ID   RECA_LEPME              Reviewed;         387 AA.
AC   P0C7T0; P48290; Q93CF0;
DT   01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT   01-JUL-2008, sequence version 1.
DT   03-AUG-2022, entry version 50.
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   Leptospira meyeri.
OC   Bacteria; Spirochaetes; Leptospirales; Leptospiraceae; Leptospira.
OX   NCBI_TaxID=29508;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=8566806; DOI=10.1016/0378-1119(95)00665-6;
RA   Stamm L.V., Frye J.G., Hardham J.M.;
RT   "Sequence of the Leptospira biflexa serovar patoc recA gene.";
RL   Gene 167:339-340(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. {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}.
CC   -!- CAUTION: Was originally thought to originate from Leptospira biflexa;
CC       taxonomy has been changed based on information in PubMed:11751822.
CC       {ECO:0000305|PubMed:8566806}.
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DR   EMBL; U32625; AAC43586.1; -; Genomic_DNA.
DR   PIR; JC4578; JC4578.
DR   RefSeq; WP_004784349.1; NZ_SORO01000003.1.
DR   AlphaFoldDB; P0C7T0; -.
DR   SMR; P0C7T0; -.
DR   STRING; 1193051.LEP1GSC017_0685; -.
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..387
FT                   /note="Protein RecA"
FT                   /id="PRO_0000122742"
FT   REGION          350..387
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        351..369
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         78..85
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00268"
SQ   SEQUENCE   387 AA;  42349 MW;  D5B08474C4CC9B44 CRC64;
     MKKEKADKAQ EKETDQRKQA IDAALGQIEK QFGKGSIMRL GADTRMAEMN VVSTGSLDLD
     IALGIGGFPS GRIVEIYGPE SSGKTTLTLS AIAETQKKGG IAAFIDAEHA LDPSYAKKLG
     VNVDDLLVAQ PDNGEEALEI CESLVRSNAI DLIVIDSVAA LVPKAEIEGD MGDSHMGLQA
     RLMSQALRKL TGTISKSNTT VIFINQIRMK IGVMFGSPET TTGGNALKFY ASIRLDIRRI
     ETLKEKEEPV GNRVRVKVVK NKCAPPFRQA EFDIMYANGI NRESSLIDLA VRHDLVAKAG
     SWYSYGGEKI GQGKEQVKNF FLENPDIAFK IENQVRDLNS LPLMDQSKIQ TREVKSIERD
     PKETKETKSK QPVSFSTEAE VDIAVGE