RECA_BLAVI
ID RECA_BLAVI Reviewed; 348 AA.
AC Q9ZIQ0;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 91.
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 Blastochloris viridis (Rhodopseudomonas viridis).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Blastochloridaceae; Blastochloris.
OX NCBI_TaxID=1079;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 19567 / DSM 133 / F;
RX PubMed=9620976; DOI=10.1128/jb.180.12.3227-3232.1998;
RA Chen I.P., Michel H.;
RT "Cloning, sequencing, and characterization of the recA gene from
RT Rhodopseudomonas viridis and construction of a recA strain.";
RL J. Bacteriol. 180:3227-3232(1998).
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.
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; AF022175; AAC64504.1; -; Genomic_DNA.
DR RefSeq; WP_055036696.1; NZ_LN907867.1.
DR AlphaFoldDB; Q9ZIQ0; -.
DR SMR; Q9ZIQ0; -.
DR STRING; 1079.BVIR_1014; -.
DR OMA; DYGEQAL; -.
DR OrthoDB; 1080436at2; -.
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_0000122820"
FT BINDING 64..71
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ SEQUENCE 348 AA; 36926 MW; D3D3F3B303EE4BA1 CRC64;
MDKTKALDAA LTQIERAFGK GSIMRLGKSG AALEVETIST GSLGLDIALG IGGLPRGRVV
EIFGPESSGK TTLALHTVAE AQKKGGVCAF IDAEHALDPL YARKLGVNLD DLLISQPDAG
EQALEIADTL VRSGAIDVLV VDSVAALVPR AELEGEMGDS QPGMQARLMS QALRKLTASI
SRSNCMVIFI NQIRMKIGVM YGSPETTTGG NALKFYASVR LDIRRIGAIK ERDEVVGNQT
RVKVVKNKLA PPFKQVEFDI MYGEGISKAG ELIDLGVKAG VVDKSGSWFS HDSQRIGQGR
ENVKGFLKGH PDVAGRIEAA IRQNAGLIAE RILGSSEDSE DGEDAAEA