ID   RECA_NEISI              Reviewed;         237 AA.
AC   O86411;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Protein RecA;
DE   AltName: Full=Recombinase A;
DE   Flags: Fragment;
GN   Name=recA;
OS   Neisseria sicca.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=490;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 29256 / DSM 17713 / CCUG 23929 / CIP 103345 / LMG 5290 / NRL
RC   30016;
RA   Smith N.H., Donovan G.M., Carpenter A., Spratt B.G.;
RT   "Do sexual bacteria have species?";
RL   Submitted (JAN-1998) 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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RecA family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AJ223872; CAA11603.1; -; Genomic_DNA.
DR   AlphaFoldDB; O86411; -.
DR   SMR; O86411; -.
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   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; 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   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..>237
FT                   /note="Protein RecA"
FT                   /id="PRO_0000122783"
FT   BINDING         26..33
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   NON_TER         1
FT   NON_TER         237
SQ   SEQUENCE   237 AA;  25488 MW;  E4535D5C378E7701 CRC64;
     STGSLGLDLA LGVGGLPRGR VVKIFGPESS GKTTLCLEAI AQCQKNGGIC AFIDAEHAFD
     PVYARKLGIK VEELYLSQPD TGEQALEICD TLVRSGGVDM VVVDSVAALV PKAEIEGEMG
     DSHVGLQARL MSQALRKLTG HIKRTNTLVV FINQIRMKIG VMFGSPETTT GGNALKFYAS
     VRLDIRRTGQ IKKGDDVIGN ETKVKVIKNK VAPPFRQAEF DILYGEGVSW EGELIDL