(data stored in ACNUC7421 zone)

SWISSPROT: NUCA_BACSU

ID   NUCA_BACSU              Reviewed;         147 AA.
AC   P12667; P12668;
DT   01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 2.
DT   11-DEC-2019, entry version 113.
DE   RecName: Full=DNA-entry nuclease;
DE            EC=3.-.-.-;
DE   AltName: Full=Competence-specific nuclease;
GN   Name=nucA; Synonyms=comI; OrderedLocusNames=BSU03430;
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=7704255; DOI=10.1099/13500872-141-2-277;
RA   Fujishima Y., Yamane K.;
RT   "A 10 kb nucleotide sequence at the 5' flanking region (32 degrees) of
RT   srfAA of the Bacillus subtilis chromosome.";
RL   Microbiology 141:277-279(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=7746143; DOI=10.1111/j.1365-2958.1995.tb02236.x;
RA   van Sinderen D., Kiewiet R., Venema G.;
RT   "Differential expression of two closely related deoxyribonuclease genes,
RT   nucA and nucB, in Bacillus subtilis.";
RL   Mol. Microbiol. 15:213-223(1995).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA   Yamane K., Kumano M., Kurita K.;
RT   "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT   determination of the sequence of a 146 kb segment and identification of 113
RT   genes.";
RL   Microbiology 142:3047-3056(1996).
RN   [4]
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   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 18-147.
RX   PubMed=2841296; DOI=10.1128/jb.170.8.3703-3710.1988;
RA   Vosman B., Kuiken G., Kooistra J., Venema G.;
RT   "Transformation in Bacillus subtilis: involvement of the 17-kilodalton DNA-
RT   entry nuclease and the competence-specific 18-kilodalton protein.";
RL   J. Bacteriol. 170:3703-3710(1988).
CC   -!- FUNCTION: By degrading DNA that enters the cell, plays a role in the
CC       competence of cells to be transformed. Degrades both double-stranded,
CC       linear and covalently closed circular DNA.
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC       Note=Mn(2+) ion stimulates activity.;
CC   -!- ACTIVITY REGULATION: The activity can be inhibited by the 18 kDa
CC       competence-specific protein nin.
CC   -!- SUBUNIT: This protein is a subunit of a 75 kDa protein complex, which
CC       governs binding and entry of donor DNA. The complex is a tetramer of
CC       two subunits of the DNA-entry nuclease and two subunits of a
CC       competence-specific protein. Only the complex is able to bind ds- and
CC       ss-DNA.
CC   -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass membrane protein.
CC   -!- SIMILARITY: To B.subtilis NucB. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=BAA06431.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC       Sequence=BAA08977.1; Type=Erroneous initiation; Evidence={ECO:0000305};
DR   EMBL; M21672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; D30762; BAA06431.1; ALT_INIT; Genomic_DNA.
DR   EMBL; AL009126; CAB12137.2; -; Genomic_DNA.
DR   EMBL; D50453; BAA08977.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_388225.2; NC_000964.3.
DR   RefSeq; WP_010886401.1; NZ_JNCM01000030.1.
DR   SMR; P12667; -.
DR   STRING; 224308.BSU03430; -.
DR   PaxDb; P12667; -.
DR   PRIDE; P12667; -.
DR   EnsemblBacteria; CAB12137; CAB12137; BSU03430.
DR   GeneID; 938309; -.
DR   KEGG; bsu:BSU03430; -.
DR   PATRIC; fig|224308.43.peg.353; -.
DR   HOGENOM; HOG000096181; -.
DR   OMA; MCKEGGE; -.
DR   BioCyc; BSUB:BSU03430-MONOMER; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004518; F:nuclease activity; IEA:UniProtKB-KW.
DR   GO; GO:0030420; P:establishment of competence for transformation; IEA:UniProtKB-KW.
DR   InterPro; IPR029476; DNase_NucA_NucB.
DR   Pfam; PF14040; DNase_NucA_NucB; 1.
PE   4: Predicted;
DR   PRODOM; P12667.
DR   SWISS-2DPAGE; P12667.
KW   Cell membrane; Competence; Hydrolase; Manganese; Membrane; Nuclease;
KW   Reference proteome; Transmembrane; Transmembrane helix.
FT   CHAIN           1..147
FT                   /note="DNA-entry nuclease"
FT                   /id="PRO_0000057977"
FT   TRANSMEM        8..24
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        120..147
FT                   /note="ADNRGAGSWVGHRLTDYPDGTKVLFTIQ -> LTTAEQALGSGIGLPITQTA
FT                   QRFYSQFSKQYIEEEQHIDQIMEAARTFDFISSIYCISKGFYTSCNGLD (in Ref.
FT                   5)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   147 AA;  16259 MW;  83FECB62220D9240 CRC64;
     MTTDIIKTIL LVIVIIAAAA VGLIKGDFFS ADQKTSQTKE YDETMAFPSD RYPETAKHIK
     DAINEGHSEV CTIDRDGAEE RREQSLKDVP SKKGYDRDEW PMAMCKEGGE GASVEYISPA
     DNRGAGSWVG HRLTDYPDGT KVLFTIQ
//

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