ID   RECA_MYCFA              Reviewed;         422 AA.
AC   Q9F416;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 105.
DE   RecName: Full=Protein RecA;
DE   AltName: Full=Recombinase A;
DE   Contains:
DE     RecName: Full=Mfa RecA intein;
DE   Flags: Fragment;
GN   Name=recA;
OS   Mycolicibacterium fallax (Mycobacterium fallax).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1793;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 35219 / DSM 44179 / JCM 6405 / KCTC 9508 / CIP 81.39;
RX   PubMed=11034333; DOI=10.1016/s0014-5793(00)01944-x;
RA   Saves I., Laneelle M.-A., Daffe M., Masson J.-M.;
RT   "Inteins invading mycobacterial RecA proteins.";
RL   FEBS Lett. 480:221-225(2000).
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   -!- PTM: This protein undergoes a protein self splicing that involves a
CC       post-translational excision of the intervening region (intein) followed
CC       by peptide ligation. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RecA family. {ECO:0000305}.
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DR   EMBL; AJ251337; CAC09589.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9F416; -.
DR   SMR; Q9F416; -.
DR   STRING; 1793.AWC04_06595; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008094; F:ATP-dependent activity, acting on DNA; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease 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:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.28.10; -; 2.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR013765; DNA_recomb/repair_RecA.
DR   InterPro; IPR020584; DNA_recomb/repair_RecA_CS.
DR   InterPro; IPR003586; Hint_dom_C.
DR   InterPro; IPR003587; Hint_dom_N.
DR   InterPro; IPR036844; Hint_dom_sf.
DR   InterPro; IPR027434; Homing_endonucl.
DR   InterPro; IPR030934; Intein_C.
DR   InterPro; IPR006141; Intein_N.
DR   InterPro; IPR004860; LAGLIDADG_2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR020587; RecA_monomer-monomer_interface.
DR   PANTHER; PTHR45900; PTHR45900; 1.
DR   Pfam; PF03161; LAGLIDADG_2; 1.
DR   Pfam; PF00154; RecA; 1.
DR   PRINTS; PR00142; RECA.
DR   SMART; SM00305; HintC; 1.
DR   SMART; SM00306; HintN; 1.
DR   SUPFAM; SSF51294; SSF51294; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF55608; SSF55608; 1.
DR   TIGRFAMs; TIGR01443; intein_Cterm; 1.
DR   TIGRFAMs; TIGR01445; intein_Nterm; 1.
DR   PROSITE; PS50818; INTEIN_C_TER; 1.
DR   PROSITE; PS50817; INTEIN_N_TER; 1.
DR   PROSITE; PS00321; RECA_1; 1.
DR   PROSITE; PS50163; RECA_3; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Autocatalytic cleavage; Cytoplasm; DNA damage;
KW   DNA recombination; DNA repair; DNA-binding; Nucleotide-binding;
KW   Protein splicing; SOS response.
FT   CHAIN           <1..9
FT                   /note="Protein RecA, 1st part"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000030251"
FT   CHAIN           10..372
FT                   /note="Mfa RecA intein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000030252"
FT   CHAIN           373..>422
FT                   /note="Protein RecA, 2nd part"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000030253"
FT   NON_TER         1
FT   NON_TER         422
SQ   SEQUENCE   422 AA;  46919 MW;  90169C968BAAD209 CRC64;
     REKIGVMFGC FSYGTRVQLA DGSTEKIGKI VNQKMDVEVM SYDPVTDQIV PRKVVNWFNN
     GPAEQFLQFT VEKSGGNGRS QFAATPNHLI RTPAGWTEAG DLIAGDRVLA AERHLLSDQQ
     FQVILGSLMG GGNLSPNLHD RNGVRFRMGH GARQADYLEW KTALLGNIGH SVRENDQGAR
     FVDFTPLPEL GELRRAVYLG DGKKFLSEDY LKALTPLALA VWYMDDGSFT VRSKGVQQRT
     QGGSGRIEIC VEAMAEGTRE RLRDYLRDTH GLDVRLRSAG SGKSMLTFST EATAKFQELV
     APHMAPSMEH KLLPRFRGLG TVEPRFVEPA QRLVPARVLD VQVKPRTRSM NRFDIEVEGN
     HNYFVDGVMV HNSPETTTGG KALKFYASVR MDVRRIETLK DGSDAVGNRT RVKVVKNKVS
     PP