ID   RECA_NEICI              Reviewed;         274 AA.
AC   Q59595;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Protein RecA {ECO:0000255|HAMAP-Rule:MF_00268};
DE   AltName: Full=Recombinase A {ECO:0000255|HAMAP-Rule:MF_00268};
DE   Flags: Fragment;
GN   Name=recA {ECO:0000255|HAMAP-Rule:MF_00268};
OS   Neisseria cinerea.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=483;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=LNP 1646;
RX   PubMed=8995060; DOI=10.1007/bf02202111;
RA   Feil E., Zhou J., Maynard Smith J., Spratt B.G.;
RT   "A comparison of the nucleotide sequences of the adk and recA genes of
RT   pathogenic and commensal Neisseria species: evidence for extensive
RT   interspecies recombination within adk.";
RL   J. Mol. Evol. 43:631-640(1996).
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   -!- SIMILARITY: Belongs to the RecA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00268}.
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DR   EMBL; U57906; AAB49191.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q59595; -.
DR   SMR; Q59595; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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; -; 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..>274
FT                   /note="Protein RecA"
FT                   /id="PRO_0000122771"
FT   BINDING         43..50
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
FT   NON_TER         1
FT   NON_TER         274
SQ   SEQUENCE   274 AA;  29602 MW;  4EF5C11097339D94 CRC64;
     SIMKMDGSQQ EENLEVISTG SLGLDLALGV GGLPRGRIVE IFGPESSGKT TLCLEAVAQC
     QKDGGVCAFI DAEHAFDPVY ARKLGVKVEE LYLSQPDTGE QALEICDTLV RSGGVDMVVV
     DSVAALVPKA EIEGDMGDSH VGLHARLMSQ ALRKLTGHIK KTNTLVVFIN QIRMKIGVMF
     GSPETTTGGN ALKFYSSVRL DIRRTGQIKK GEEVIGNETR VKVIKNKVAP PFRQAEFDIL
     YGEGVSWEGE LIDIGVKNDI INKSGAWYSY NGAK