ID   RECA_MYCSH              Reviewed;         423 AA.
AC   Q9F410;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 103.
DE   RecName: Full=Protein RecA;
DE   AltName: Full=Recombinase A;
DE   Contains:
DE     RecName: Full=Msh RecA intein;
DE   Flags: Fragment;
GN   Name=recA;
OS   Mycobacterium shimoidei.
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=29313;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 27962 / DSM 44152 / JCM 12376;
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; AJ251338; CAC09592.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9F410; -.
DR   SMR; Q9F410; -.
DR   STRING; 29313.BHQ16_21240; -.
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; IPR006142; INTEIN.
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; PR00379; INTEIN.
DR   PRINTS; PR00142; RECA.
DR   SMART; SM00305; HintC; 1.
DR   SMART; SM00306; HintN; 1.
DR   SUPFAM; SSF51294; SSF51294; 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_0000030263"
FT   CHAIN           10..373
FT                   /note="Msh RecA intein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000030264"
FT   CHAIN           374..>423
FT                   /note="Protein RecA, 2nd part"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000030265"
FT   NON_TER         1
FT   NON_TER         423
SQ   SEQUENCE   423 AA;  47084 MW;  D36A8C64C39F2AEA CRC64;
     REKIGVMFGC MNYSTRVTLA DGSTEKIGKI VNNKMDVKVL SYDPDSDRIV PRKIVNWFNN
     GPAEQFLQFT VEKSGGNGKS QFAATPNHLI RTPAGWTEAG DLNTGDRVLA AEPHLLSDQQ
     FQVVLGSLMG DGNLSPNRRD RNGVRFRLGH GAKQAEYLQW KTALMGNIGH TVRENAKGAS
     FVDFTPLPEL AELQRAVYMG DGKKFFSEEY LKALTPLALA IWYMDDGSFT LRSRGLQERT
     AGGSGRIAIC VEAMTEGTRV RLRDYLRDTH GLDVRLRSAG SAGKTVLVFS MAATAKFQEL
     VAPYMAPSME YKLLPRFRGR STVRPQFVEP TQRLVPARIL DVHVKPHTRS MNRFDIEVEG
     NHNYFVDGVM VHNSPETTTG GKALKFYASV RMDVRRIETL KDGTDAVGNR TRVKVVKNKV
     SPP