ID   RECA_SYNY3              Reviewed;         354 AA.
AC   P74737;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   03-AUG-2022, entry version 132.
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=sll0569;
OS   Synechocystis sp. (strain PCC 6803 / Kazusa).
OC   Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC   unclassified Synechocystis.
OX   NCBI_TaxID=1111708;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA   Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA   Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA   Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA   Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT   "Sequence analysis of the genome of the unicellular cyanobacterium
RT   Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT   genome and assignment of potential protein-coding regions.";
RL   DNA Res. 3:109-136(1996).
RN   [2]
RP   INDUCTION.
RC   STRAIN=PCC 6803 / Kazusa;
RX   PubMed=15225304; DOI=10.1111/j.1365-2958.2004.04100.x;
RA   Domain F., Houot L., Chauvat F., Cassier-Chauvat C.;
RT   "Function and regulation of the cyanobacterial genes lexA, recA and ruvB:
RT   LexA is critical to the survival of cells facing inorganic carbon
RT   starvation.";
RL   Mol. Microbiol. 53:65-80(2004).
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: Expressed in light grown cells, strongly repressed post-
CC       transcriptionally by UV-C light, repressed by H(2)O(2) and SeO(4) but
CC       not by SeO(3) (PubMed:15225304). {ECO:0000269|PubMed:15225304}.
CC   -!- MISCELLANEOUS: This bacterium is considerably more resistant to UV and
CC       gamma irradiation than E.coli; the E.coli-like SOS regulon model is not
CC       an appropriate model for DNA repair in this cyanobacterium.
CC       {ECO:0000305|PubMed:15225304}.
CC   -!- SIMILARITY: Belongs to the RecA family. {ECO:0000255|HAMAP-
CC       Rule:MF_00268}.
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; BA000022; BAA18857.1; -; Genomic_DNA.
DR   PIR; S76945; S76945.
DR   AlphaFoldDB; P74737; -.
DR   SMR; P74737; -.
DR   IntAct; P74737; 1.
DR   STRING; 1148.1653947; -.
DR   PaxDb; P74737; -.
DR   EnsemblBacteria; BAA18857; BAA18857; BAA18857.
DR   KEGG; syn:sll0569; -.
DR   eggNOG; COG0468; Bacteria.
DR   InParanoid; P74737; -.
DR   OMA; DYGEQAL; -.
DR   PhylomeDB; P74737; -.
DR   Proteomes; UP000001425; 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   2: Evidence at transcript level;
KW   ATP-binding; Cytoplasm; DNA recombination; DNA-binding; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..354
FT                   /note="Protein RecA"
FT                   /id="PRO_0000122877"
FT   BINDING         68..75
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ   SEQUENCE   354 AA;  37805 MW;  67BD15C5162722CD CRC64;
     MASTNISDRE KALNAALAQI ERSFGKGAIM RLGDATQMRV ETISTGALTL DLALGGGLPK
     GRIVEIYGPE SSGKTTLALH AVAATQQAGG VAAFVDAEHA LDPVYSKALG VDIDNLLVAQ
     PDNGESALEI VDQLVRSTAV DIIVVDSVAA LVPRAEIEGE MGDTSVGSQA RLMSKAMRKI
     AGNIGRSGCL VIFLNQLRQK IGVTYGSPEV TTGGNALKFY ASVRLDIRRI QTLKKGTEGE
     YGIRAKVKVA KNKVAPPFRI AEFDIIFGQG ISRMGCTIDL AEKCEVITRK GAWYSYNGEN
     IAQGRDNAMK YLEENPEIAA TIDQQVREKL SLVNAVFPVE TEDGAEEQGE DGDF