EXOA_BACSU
ID EXOA_BACSU Reviewed; 252 AA.
AC P37454;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 147.
DE RecName: Full=Exodeoxyribonuclease;
DE EC=3.1.11.2;
GN Name=exoA; OrderedLocusNames=BSU40880;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=7584024; DOI=10.1093/dnares/1.1.1;
RA Ogasawara N., Nakai S., Yoshikawa H.;
RT "Systematic sequencing of the 180 kilobase region of the Bacillus subtilis
RT chromosome containing the replication origin.";
RL DNA Res. 1:1-14(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP CHARACTERIZATION.
RX PubMed=10540738; DOI=10.1271/bbb.63.1528;
RA Shida T., Ogawa T., Ogasawara N., Sekiguchi J.;
RT "Characterization of Bacillus subtilis ExoA protein: a multifunctional DNA-
RT repair enzyme similar to the Escherichia coli exonuclease III.";
RL Biosci. Biotechnol. Biochem. 63:1528-1534(1999).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Exonucleolytic cleavage in the 3'- to 5'-direction to yield
CC nucleoside 5'-phosphates.; EC=3.1.11.2;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Probably binds two magnesium or manganese ions per subunit.
CC {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the DNA repair enzymes AP/ExoA family.
CC {ECO:0000305}.
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DR EMBL; D26185; BAA05218.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB16125.1; -; Genomic_DNA.
DR PIR; S66012; S66012.
DR RefSeq; NP_391968.1; NC_000964.3.
DR RefSeq; WP_003243194.1; NZ_JNCM01000034.1.
DR PDB; 5CFE; X-ray; 1.84 A; A=1-252.
DR PDBsum; 5CFE; -.
DR AlphaFoldDB; P37454; -.
DR SMR; P37454; -.
DR STRING; 224308.BSU40880; -.
DR PaxDb; P37454; -.
DR PRIDE; P37454; -.
DR EnsemblBacteria; CAB16125; CAB16125; BSU_40880.
DR GeneID; 937918; -.
DR KEGG; bsu:BSU40880; -.
DR PATRIC; fig|224308.179.peg.4429; -.
DR eggNOG; COG0708; Bacteria.
DR InParanoid; P37454; -.
DR OMA; DCICVQE; -.
DR PhylomeDB; P37454; -.
DR BioCyc; BSUB:BSU40880-MON; -.
DR BRENDA; 3.1.11.1; 658.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0003906; F:DNA-(apurinic or apyrimidinic site) endonuclease activity; IBA:GO_Central.
DR GO; GO:0008311; F:double-stranded DNA 3'-5' exodeoxyribonuclease activity; IBA:GO_Central.
DR GO; GO:0004519; F:endonuclease activity; IEA:InterPro.
DR GO; GO:0008853; F:exodeoxyribonuclease III activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008081; F:phosphoric diester hydrolase activity; IBA:GO_Central.
DR GO; GO:0006284; P:base-excision repair; IBA:GO_Central.
DR Gene3D; 3.60.10.10; -; 1.
DR InterPro; IPR004808; AP_endonuc_1.
DR InterPro; IPR020847; AP_endonuclease_F1_BS.
DR InterPro; IPR020848; AP_endonuclease_F1_CS.
DR InterPro; IPR036691; Endo/exonu/phosph_ase_sf.
DR InterPro; IPR005135; Endo/exonuclease/phosphatase.
DR PANTHER; PTHR22748; PTHR22748; 1.
DR Pfam; PF03372; Exo_endo_phos; 1.
DR SUPFAM; SSF56219; SSF56219; 1.
DR TIGRFAMs; TIGR00633; xth; 1.
DR PROSITE; PS00726; AP_NUCLEASE_F1_1; 1.
DR PROSITE; PS00727; AP_NUCLEASE_F1_2; 1.
DR PROSITE; PS00728; AP_NUCLEASE_F1_3; 1.
DR PROSITE; PS51435; AP_NUCLEASE_F1_4; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Exonuclease; Hydrolase; Magnesium; Metal-binding;
KW Nuclease; Reference proteome.
FT CHAIN 1..252
FT /note="Exodeoxyribonuclease"
FT /id="PRO_0000200025"
FT ACT_SITE 106
FT /evidence="ECO:0000250"
FT ACT_SITE 145
FT /note="Proton donor/acceptor"
FT /evidence="ECO:0000250"
FT BINDING 36
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250"
FT BINDING 242
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250"
FT SITE 147
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT SITE 217
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000250"
FT SITE 243
FT /note="Interaction with DNA substrate"
FT /evidence="ECO:0000250"
FT STRAND 2..7
FT /evidence="ECO:0007829|PDB:5CFE"
FT HELIX 11..17
FT /evidence="ECO:0007829|PDB:5CFE"
FT HELIX 20..27
FT /evidence="ECO:0007829|PDB:5CFE"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:5CFE"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:5CFE"
FT STRAND 52..56
FT /evidence="ECO:0007829|PDB:5CFE"
FT STRAND 58..60
FT /evidence="ECO:0007829|PDB:5CFE"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:5CFE"
FT STRAND 75..80
FT /evidence="ECO:0007829|PDB:5CFE"
FT HELIX 84..86
FT /evidence="ECO:0007829|PDB:5CFE"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:5CFE"
FT STRAND 92..96
FT /evidence="ECO:0007829|PDB:5CFE"
FT STRAND 101..106
FT /evidence="ECO:0007829|PDB:5CFE"
FT HELIX 112..114
FT /evidence="ECO:0007829|PDB:5CFE"
FT HELIX 117..137
FT /evidence="ECO:0007829|PDB:5CFE"
FT STRAND 140..145
FT /evidence="ECO:0007829|PDB:5CFE"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:5CFE"
FT HELIX 158..160
FT /evidence="ECO:0007829|PDB:5CFE"
FT HELIX 169..180
FT /evidence="ECO:0007829|PDB:5CFE"
FT STRAND 183..185
FT /evidence="ECO:0007829|PDB:5CFE"
FT HELIX 186..190
FT /evidence="ECO:0007829|PDB:5CFE"
FT STRAND 199..201
FT /evidence="ECO:0007829|PDB:5CFE"
FT TURN 205..211
FT /evidence="ECO:0007829|PDB:5CFE"
FT STRAND 217..222
FT /evidence="ECO:0007829|PDB:5CFE"
FT HELIX 223..228
FT /evidence="ECO:0007829|PDB:5CFE"
FT STRAND 229..234
FT /evidence="ECO:0007829|PDB:5CFE"
FT STRAND 240..243
FT /evidence="ECO:0007829|PDB:5CFE"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:5CFE"
SQ SEQUENCE 252 AA; 29252 MW; 08F3636B70FE6625 CRC64;
MKLISWNVNG LRAVMRKMDF LSYLKEEDAD IICLQETKIQ DGQVDLQPED YHVYWNYAVK
KGYSGTAVFS KQEPLQVIYG IGVEEHDQEG RVITLEFENV FVMTVYTPNS RRGLERIDYR
MQWEEALLSY ILELDQKKPV ILCGDLNVAH QEIDLKNPKA NRNNAGFSDQ EREAFTRFLE
AGFVDSFRHV YPDLEGAYSW WSYRAGARDR NIGWRIDYFV VSESLKEQIE DASISADVMG
SDHCPVELII NI
