ID   RECA_BORPE              Reviewed;         353 AA.
AC   P0A448; P17740;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   03-AUG-2022, entry version 96.
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=BP2546;
OS   Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257313;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=165;
RX   PubMed=2377463; DOI=10.1093/nar/18.14.4243;
RA   Favre D., Viret J.F.;
RT   "Nucleotide sequence of the recA gene of Bordetella pertussis.";
RL   Nucleic Acids Res. 18:4243-4243(1990).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=165;
RX   PubMed=1832021; DOI=10.1016/0300-9084(91)90208-i;
RA   Favre D., Cryz S.J. Jr., Viret J.F.;
RT   "Cloning of the recA gene of Bordetella pertussis and characterization of
RT   its product.";
RL   Biochimie 73:235-244(1991).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251;
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(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.
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; X53457; CAA37537.1; -; Genomic_DNA.
DR   EMBL; BX640418; CAE42821.1; -; Genomic_DNA.
DR   PIR; S10499; S10499.
DR   RefSeq; NP_881173.1; NC_002929.2.
DR   RefSeq; WP_003812760.1; NZ_CP039022.1.
DR   AlphaFoldDB; P0A448; -.
DR   SMR; P0A448; -.
DR   STRING; 257313.BP2546; -.
DR   GeneID; 56478250; -.
DR   GeneID; 66438325; -.
DR   KEGG; bpe:BP2546; -.
DR   PATRIC; fig|257313.5.peg.2746; -.
DR   eggNOG; COG0468; Bacteria.
DR   HOGENOM; CLU_040469_1_2_4; -.
DR   OMA; DYGEQAL; -.
DR   Proteomes; UP000002676; Chromosome.
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; Reference proteome; SOS response.
FT   CHAIN           1..353
FT                   /note="Protein RecA"
FT                   /id="PRO_0000122668"
FT   BINDING         74..81
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
FT   CONFLICT        66..68
FT                   /note="RGR -> AA (in Ref. 1 and 2)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   353 AA;  37949 MW;  6FDFD3FB6A7F1F95 CRC64;
     MDDKTSKAAA AEKAKALAAA LSQIEKQFGK GSIMRYGDNE VEHDIQVVST GSLGLDIALG
     VGGLPRGRVI EVYGPESSGK TTLTLQVIAE MQKLGGTCAF VDAEHALDVQ YASKLGVNLT
     DLLISQPDTG EQALEITDAL VRSGSVDLIV IDSVAALVPK AEIEGEMGDS LPGLQARLMS
     QALRKLTATI KRTNCMVIFI NQIRMKIGVM FGNPETTTGG NALKFYSSVR LDIRRIGAIK
     KGDEVVGNET RVKVVKNKVA PPFKQAEFDI MYGSGISREG EIIDLGVQAN VVDKSGAWYS
     YSGNRIGQGK DNVREYLKEH KEMAIEIENK VRENQGIVSR AATFPASEAE DGE