ID   RECA_MYCCI              Reviewed;         423 AA.
AC   Q9F417;
DT   26-SEP-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 106.
DE   RecName: Full=Protein RecA;
DE   AltName: Full=Recombinase A;
DE   Contains:
DE     RecName: Full=Mch RecA intein;
DE   Flags: Fragment;
GN   Name=recA;
OS   Mycolicibacterium chitae (Mycobacterium chitae).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=1792;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=IP14116003;
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; AJ251336; CAC09588.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9F417; -.
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; 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_0000030248"
FT   CHAIN           10..373
FT                   /note="Mch RecA intein"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000030249"
FT   CHAIN           374..>423
FT                   /note="Protein RecA, 2nd part"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000030250"
FT   NON_TER         1
FT   NON_TER         423
SQ   SEQUENCE   423 AA;  46960 MW;  DDFFD79A38527A08 CRC64;
     REKIGVMFGC FNYSTRVQLA DGTTEKIGKI VNNKMDVEVL SYDPVADQVV PRKVVNWFNN
     GPAEQFLQFT VEKSGGNGRS QFAATPNHLI RTPAGWSEAG DLIAGDRVMA SEPHRLSDQQ
     FQVVLGSLMG DGNLSPNRRD RNGVRFRMGH GAKQGDYLQW KTDLLANIAH SAHENAKGAR
     FVDFTPLPEL AELQRAVYLG DGKKFLSEEY LKALTPLALA IWYMDDGGFT VRSKGLQQRT
     EGGSGRIEIC VEAMSVGSRD RLRDYLRDTH GLDVRLRHAG AAGKAMLVFT TAASAKFQEI
     VAPYMAPSME YKLLPRFRGQ GTVAPQFVEP TERLVPARIL DIHVKPHTRS MNRFDIEVEG
     NHNYFVDGVM VHNSPETTTG GKALKFYASV RIDVRRIETL KDGTDAVGNR TRAKIVKNKV
     SPP