305"
FT CONFLICT 174..175
FT /note="LP -> H (in Ref. 1; AAA22999)"
FT /evidence="ECO:0000305"
FT CONFLICT 186
FT /note="L -> V (in Ref. 1; AAA22999)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 361 AA; 38735 MW; 6E15766D33E5756E CRC64;
MSQNSLRLVE DNSVDKTKAL DAALSQIERA FGKGSIMRLG QNDQVVEIET VSTGSLSLDI
ALGVGGLPKG RIVEIYGPES SGKTTLALHT IAEAQKKGGI CAFVDAEHAL DPVYARKLGV
DLENLLISQP DTGEQALEIT DTLVRSGAID VLVVDSVAAL TPRAEIEGEM GDSLPGLQAR
LMSQALRKLT GSISRSNCMV IFINQIRMKI GVMFGSPETT TGGNALKFYA SVRLDIRRIG
SIKERDEVVG NQTRVKVVKN KLAPPFKQVE FDIMYGAGVS KVGELVDLGV KAGVVEKSGA
WFSYNSQRLG QGRENAKQYL KDNPEVAREI ETTLRQNAGL IAEQFLDDGG PEEDAAGAAE
M
