RECA_NEILA
ID RECA_NEILA Reviewed; 274 AA.
AC P97195;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 97.
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 lactamica.
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=486;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 23970 / DSM 4691 / CCUG 5853 / CIP 72.17 / NCTC 10617 / NCDC
RC A7515;
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).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-254.
RC STRAIN=CCUG 7852, and LCDC 77-143;
RA Smith N.H.;
RL Submitted (MAR-1997) to the EMBL/GenBank/DDBJ databases.
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; Y11819; CAA72504.1; -; Genomic_DNA.
DR EMBL; Y11818; CAA72503.1; -; Genomic_DNA.
DR EMBL; U57905; AAB49194.1; -; Genomic_DNA.
DR AlphaFoldDB; P97195; -.
DR SMR; P97195; -.
DR STRING; 486.B2G52_09295; -.
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_0000122776"
FT BINDING 43..50
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
FT VARIANT 115
FT /note="I -> V (in strain: P63)"
FT NON_TER 1
FT NON_TER 274
SQ SEQUENCE 274 AA; 29549 MW; 0A2B873F1EC4284D CRC64;
AIMKMDGSQQ EENLEVISTG SLGLDLALGV GGLPRGRIVE IFGPESSGKT TLCLEAVAQC
QKNGGVCAFV DAEHAFDPVY ARKLGVKVEE LYLSQPDTGE QALEICDTLV RSGGIDMVVV
DSVAALVPKA EIEGDMGDSH VGLQARLMSQ ALRKLTGHIK KTNTLVVFIN QIRMKIGVMF
GSPETTTGGN ALKFYSSVRL DIRRTGSIKK GEEVLGNETR VKVIKNKVAP PFRQAEFDIL
YGEGISWEGE LIDIGVKNDI INKSGAWYSY NGAK
