ID   ASPG2_BACSU             Reviewed;         375 AA.
AC   O34482;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=L-asparaginase 2;
DE            Short=L-ASNase 2;
DE            EC=3.5.1.1;
DE   AltName: Full=L-asparagine amidohydrolase 2;
DE   Flags: Precursor;
GN   Name=ansZ; Synonyms=yccC; OrderedLocusNames=BSU02690;
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=9274031; DOI=10.1099/00221287-143-8-2775;
RA   Kumano M., Tamakoshi A., Yamane K.;
RT   "A 32 kb nucleotide sequence from the region of the lincomycin-resistance
RT   gene (22 degrees-25 degrees) of the Bacillus subtilis chromosome and
RT   identification of the site of the lin-2 mutation.";
RL   Microbiology 143:2775-2782(1997).
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   FUNCTION, AND INDUCTION.
RX   PubMed=11914346; DOI=10.1128/jb.184.8.2148-2154.2002;
RA   Fisher S.H., Wray L.V. Jr.;
RT   "Bacillus subtilis 168 contains two differentially regulated genes encoding
RT   L-asparaginase.";
RL   J. Bacteriol. 184:2148-2154(2002).
CC   -!- FUNCTION: Catalyzes the conversion of L-asparagine to L-aspartate and
CC       ammonium. {ECO:0000269|PubMed:11914346}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + L-asparagine = L-aspartate + NH4(+);
CC         Xref=Rhea:RHEA:21016, ChEBI:CHEBI:15377, ChEBI:CHEBI:28938,
CC         ChEBI:CHEBI:29991, ChEBI:CHEBI:58048; EC=3.5.1.1;
CC   -!- SUBUNIT: Homotetramer. {ECO:0000250}.
CC   -!- INDUCTION: Expression is induced during limiting-nitrogen conditions by
CC       the nitrogen regulatory factor TnrA. {ECO:0000269|PubMed:11914346}.
CC   -!- MISCELLANEOUS: B.subtilis contains two L-asparaginase isoenzymes: L-
CC       asparaginase I, a low-affinity enzyme located in the cytoplasm, and L-
CC       asparaginase II, a high-affinity secreted enzyme.
CC   -!- SIMILARITY: Belongs to the asparaginase 1 family. {ECO:0000305}.
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DR   EMBL; AB000617; BAA22230.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB12063.1; -; Genomic_DNA.
DR   PIR; F69754; F69754.
DR   RefSeq; NP_388151.1; NC_000964.3.
DR   RefSeq; WP_003246337.1; NZ_JNCM01000030.1.
DR   AlphaFoldDB; O34482; -.
DR   SMR; O34482; -.
DR   STRING; 224308.BSU02690; -.
DR   PaxDb; O34482; -.
DR   EnsemblBacteria; CAB12063; CAB12063; BSU_02690.
DR   GeneID; 938392; -.
DR   KEGG; bsu:BSU02690; -.
DR   PATRIC; fig|224308.179.peg.279; -.
DR   eggNOG; COG0252; Bacteria.
DR   InParanoid; O34482; -.
DR   OMA; DESPYFL; -.
DR   PhylomeDB; O34482; -.
DR   BioCyc; BSUB:BSU02690-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0042597; C:periplasmic space; IBA:GO_Central.
DR   GO; GO:0004067; F:asparaginase activity; IBA:GO_Central.
DR   GO; GO:0006530; P:asparagine catabolic process; IBA:GO_Central.
DR   CDD; cd08964; L-asparaginase_II; 1.
DR   Gene3D; 3.40.50.1170; -; 1.
DR   Gene3D; 3.40.50.40; -; 1.
DR   InterPro; IPR004550; AsnASE_II.
DR   InterPro; IPR036152; Asp/glu_Ase-like_sf.
DR   InterPro; IPR006034; Asparaginase/glutaminase-like.
DR   InterPro; IPR020827; Asparaginase/glutaminase_AS1.
DR   InterPro; IPR027475; Asparaginase/glutaminase_AS2.
DR   InterPro; IPR040919; Asparaginase_C.
DR   InterPro; IPR027473; L-asparaginase_C.
DR   InterPro; IPR027474; L-asparaginase_N.
DR   InterPro; IPR037152; L-asparaginase_N_sf.
DR   Pfam; PF00710; Asparaginase; 1.
DR   Pfam; PF17763; Asparaginase_C; 1.
DR   PIRSF; PIRSF001220; L-ASNase_gatD; 1.
DR   PRINTS; PR00139; ASNGLNASE.
DR   SMART; SM00870; Asparaginase; 1.
DR   SUPFAM; SSF53774; SSF53774; 1.
DR   TIGRFAMs; TIGR00520; asnASE_II; 1.
DR   PROSITE; PS00144; ASN_GLN_ASE_1; 1.
DR   PROSITE; PS00917; ASN_GLN_ASE_2; 1.
DR   PROSITE; PS51732; ASN_GLN_ASE_3; 1.
PE   2: Evidence at transcript level;
KW   Hydrolase; Reference proteome; Signal.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000255"
FT   CHAIN           20..375
FT                   /note="L-asparaginase 2"
FT                   /id="PRO_0000171077"
FT   DOMAIN          51..375
FT                   /note="Asparaginase/glutaminase"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01068"
FT   REGION          22..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        61
FT                   /note="O-isoaspartyl threonine intermediate"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU10099,
FT                   ECO:0000255|PROSITE-ProRule:PRU10100"
FT   BINDING         108
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         141..142
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   375 AA;  40103 MW;  95FC5A221CE57B58 CRC64;
     MKKQRMLVLF TALLFVFTGC SHSPETKESP KEKAQTQKVS SASASEKKDL PNIRILATGG
     TIAGADQSKT STTEYKAGVV GVESLIEAVP EMKDIANVSG EQIVNVGSTN IDNKILLKLA
     KRINHLLASD DVDGIVVTHG TDTLEETAYF LNLTVKSDKP VVIVGSMRPS TAISADGPSN
     LYNAVKVAGA PEAKGKGTLV VLNDRIASAR YVTKTNTTTT DTFKSEEMGF VGTIADDIYF
     NNEITRKHTK DTDFSVSNLD ELPQVDIIYG YQNDGSYLFD AAVKAGAKGI VFAGSGNGSL
     SDAAEKGADS AVKKGVTVVR STRTGNGVVT PNQDYAEKDL LASNSLNPQK ARMLLMLALT
     KTNDPQKIQA YFNEY