ID   RECA_MYCLE              Reviewed;         711 AA.
AC   P35901;
DT   01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-1994, sequence version 1.
DT   27-MAR-2024, entry version 160.
DE   RecName: Full=Protein RecA;
DE   AltName: Full=Recombinase A;
DE   Contains:
DE     RecName: Full=Mle RecA intein;
GN   Name=recA; OrderedLocusNames=ML0987;
OS   Mycobacterium leprae (strain TN).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium.
OX   NCBI_TaxID=272631;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7508863; DOI=10.1002/j.1460-2075.1994.tb06309.x;
RA   Davis E.O., Thangaraj H.S., Brooks P.C., Colston M.J.;
RT   "Evidence of selection for protein introns in the recAs of pathogenic
RT   mycobacteria.";
RL   EMBO J. 13:699-703(1994).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA   Smith D.R., Robison K.;
RL   Submitted (MAR-1994) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TN;
RX   PubMed=11234002; DOI=10.1038/35059006;
RA   Cole S.T., Eiglmeier K., Parkhill J., James K.D., Thomson N.R.,
RA   Wheeler P.R., Honore N., Garnier T., Churcher C.M., Harris D.E.,
RA   Mungall K.L., Basham D., Brown D., Chillingworth T., Connor R.,
RA   Davies R.M., Devlin K., Duthoy S., Feltwell T., Fraser A., Hamlin N.,
RA   Holroyd S., Hornsby T., Jagels K., Lacroix C., Maclean J., Moule S.,
RA   Murphy L.D., Oliver K., Quail M.A., Rajandream M.A., Rutherford K.M.,
RA   Rutter S., Seeger K., Simon S., Simmonds M., Skelton J., Squares R.,
RA   Squares S., Stevens K., Taylor K., Whitehead S., Woodward J.R.,
RA   Barrell B.G.;
RT   "Massive gene decay in the leprosy bacillus.";
RL   Nature 409:1007-1011(2001).
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.
CC   -!- SIMILARITY: Belongs to the RecA family. {ECO:0000305}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; X73822; CAA52040.1; -; Genomic_DNA.
DR   EMBL; U00019; AAA17277.1; -; Genomic_DNA.
DR   EMBL; AL583920; CAC31368.1; -; Genomic_DNA.
DR   PIR; S37025; S37025.
DR   RefSeq; NP_301732.1; NC_002677.1.
DR   RefSeq; WP_010908056.1; NC_002677.1.
DR   AlphaFoldDB; P35901; -.
DR   SMR; P35901; -.
DR   STRING; 272631.gene:17574813; -.
DR   MEROPS; N10.009; -.
DR   KEGG; mle:ML0987; -.
DR   PATRIC; fig|272631.5.peg.1789; -.
DR   Leproma; ML0987; -.
DR   eggNOG; COG0468; Bacteria.
DR   eggNOG; COG1372; Bacteria.
DR   HOGENOM; CLU_019600_1_0_11; -.
DR   OrthoDB; 9776733at2; -.
DR   Proteomes; UP000000806; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
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:0004519; F:endonuclease activity; IEA:InterPro.
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:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR   CDD; cd00081; Hint; 2.
DR   CDD; cd00983; RecA; 1.
DR   Gene3D; 3.10.28.10; Homing endonucleases; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2.
DR   Gene3D; 3.30.250.10; RecA protein, C-terminal domain; 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; 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; IPR004042; Intein_endonuc.
DR   InterPro; IPR006141; Intein_N.
DR   InterPro; IPR004860; LAGLIDADG_2.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR049261; RecA-like_C.
DR   InterPro; IPR049428; RecA-like_N.
DR   InterPro; IPR020588; RecA_ATP-bd.
DR   InterPro; IPR023400; RecA_C_sf.
DR   InterPro; IPR020587; RecA_monomer-monomer_interface.
DR   NCBIfam; TIGR01443; intein_Cterm; 1.
DR   NCBIfam; TIGR01445; intein_Nterm; 1.
DR   NCBIfam; TIGR02012; tigrfam_recA; 1.
DR   PANTHER; PTHR45900:SF1; MITOCHONDRIAL DNA REPAIR PROTEIN RECA HOMOLOG-RELATED; 1.
DR   PANTHER; PTHR45900; RECA; 1.
DR   Pfam; PF03161; LAGLIDADG_2; 1.
DR   Pfam; PF00154; RecA; 2.
DR   Pfam; PF21096; RecA_C; 1.
DR   PRINTS; PR00142; RECA.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00305; HintC; 1.
DR   SMART; SM00306; HintN; 1.
DR   SUPFAM; SSF51294; Hedgehog/intein (Hint) domain; 1.
DR   SUPFAM; SSF55608; Homing endonucleases; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR   SUPFAM; SSF54752; RecA protein, C-terminal domain; 1.
DR   PROSITE; PS50818; INTEIN_C_TER; 1.
DR   PROSITE; PS50819; INTEIN_ENDONUCLEASE; 1.
DR   PROSITE; PS50817; INTEIN_N_TER; 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; Autocatalytic cleavage; Cytoplasm; DNA damage;
KW   DNA recombination; DNA repair; DNA-binding; Nucleotide-binding;
KW   Protein splicing; Reference proteome; SOS response.
FT   CHAIN           1..205
FT                   /note="Protein RecA, 1st part"
FT                   /id="PRO_0000030260"
FT   CHAIN           206..570
FT                   /note="Mle RecA intein"
FT                   /id="PRO_0000030261"
FT   CHAIN           571..711
FT                   /note="Protein RecA, 2nd part"
FT                   /id="PRO_0000030262"
FT   DOMAIN          320..420
FT                   /note="DOD-type homing endonuclease"
FT   BINDING         67..74
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   711 AA;  77638 MW;  4D6A5B8B2A115C0E CRC64;
     MAQVPDREKA LELAMAQIEK NYGKGSVMRL GDEMCQPISV IPTGSIALDV ALGIGGLPRG
     RIVEIYGPES SGKTTVALHA VANAQAVGGV AAFIDAEHAL EPEYAKKLGV DTDSLLVSQP
     DTGEQALEIA DMLIRSGALD IVVIDSVAAL VPRAELEGEM GDSYVGLQAR LMSQALRKMT
     GALSNSGTTA IFINQLREKI GVMFGCMNYS TRVTLADGST EKIGKIVNNK MDVRVLSYDP
     VTDRIVPRKV VNWFNNGPAE QFLQFTVEKS GSNGKSQFAA TPNHLIRTPG GWTEAGNLIA
     GDRVLAVEPH MLSDQQFQVV LGSLMGDGNL SPNLCDRNGV RFRLLGYGCK QVEYLQWKKA
     LMGNIRHTVR ENSMGASFID FTPLPELVEL QRAVYLGDGK KFLSEEYLKA LTPLVLAIWY
     MDDGSFTVGS KRVQERTAGG SGRIEICVDA MTEGTRVRLR DYLCDTHGLD VRLREVGSAG
     KAVLVFSTAA TAKFQSLIAP YVAPSMEYKL LPQFRGRGSV TPQFVEPTQQ LVPARVLDVH
     VKLSTRSMNR FDIEVEGNHN YFVDGVMVHN SPETTTGGKA LKFYASVRMD VRRIETLKDG
     VDAVGNRTRV KIVKNKVSPP FKQAEFDILY GKGISREGSL IDMGVEQGFV RKSGSWFTYE
     GEQLGQGKEN ARNFLLENAD VANEIEKKIK EKLGIGAVVT DDDILPTPVD F
//