RECA_MYCBO
ID RECA_MYCBO Reviewed; 790 AA.
AC P0A5U5; A0A1R3Y236; O34519; P26345; X2BLS4;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=BQ2027_MB2756C;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; 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., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA 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).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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 -!- 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 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; LT708304; SIU01374.1; -; Genomic_DNA.
DR RefSeq; NP_856402.1; NC_002945.3.
DR RefSeq; WP_003414006.1; NC_002945.4.
DR AlphaFoldDB; P0A5U5; -.
DR SMR; P0A5U5; -.
DR MEROPS; N10.009; -.
DR PRIDE; P0A5U5; -.
DR EnsemblBacteria; SIU01374; SIU01374; BQ2027_MB2756C.
DR PATRIC; fig|233413.5.peg.3019; -.
DR OMA; MAPSMEY; -.
DR Proteomes; UP000001419; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
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:UniProtKB-KW.
DR GO; GO:0003697; F:single-stranded DNA binding; 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:0006314; P:intron homing; IEA:UniProtKB-KW.
DR GO; GO:0009432; P:SOS response; IEA:UniProtKB-UniRule.
DR CDD; cd00983; recA; 1.
DR Gene3D; 3.10.28.10; -; 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; 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; IPR004042; Intein_endonuc.
DR InterPro; IPR006141; Intein_N.
DR InterPro; IPR004860; LAGLIDADG_2.
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; PTHR45900; PTHR45900; 1.
DR Pfam; PF14528; LAGLIDADG_3; 1.
DR Pfam; PF00154; RecA; 1.
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; 1.
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; Cytoplasm; DNA damage;
KW DNA recombination; DNA repair; DNA-binding; Endonuclease; Hydrolase;
KW Intron homing; Nuclease; Nucleotide-binding; Protein splicing;
KW SOS response.
FT CHAIN 1..251
FT /note="Protein RecA, 1st part"
FT /id="PRO_0000030272"
FT CHAIN 252..691
FT /note="Endonuclease PI-MboI"
FT /id="PRO_0000030273"
FT CHAIN 692..790
FT /note="Protein RecA, 2nd part"
FT /id="PRO_0000030274"
FT DOMAIN 366..508
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 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
