ID   RECA_RHOCA              Reviewed;         355 AA.
AC   P42447;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
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};
GN   Name=recA {ECO:0000255|HAMAP-Rule:MF_00268};
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=J50;
RX   PubMed=7607398; DOI=10.1111/j.1574-6968.1995.tb07576.x;
RA   Fernandez de Henestrosa A.R., Rivera E., Barbe J.;
RT   "Non-reciprocal regulation of Rhodobacter capsulatus and Rhodobacter
RT   sphaeroides recA genes expression.";
RL   FEMS Microbiol. Lett. 129:175-181(1995).
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; X82183; CAA57673.1; -; Genomic_DNA.
DR   PIR; S49464; S49464.
DR   AlphaFoldDB; P42447; -.
DR   SMR; P42447; -.
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; SOS response.
FT   CHAIN           1..355
FT                   /note="Protein RecA"
FT                   /id="PRO_0000122817"
FT   BINDING         78..85
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ   SEQUENCE   355 AA;  38027 MW;  64E408A33A2DE77E CRC64;
     MATTGLFEMN DKGKADKQKA LECALAQIER QFGKGSIMKL GGDTPPPEIE ATSTGSLGLD
     IALGIGGLPK GRIVEIYGPE SSGKTTLTLH CIAEEQKKGG VCAFVDAEHA LDPYYAKKLG
     VSLEDLLISQ PDTGEQALEI VDTLVRSGAV SLVVVDSVAA LTPKAEIEGD MGDATVGAQA
     RLMSQAMRKL TASIGRSNCM VIFINQIRMK IGVMFGSPET TSGGNALKFY ASVRLDIRRT
     GAIKDRDEVI GNQTRVKVVK NKVAPPFREV EFDILYGEGI SKVGELVDLG VKAGVVAKSG
     AWYSYGDERI GQGRENAKQF LRDNPDIAYE IEDKIRASHG LEFGVDPTAE DLTEE