ID   AK2_BACSU               Reviewed;         408 AA.
AC   P08495; P08496; P94554; P97183;
DT   01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT   04-AUG-2003, sequence version 2.
DT   16-JUN-2009, entry version 90.
DE   RecName: Full=Aspartokinase 2;
DE            EC=2.7.2.4;
DE   AltName: Full=Aspartokinase II;
DE   AltName: Full=Aspartate kinase 2;
GN   Name=lysC; OrderedLocusNames=BSU28470;
OS   Bacillus subtilis.
OC   Bacteria; Firmicutes; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1423;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   MEDLINE=87250503; PubMed=3036830;
RA   Chen N.-Y., Hu F.M., Paulus H.;
RT   "Nucleotide sequence of the overlapping genes for the subunits of
RT   Bacillus subtilis aspartokinase II and their control regions.";
RL   J. Biol. Chem. 262:8787-8798(1987).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=97124191; PubMed=8969504;
RA   Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J.,
RA   Emmerson P.T., Harwood C.R.;
RT   "The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus
RT   subtilis chromosome containing genes responsible for stress responses,
RT   the utilization of plant cell walls and primary metabolism.";
RL   Microbiology 142:3067-3078(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   MEDLINE=98044033; PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G.,
RA   Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S.,
RA   Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S.,
RA   Brouillet S., Bruschi C.V., Caldwell B., Capuano V., Carter N.M.,
RA   Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A.,
RA   Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T.,
RA   Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D.,
RA   Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N.,
RA   Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G.,
RA   Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A.,
RA   Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M.,
RA   Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M.,
RA   Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S.,
RA   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.,
RA   Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B.,
RA   Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R.,
RA   Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P.,
RA   Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H.,
RA   Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P.,
RA   Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F.,
RA   Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H.,
RA   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   [4]
RP   ALTERNATIVE INITIATION.
RX   MEDLINE=88243847; PubMed=2837491;
RA   Chen N.-Y., Paulus H.;
RT   "Mechanism of expression of the overlapping genes of Bacillus subtilis
RT   aspartokinase II.";
RL   J. Biol. Chem. 263:9526-9532(1988).
RN   [5]
RP   REGULATION BY DEGRADATION.
RX   MEDLINE=90368669; PubMed=2168395;
RA   Graves L.M., Switzer R.L.;
RT   "Aspartokinase II from Bacillus subtilis is degraded in response to
RT   nutrient limitation.";
RL   J. Biol. Chem. 265:14947-14955(1990).
CC   -!- CATALYTIC ACTIVITY: ATP + L-aspartate = ADP + 4-phospho-L-
CC       aspartate.
CC   -!- ENZYME REGULATION: Lysine-sensitive. Regulated by degradation in
CC       response to starvation of cells for various nutrients. Ammonium
CC       starvation induced the fastest aspartokinase II decline, followed
CC       by amino acid starvation and glucose limitation.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-lysine biosynthesis via DAP
CC       pathway; tetrahydrodipicolinate from L-aspartate: step 1/4.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-methionine biosynthesis via de
CC       novo pathway; L-homoserine from L-aspartate: step 1/3.
CC   -!- PATHWAY: Amino-acid biosynthesis; L-threonine biosynthesis; L-
CC       threonine from L-aspartate: step 1/5.
CC   -!- SUBUNIT: Tetramer consisting of 2 isoforms Alpha (catalytic) and 2
CC       isoforms Beta (function not known).
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative initiation; Named isoforms=2;
CC       Name=Alpha; Synonyms=Aspartokinase 2 subunit alpha;
CC         IsoId=P08495-1; Sequence=Displayed;
CC       Name=Beta; Synonyms=Aspartokinase 2 subunit beta;
CC         IsoId=P08495-2; Sequence=VSP_018655;
CC   -!- SIMILARITY: Belongs to the aspartokinase family.
CC   -!- SIMILARITY: Contains 2 ACT domains.
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DR   EMBL; J03294; AAA87318.1; -; Genomic_DNA.
DR   EMBL; J03294; AAA87319.1; -; Genomic_DNA.
DR   EMBL; Z75208; CAA99580.1; -; Genomic_DNA.
DR   EMBL; Z75208; CAA99581.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14807.1; -; Genomic_DNA.
DR   PIR; A29314; A29314.
DR   RefSeq; NP_390725.1; -.
DR   GeneID; 937451; -.
DR   GenomeReviews; AL009126_GR; BSU28470.
DR   KEGG; bsu:BSU28470; -.
DR   NMPDR; fig|224308.1.peg.2850; -.
DR   SubtiList; BG10350; lysC.
DR   HOGENOM; P08495; -.
DR   OMA; P08495; MGKTTDN.
DR   BioCyc; BSUB224308:BSU2843-MON; -.
DR   BioCyc; MetaCyc:MON-6561; -.
DR   BioCyc; MetaCyc:MON-6562; -.
DR   BRENDA; 2.7.2.4; 150.
DR   GO; GO:0016597; F:amino acid binding; IEA:InterPro.
DR   GO; GO:0004072; F:aspartate kinase activity; IEA:EC.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0019877; P:diaminopimelate biosynthetic process; IEA:UniProtKB-KW.
DR   InterPro; IPR002912; ACT_bd.
DR   InterPro; IPR001048; Asp/Glu/Uridylate_kinase.
DR   InterPro; IPR005260; Asp_kin_monofn.
DR   InterPro; IPR001341; Asp_kin_reg.
DR   InterPro; IPR018042; Aspartate_kinase_CS.
DR   Gene3D; G3DSA:3.40.1160.10; Aa_kinase; 1.
DR   Pfam; PF00696; AA_kinase; 1.
DR   Pfam; PF01842; ACT; 2.
DR   TIGRFAMs; TIGR00656; asp_kin_monofn; 1.
DR   TIGRFAMs; TIGR00657; asp_kinases; 1.
DR   PROSITE; PS00324; ASPARTOKINASE; 1.
PE   3: Inferred from homology;
KW   Alternative initiation; Amino-acid biosynthesis; ATP-binding;
KW   Complete proteome; Diaminopimelate biosynthesis; Kinase;
KW   Lysine biosynthesis; Nucleotide-binding; Repeat; Transferase.
FT   CHAIN         1    408       Aspartokinase 2.
FT                                /FTId=PRO_0000002373.
FT   DOMAIN      276    335       ACT 1.
FT   DOMAIN      342    407       ACT 2.
FT   VAR_SEQ       1    245       Missing (in isoform Beta).
FT                                /FTId=VSP_018655.
FT   CONFLICT    166    166       A -> V (in Ref. 1; AAA87318).
SQ   SEQUENCE   408 AA;  43808 MW;  2E7189F938F97120 CRC64;
     MGLIVQKFGG TSVGSVEKIQ NAANRAIAEK QKGHQVVVVV SAMGKSTDEL VSLAKAISDQ
     PSKREMDMLL ATGEQVTISL LSMALQEKGY DAVSYTGWQA GIRTEAIHGN ARITDIDTSV
     LADQLEKGKI VIVAGFQGMT EDCEITTLGR GGSDTTAVAL AAALKADKCD IYTDVPGVFT
     TDPRYVKSAR KLEGISYDEM LELANLGAGV LHPRAVEFAK NYQVPLEVRS STETEAGTLI
     EEESSMEQNL IVRGIAFEDQ ITRVTIYGLT SGLTTLSTIF TTLAKRNINV DIIIQTQAED
     KTGISFSVKT EDADQTVAVL EEYKDALEFE KIETESKLAK VSIVGSGMVS NPGVAAEMFA
     VLAQKNILIK MVSTSEIKVS TVVSENDMVK AVESLHDAFE LSKHPSAV
//