Reviewed, UniProtKB/Swiss-Prot P08495 (AK2_BACSU)

Names and origin

Protein names

Recommended name:
    Aspartokinase 2
    EC=2.7.2.4
Alternative name(s):
    Aspartokinase II
    Aspartate kinase 2

Gene names

Name:	lysC
Ordered Locus Names:	BSU28470

Organism

Bacillus subtilis [Complete proteome] [HAMAP]

Taxonomic identifier

1423 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Bacillus

Protein attributes

Sequence length	408 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Inferred from homology.

General annotation (Comments)

Catalytic activity	ATP + L-aspartate = ADP + 4-phospho-L-aspartate.
Enzyme regulation	Lysine-sensitive. Regulated by degradation in response to starvation of cells for various nutrients. Ammonium starvation induced the fastest aspartokinase II decline, followed by amino acid starvation and glucose limitation.
Pathway	Amino-acid biosynthesis; L-lysine biosynthesis via DAP pathway; (S)-tetrahydrodipicolinate from L-aspartate: step 1/4. Amino-acid biosynthesis; L-methionine biosynthesis via de novo pathway; L-homoserine from L-aspartate: step 1/3. Amino-acid biosynthesis; L-threonine biosynthesis; L-threonine from L-aspartate: step 1/5.
Subunit structure	Tetramer consisting of 2 isoforms Alpha (catalytic) and 2 isoforms Beta (function not known).
Sequence similarities	Belongs to the aspartokinase family. Contains 2 ACT domains.

Ontologies

Keywords
Biological process	Amino-acid biosynthesis Diaminopimelate biosynthesis Lysine biosynthesis
Coding sequence diversity	Alternative initiation
Domain	Repeat
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	diaminopimelate biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW amino acid binding Inferred from electronic annotation. Source: InterPro aspartate kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative initiation. [Align] [Select]

Isoform Alpha (identifier: P08495-1)

Also known as: Aspartokinase 2 subunit alpha;

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform Beta (identifier: P08495-2)

Also known as: Aspartokinase 2 subunit beta;

The sequence of this isoform differs from the canonical sequence as follows:
     1-245: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 408	408	Aspartokinase 2		PRO_0000002373
Regions
	Domain	276 – 335	60	ACT 1
	Domain	342 – 407	66	ACT 2
Natural variations
	Alternative sequence	1 – 245	245	Missing in isoform Beta.		VSP_018655
Experimental info
	Sequence conflict	166	1	A → V in AAA87318. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform Alpha (Aspartokinase 2 subunit alpha) [UniParc]. Last modified August 4, 2003. Version 2. Checksum: 2E7189F938F97120	FASTA	408	43,808
	10 20 30 40 50 60 MGLIVQKFGG TSVGSVEKIQ NAANRAIAEK QKGHQVVVVV SAMGKSTDEL VSLAKAISDQ 70 80 90 100 110 120 PSKREMDMLL ATGEQVTISL LSMALQEKGY DAVSYTGWQA GIRTEAIHGN ARITDIDTSV 130 140 150 160 170 180 LADQLEKGKI VIVAGFQGMT EDCEITTLGR GGSDTTAVAL AAALKADKCD IYTDVPGVFT 190 200 210 220 230 240 TDPRYVKSAR KLEGISYDEM LELANLGAGV LHPRAVEFAK NYQVPLEVRS STETEAGTLI 250 260 270 280 290 300 EEESSMEQNL IVRGIAFEDQ ITRVTIYGLT SGLTTLSTIF TTLAKRNINV DIIIQTQAED 310 320 330 340 350 360 KTGISFSVKT EDADQTVAVL EEYKDALEFE KIETESKLAK VSIVGSGMVS NPGVAAEMFA 370 380 390 400 VLAQKNILIK MVSTSEIKVS TVVSENDMVK AVESLHDAFE LSKHPSAV
	Isoform Beta (Aspartokinase 2 subunit beta). Checksum: EDEE1FD394D18A58	FASTA	163	17,726
	10 20 30 40 50 60 MEQNLIVRGI AFEDQITRVT IYGLTSGLTT LSTIFTTLAK RNINVDIIIQ TQAEDKTGIS 70 80 90 100 110 120 FSVKTEDADQ TVAVLEEYKD ALEFEKIETE SKLAKVSIVG SGMVSNPGVA AEMFAVLAQK 130 140 150 160 NILIKMVSTS EIKVSTVVSE NDMVKAVESL HDAFELSKHP SAV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of the overlapping genes for the subunits of Bacillus subtilis aspartokinase II and their control regions." Chen N.-Y., Hu F.M., Paulus H. J. Biol. Chem. 262:8787-8798(1987) [PubMed: 3036830] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]	"The dnaB-pheA (256 degrees-240 degrees) region of the Bacillus subtilis chromosome containing genes responsible for stress responses, the utilization of plant cell walls and primary metabolism." Wipat A., Carter N., Brignell C.S., Guy J.B., Piper K., Sanders J., Emmerson P.T., Harwood C.R. Microbiology 142:3067-3078(1996) [PubMed: 8969504] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: 168.
[3]	"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis." Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A. Nature 390:249-256(1997) [PubMed: 9384377] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: 168.
[4]	"Mechanism of expression of the overlapping genes of Bacillus subtilis aspartokinase II." Chen N.-Y., Paulus H. J. Biol. Chem. 263:9526-9532(1988) [PubMed: 2837491] [Abstract] Cited for: ALTERNATIVE INITIATION.
[5]	"Aspartokinase II from Bacillus subtilis is degraded in response to nutrient limitation." Graves L.M., Switzer R.L. J. Biol. Chem. 265:14947-14955(1990) [PubMed: 2168395] [Abstract] Cited for: REGULATION BY DEGRADATION.

Cross-references

Sequence databases
EMBLGenBankDDBJ	J03294 Genomic DNA. Translation: AAA87318.1. J03294 Genomic DNA. Translation: AAA87319.1. Z75208 Genomic DNA. Translation: CAA99580.1. Z75208 Genomic DNA. Translation: CAA99581.1. AL009126 Genomic DNA. Translation: CAB14807.1.
PIR	A29314.
RefSeq	NP_390725.1.
3D structure databases
ModBase	Search...
Genome annotation databases
GeneID	937451.
GenomeReviews	Gene locus BSU28470 in contig AL009126_GR.
KEGG	bsu:BSU28470.
NMPDR	fig|224308.1.peg.2850.
Organism-specific databases
SubtiList	BG10350. lysC. [Micado]
CMR	Search...
Phylogenomic databases
HOGENOM	P08495.
OMA	MGKTTDN.
Enzyme and pathway databases
BioCyc	BSUB224308:BSU2843-MON. MetaCyc:MON-6561. MetaCyc:MON-6562.
BRENDA	2.7.2.4. 150.
Family and domain databases
InterPro	IPR002912. ACT_bd. IPR001048. Asp/Glu/Uridylate_kinase. IPR005260. Asp_kin_monofn. IPR001341. Asp_kin_reg. IPR018042. Aspartate_kinase_CS. [Graphical view]
Gene3D	G3DSA:3.40.1160.10. Aa_kinase. 1 hit.
Pfam	PF00696. AA_kinase. 1 hit. PF01842. ACT. 2 hits. [Graphical view]
TIGRFAMs	TIGR00656. asp_kin_monofn. 1 hit. TIGR00657. asp_kinases. 1 hit.
PROSITE	PS00324. ASPARTOKINASE. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AK2_BACSU

Accession

Primary (citable) accession number: P08495
Secondary accession number(s): P08496, P94554, P97183

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1988
Last sequence update:	August 4, 2003
Last modified:	November 3, 2009
This is version 92 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)