Isoaspartyl peptidase precursor - Escherichia coli (strain K12)

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P37595 (IAAA_ECOLI) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 95. History...

Clusters with 100%, 90%, 50% identity |

Documents (3) |

Third-party data

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Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents Customize order

Names and origin

Protein names

Recommended name:
Isoaspartyl peptidase
EC=3.4.19.5

Alternative name(s):
Beta-aspartyl-peptidase
EcAIII
Isoaspartyl dipeptidase

Gene names

Name:	iaaA
Synonyms:	spt, ybiK
Ordered Locus Names:	b0828, JW0812

Organism

Escherichia coli (strain K12)

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	321 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Degrades proteins damaged by L-isoaspartyl residue formation (also known as beta-Asp residues). Degrades L-isoaspartyl-containing di- and maybe also tripeptides. Also has L-asparaginase activity, although this may not be its principal function. Ref.5 Ref.8 May be involved in glutathione, and possibly other peptide, transport, although these results could also be due to polar effects of disruption. Ref.5 Ref.8
Catalytic activity	Cleavage of a beta-linked Asp residue from the N-terminus of a polypeptide.
Subunit structure	Heterotetramer of two alpha and two beta chains arranged as a dimer of alpha/beta heterodimers. Ref.5 Ref.7 Ref.11
Induction	Repressed by cysteine, an effect that is attributed to CysB.
Post-translational modification	Autocleaved. Generates the alpha and beta subunits. The N-terminal residue of the beta subunit is thought to be responsible for the nucleophile hydrolase activity. Ref.5 Ref.7 Both subunits undergo further processing at their C-termini. The overexpressed alpha subunit seems to consist of residues 2-161, with an oxidized Met residue and a tighly coordinated Na⁺, whereas the overexpressed beta subunit is processed to residue 315 and has 3 oxidized Met residues. Processing of the alpha subunit is inhibited by Zn²⁺.
Sequence similarities	Belongs to the Ntn-hydrolase family.
Biophysicochemical properties	Kinetic parameters: No activity for GlcNAc-Asn, Gly-L-Asn, L-Asp, L-Asn-alpha-amide, L-Gln, aspartylglucosamides alpha- or gamma-aspartyl dipeptides. K_M=0.138 mM for beta-L-Asp-L-Leu Ref.9 K_M=3.9 mM for L-Asn
Mass spectrometry	Molecular mass is 17091 Da from positions 2 - 161. Determined by ESI. Subunit alpha. Ref.9 Molecular mass is 13852 Da from positions 179 - 315. Determined by ESI. Subunit beta. Ref.9

Ontologies

Keywords
Molecular function	Hydrolase Protease
PTM	Autocatalytic cleavage
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	asparagine catabolic process via L-aspartate Inferred from Biological aspect of Ancestor. Source: RefGenome protein maturation Inferred from Biological aspect of Ancestor. Source: RefGenome proteolysis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular component	cytoplasm Inferred by curator Ref.12. Source: EcoliWiki
Molecular function	aminopeptidase activity Inferred from direct assay Ref.9. Source: EcoliWiki asparaginase activity Inferred from direct assay Ref.9. Source: EcoliWiki beta-aspartyl-peptidase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 178

177

Isoaspartyl peptidase subunit alpha

PRO_0000002349

Chain

179 – 321

143

Isoaspartyl peptidase subunit beta

PRO_0000329014

Sites

Active site

179

Nucleophile By similarity

Site

178 – 179

Cleavage; by autolysis

Experimental info

Mutagenesis

179

T → A: Catalytically inactive.

Secondary structure

321

Helix Strand Turn

Details...

Sequences

Sequence

Length

Mass (Da)

Tools

P37595 [UniParc].

Last modified November 1, 1997. Version 2.
Checksum: 85C6D5377DA0B84D
Show »

FASTA

321

33,394

        10         20         30         40         50         60 
MGKAVIAIHG GAGAISRAQM SLQQELRYIE ALSAIVETGQ KMLEAGESAL DVVTEAVRLL 

        70         80         90        100        110        120 
EECPLFNAGI GAVFTRDETH ELDACVMDGN TLKAGAVAGV SHLRNPVLAA RLVMEQSPHV 

       130        140        150        160        170        180 
MMIGEGAENF AFARGMERVS PEIFSTSLRY EQLLAARKEG ATVLDHSGAP LDEKQKMGTV 

       190        200        210        220        230        240 
GAVALDLDGN LAAATSTGGM TNKLPGRVGD SPLVGAGCYA NNASVAVSCT GTGEVFIRAL 

       250        260        270        280        290        300 
AAYDIAALMD YGGLSLAEAC ERVVMEKLPA LGGSGGLIAI DHEGNVALPF NTEGMYRAWG 

       310        320 
YAGDTPTTGI YREKGDTVAT Q

« Hide

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 12.7-28.0 min region on the linkage map." Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K., Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S., Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K. Horiuchi T. DNA Res. 3:137-155(1996) [PubMed: 8905232] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Cloning and sequencing of the Escherichia coli chlEN operon involved in molybdopterin biosynthesis." Nohno T., Kasai Y., Saito T. J. Bacteriol. 170:4097-4102(1988) [PubMed: 3045084] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-52.
[5]	"Isoaspartyl dipeptidase activity of plant-type asparaginases." Hejazi M., Piotukh K., Mattow J., Deutzmann R., Volkmer-Engert R., Lockau W. Biochem. J. 364:129-136(2002) [PubMed: 11988085] [Abstract] Cited for: PROTEIN SEQUENCE OF 179-183, FUNCTION, SUBUNIT, AUTOCATALYTIC CLEAVAGE.
[6]	"Intrinsic and extrinsic approaches for detecting genes in a bacterial genome." Borodovsky M., Rudd K.E., Koonin E.V. Nucleic Acids Res. 22:4756-4767(1994) [PubMed: 7984428] [Abstract] Cited for: IDENTIFICATION.
[7]	"Crystallization and preliminary crystallographic studies of a new L-asparaginase encoded by the Escherichia coli genome." Borek D., Jaskolski M. Acta Crystallogr. D 56:1505-1507(2000) [PubMed: 11053866] [Abstract] Cited for: PROBABLE AUTOCATALYTIC CLEAVAGE, SUBUNIT, PRELIMINARY CRYSTALLIZATION. Strain: K12 / JM108.
[8]	"Identification of a CysB-regulated gene involved in glutathione transport in Escherichia coli." Parry J., Clark D.P. FEMS Microbiol. Lett. 209:81-85(2002) [PubMed: 12007658] [Abstract] Cited for: POSSIBLE FUNCTION IN GLUTATHIONE TRANSPORT, CONTROL OF EXPRESSION BY CYSB. Strain: K12.
[9]	"Expression, purification and catalytic activity of Lupinus luteus asparagine beta-amidohydrolase and its Escherichia coli homolog." Borek D., Michalska K., Brzezinski K., Kisiel A., Podkowinski J., Bonthron D.T., Krowarsch D., Otlewski J., Jaskolski M. Eur. J. Biochem. 271:3215-3226(2004) [PubMed: 15265041] [Abstract] Cited for: MASS SPECTROMETRY, KINETIC PROPERTIES. Strain: K12 / DH5-alpha.
[10]	"Structural and biochemical studies of asparaginases." Borek D. Thesis (2001), A. Mickiewicz University, Poland Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-321.
[11]	"Structure of the isoaspartyl peptidase with L-asparaginase activity from Escherichia coli." Prahl A., Pazgier M., Hejazi M., Lockau W., Lubkowski J. Acta Crystallogr. D 60:1173-1176(2004) [PubMed: 15159592] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) OF 2-321, SUBUNIT.
[12]	"Crystal structure of isoaspartyl aminopeptidase in complex with L-aspartate." Michalska K., Brzezinski K., Jaskolski M. J. Biol. Chem. 280:28484-28491(2005) [PubMed: 15946951] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 2-315 IN COMPLEX WITH L-ASPARTATE. Strain: K12 / DH5-alpha.
[13]	"Crystal packing of plant-type L-asparaginase from Escherichia coli." Michalska K., Borek D., Hernandez-Santoyo A., Jaskolski M. Acta Crystallogr. D 64:309-320(2008) [PubMed: 18323626] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 2-313 OF MUTANT THR-179.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

U00096 Genomic DNA. Translation: AAC73915.1.
AP009048 Genomic DNA. Translation: BAA35516.1.
M21151 Genomic DNA. No translation available.

PIR

D64820.

RefSeq

NP_415349.1. NC_000913.2.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1JN9	X-ray	2.30	A/C	2-178	[»]
			B/D	179-321	[»]
1K2X	X-ray	1.65	A/C	2-178	[»]
			B/D	179-321	[»]
1T3M	X-ray	1.65	A/C	2-178	[»]
			B/D	179-321	[»]
2ZAK	X-ray	2.01	A/B	2-321	[»]
2ZAL	X-ray	1.90	A/C	2-161	[»]
			B/D	179-315	[»]
3C17	X-ray	1.95	A/B	2-321	[»]

ProteinModelPortal

P37595.

SMR

P37595. Positions 2-313.

ModBase

Search...

Protein-protein interaction databases

IntAct

P37595. 9 interactions.

Protein family/group databases

MEROPS

T02.002.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

EnsemblBacteria

EBESCT00000004409; EBESCP00000004409; EBESCG00000003596.
EBESCT00000016781; EBESCP00000016072; EBESCG00000015840.

GeneID

945456.

GenomeReviews

Gene locus JW0812 in contig AP009048_GR.
Gene locus b0828 in contig U00096_GR.

KEGG

ecj:JW0812.
eco:b0828.

PATRIC

32116859. VBIEscCol129921_0855.

Organism-specific databases

EchoBASE

EB2307.

EcoGene

EG12407. iaaA.

Phylogenomic databases

eggNOG

COG1446.

GeneTree

EBGT00050000011466.

HOGENOM

HBG735787.

OMA

NKQVGRV.

PhylomeDB

P37595.

ProtClustDB

PRK10226.

Enzyme and pathway databases

BioCyc

EcoCyc:EG12407-MONOMER.
MetaCyc:EG12407-MONOMER.

Gene expression databases

Genevestigator

P37595.

Family and domain databases

InterPro

IPR000246. Peptidase_T2.
[Graphical view]

K13051.

PANTHER

PTHR10188. Peptidase_T2. 1 hit.

Pfam

PF01112. Asparaginase_2. 1 hit.
[Graphical view]

ProtoNet

Search...

Other

DrugBank

DB00023. Asparaginase.
DB00059. Pegaspargase.

Entry information

Entry name

IAAA_ECOLI

Accession

Primary (citable) accession number: P37595
Secondary accession number(s): P75795

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1994
Last sequence update:	November 1, 1997
Last modified:	January 25, 2012
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program

Relevant documents

Escherichia coli

Escherichia coli (strain K12): entries and cross-references to EcoGene

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents

Preferred order of sections

Names and origin

Cleaved into the following 2 chains:

Protein attributes

General annotation (Comments)

Ontologies

Sequence annotation (Features)

Molecule processing

Sites

Experimental info

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other

Entry information

Relevant documents