ID   RECA_HERSE              Reviewed;         351 AA.
AC   Q9F672;
DT   16-APR-2002, integrated into UniProtKB/Swiss-Prot.
DT   15-AUG-2003, sequence version 2.
DT   03-AUG-2022, entry version 94.
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   Herbaspirillum seropedicae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herbaspirillum.
OX   NCBI_TaxID=964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND INDUCTION.
RX   PubMed=12718403; DOI=10.1139/w03-010;
RA   Galvao C.W., Pedrosa F.O., Souza E.M., Yates M.G., Chubatsu L.S.,
RA   Steffens M.B.R.;
RT   "The recX gene product is involved in the SOS response in Herbaspirillum
RT   seropedicae.";
RL   Can. J. Microbiol. 49:145-150(2003).
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:0000255|HAMAP-Rule:MF_00268}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00268}.
CC   -!- INDUCTION: By methyl methanesulfonate. {ECO:0000269|PubMed:12718403}.
CC   -!- SIMILARITY: Belongs to the RecA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00268}.
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DR   EMBL; AF297289; AAG13409.2; -; Genomic_DNA.
DR   RefSeq; WP_013232692.1; NZ_JWZZ01000002.1.
DR   AlphaFoldDB; Q9F672; -.
DR   SMR; Q9F672; -.
DR   PATRIC; fig|964.11.peg.677; -.
DR   OMA; DYGEQAL; -.
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; SOS response.
FT   CHAIN           1..351
FT                   /note="Protein RecA"
FT                   /id="PRO_0000122727"
FT   BINDING         73..80
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ   SEQUENCE   351 AA;  37472 MW;  76279A7186A1DCA0 CRC64;
     MDDKKAANNS EKSKALAAAL AQIEKQFGKG SVMRMEDGVI AEEIQAVSTG SLGLDIALGI
     GGLPRGRVIE IYGPESSGKT TLTLQSIAEM QKLGGTCAFI DAEHALDVTY AQKLGVNLND
     LLISQPDTGE QALEICDALV RSGAVDLIVV DSVAALTPKA EIEGDMGDSL PGLQARLMSQ
     ALRKLTGSIN RTNTTVIFIN QIRMKIGVMF GNPETTTGGN ALKFYASVRL DIRRTGSIKS
     GDEVIGSETK VKVVKNKVAP PFREAHFDIL YGEGTSREGE ILDLGSEHKV VEKSGAWYSY
     NGERIGQGKD NARNYLKEHP ELAREIENKV RVALGVPELA GGEAEAEAKA S