ID   RECA_MYCBO              Reviewed;         790 AA.
AC   P0A5U5; O34519; P26345; X2BLS4;
DT   15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT   15-MAR-2005, sequence version 1.
DT   27-MAY-2015, entry version 80.
DE   RecName: Full=Protein RecA;
DE   AltName: Full=Recombinase A;
DE   Contains:
DE     RecName: Full=Endonuclease PI-MboI;
DE              EC=3.1.-.-;
DE     AltName: Full=Mbo RecA intein;
GN   Name=recA; OrderedLocusNames=Mb2756c;
OS   Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC   Bacteria; Actinobacteria; Actinobacteridae; Actinomycetales;
OC   Corynebacterineae; Mycobacteriaceae; Mycobacterium;
OC   Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=233413;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-935 / AF2122/97;
RX   PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA   Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H.,
RA   Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S.,
RA   Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R.,
RA   Parkhill J., Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT   "The complete genome sequence of Mycobacterium bovis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
CC   -!- FUNCTION: Can catalyze the hydrolysis of ATP in the presence of
CC       single-stranded DNA, the ATP-dependent uptake of single-stranded
CC       DNA by duplex DNA, and the ATP-dependent hybridization of
CC       homologous single-stranded DNAs. It interacts with LexA causing
CC       its activation and leading to its autocatalytic cleavage (By
CC       similarity). {ECO:0000250}.
CC   -!- FUNCTION: PI-MboI is an endonuclease. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- PTM: This protein undergoes a protein self splicing that involves
CC       a post-translational excision of the intervening region (intein)
CC       followed by peptide ligation. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the RecA family. {ECO:0000305}.
CC   -!- SIMILARITY: Contains 1 DOD-type homing endonuclease domain.
CC       {ECO:0000305}.
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DR   EMBL; BX248333; CDO44020.1; -; Genomic_DNA.
DR   RefSeq; NP_856402.1; NC_002945.3.
DR   RefSeq; WP_003414006.1; NC_002945.3.
DR   ProteinModelPortal; P0A5U5; -.
DR   SMR; P0A5U5; 1-345, 589-769.
DR   STRING; 233413.Mb2756c; -.
DR   BindingDB; P0A5U5; -.
DR   MEROPS; N10.009; -.
DR   PRIDE; P0A5U5; -.
DR   EnsemblBacteria; CDO44020; CDO44020; Mb2756c.
DR   GeneID; 1091758; -.
DR   KEGG; mbo:Mb2756c; -.
DR   PATRIC; 18007773; VBIMycBov88188_3019.
DR   eggNOG; COG1372; -.
DR   KO; K03553; -.
DR   OMA; DQGTQDV; -.
DR   OrthoDB; EOG6ZKXNZ; -.
DR   Proteomes; UP000001419; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0008094; F:DNA-dependent ATPase activity; IEA:InterPro.
DR   GO; GO:0004519; F:endonuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0003697; F:single-stranded DNA binding; IEA:InterPro.
DR   GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR   GO; GO:0016539; P:intein-mediated protein splicing; IEA:InterPro.
DR   GO; GO:0006314; P:intron homing; IEA:UniProtKB-KW.
DR   GO; GO:0009432; P:SOS response; IEA:UniProtKB-KW.
DR   Gene3D; 2.170.16.10; -; 2.
DR   Gene3D; 3.10.28.10; -; 1.
DR   Gene3D; 3.30.250.10; -; 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; IPR028992; Hedgehog/Intein_dom.
DR   InterPro; IPR003586; Hint_dom_C.
DR   InterPro; IPR003587; Hint_dom_N.
DR   InterPro; IPR027434; Homing_endonucl.
DR   InterPro; IPR006142; INTEIN.
DR   InterPro; IPR030934; Intein_C.
DR   InterPro; IPR004042; Intein_endonuc.
DR   InterPro; IPR006141; Intein_N.
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; PTHR22942:SF1; PTHR22942:SF1; 1.
DR   Pfam; PF14528; LAGLIDADG_3; 1.
DR   Pfam; PF00154; RecA; 2.
DR   PRINTS; PR00379; INTEIN.
DR   PRINTS; PR00142; RECA.
DR   SMART; SM00382; AAA; 1.
DR   SMART; SM00305; HintC; 1.
DR   SMART; SM00306; HintN; 1.
DR   SUPFAM; SSF51294; SSF51294; 2.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   SUPFAM; SSF54752; SSF54752; 1.
DR   SUPFAM; SSF55608; SSF55608; 1.
DR   TIGRFAMs; TIGR01443; intein_Cterm; 1.
DR   TIGRFAMs; TIGR01445; intein_Nterm; 1.
DR   TIGRFAMs; TIGR02012; tigrfam_recA; 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; 2.
PE   3: Inferred from homology;
KW   ATP-binding; Autocatalytic cleavage; Complete proteome; Cytoplasm;
KW   DNA damage; DNA recombination; DNA repair; DNA-binding; Endonuclease;
KW   Hydrolase; Intron homing; Nuclease; Nucleotide-binding;
KW   Protein splicing; SOS response.
FT   CHAIN         1    251       Protein RecA, 1st part.
FT                                /FTId=PRO_0000030272.
FT   CHAIN       252    691       Endonuclease PI-MboI.
FT                                /FTId=PRO_0000030273.
FT   CHAIN       692    790       Protein RecA, 2nd part.
FT                                /FTId=PRO_0000030274.
FT   DOMAIN      366    508       DOD-type homing endonuclease.
FT   NP_BIND      67     74       ATP. {ECO:0000250}.
SQ   SEQUENCE   790 AA;  85389 MW;  AD16340D2ED5E572 CRC64;
     MTQTPDREKA LELAVAQIEK SYGKGSVMRL GDEARQPISV IPTGSIALDV ALGIGGLPRG
     RVIEIYGPES SGKTTVALHA VANAQAAGGV AAFIDAEHAL DPDYAKKLGV DTDSLLVSQP
     DTGEQALEIA DMLIRSGALD IVVIDSVAAL VPRAELEGEM GDSHVGLQAR LMSQALRKMT
     GALNNSGTTA IFINQLRDKI GVMFGSPETT TGGKALKFYA SVRMDVRRVE TLKDGTNAVG
     NRTRVKVVKN KCLAEGTRIF DPVTGTTHRI EDVVDGRKPI HVVAAAKDGT LHARPVVSWF
     DQGTRDVIGL RIAGGAIVWA TPDHKVLTEY GWRAAGELRK GDRVAQPRRF DGFGDSAPIP
     ADHARLLGYL IGDGRDGWVG GKTPINFINV QRALIDDVTR IAATLGCAAH PQGRISLAIA
     HRPGERNGVA DLCQQAGIYG KLAWEKTIPN WFFEPDIAAD IVGNLLFGLF ESDGWVSREQ
     TGALRVGYTT TSEQLAHQIH WLLLRFGVGS TVRDYDPTQK RPSIVNGRRI QSKRQVFEVR
     ISGMDNVTAF AESVPMWGPR GAALIQAIPE ATQGRRRGSQ ATYLAAEMTD AVLNYLDERG
     VTAQEAAAMI GVASGDPRGG MKQVLGASRL RRDRVQALAD ALDDKFLHDM LAEELRYSVI
     REVLPTRRAR TFDLEVEELH TLVAEGVVVH NCSPPFKQAE FDILYGKGIS REGSLIDMGV
     DQGLIRKSGA WFTYEGEQLG QGKENARNFL VENADVADEI EKKIKEKLGI GAVVTDDPSN
     DGVLPAPVDF
//