IAAA_SALTY
ID IAAA_SALTY Reviewed; 313 AA.
AC Q7CQV5;
DT 22-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Isoaspartyl peptidase;
DE EC=3.4.19.5;
DE AltName: Full=Beta-aspartyl-peptidase;
DE AltName: Full=Isoaspartyl dipeptidase;
DE Contains:
DE RecName: Full=Isoaspartyl peptidase subunit alpha;
DE Contains:
DE RecName: Full=Isoaspartyl peptidase subunit beta;
DE Flags: Precursor;
GN Name=iaaA; OrderedLocusNames=STM0847;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10 AND 179-188,
RP AUTOCATALYTIC CLEAVAGE, MASS SPECTROMETRY, AND FUNCTION.
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11325937; DOI=10.1128/jb.183.10.3089-3097.2001;
RA Larsen R.A., Knox T.M., Miller C.G.;
RT "Aspartic peptide hydrolases in Salmonella enterica serovar typhimurium.";
RL J. Bacteriol. 183:3089-3097(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
CC -!- FUNCTION: Degrades proteins damaged by L-isoaspartyl residue formation
CC (also known as beta-Asp residues). Degrades L-isoaspartyl-containing
CC di- and tripeptides. Acts best on iso-Asp-Leu, followed by iso-Asp-Ala,
CC -His and to a lesser extent iso-Asp-Lys, -Phe and iso-Asp-Leu-Ala. Does
CC not act on internal iso-Asp bonds (Als-iso-Asp-Leu-Ala). Does not act
CC on alpha-Asp bonds. Has poor L-asparaginase activity.
CC {ECO:0000269|PubMed:11325937}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Cleavage of a beta-linked Asp residue from the N-terminus of a
CC polypeptide.; EC=3.4.19.5;
CC -!- SUBUNIT: Heterotetramer of two alpha and two beta chains arranged as a
CC dimer of alpha/beta heterodimers. {ECO:0000305}.
CC -!- PTM: Autocleaved. Generates the alpha and beta subunits. The beta
CC subunit is thought to be responsible for the nucleophile hydrolase
CC activity.
CC -!- MASS SPECTROMETRY: [Isoaspartyl peptidase subunit alpha]: Mass=18787.4;
CC Method=MALDI; Note=Subunit alpha.;
CC Evidence={ECO:0000269|PubMed:11325937};
CC -!- MASS SPECTROMETRY: [Isoaspartyl peptidase subunit beta]: Mass=13719.9;
CC Method=MALDI; Note=Subunit beta.;
CC Evidence={ECO:0000269|PubMed:11325937};
CC -!- SIMILARITY: Belongs to the Ntn-hydrolase family. {ECO:0000305}.
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DR EMBL; AE006468; AAL19783.1; -; Genomic_DNA.
DR RefSeq; NP_459824.1; NC_003197.2.
DR RefSeq; WP_001030503.1; NC_003197.2.
DR AlphaFoldDB; Q7CQV5; -.
DR SMR; Q7CQV5; -.
DR STRING; 99287.STM0847; -.
DR PaxDb; Q7CQV5; -.
DR EnsemblBacteria; AAL19783; AAL19783; STM0847.
DR GeneID; 1252366; -.
DR KEGG; stm:STM0847; -.
DR PATRIC; fig|99287.12.peg.884; -.
DR HOGENOM; CLU_021603_1_0_6; -.
DR OMA; YSRMRWK; -.
DR PhylomeDB; Q7CQV5; -.
DR BioCyc; SENT99287:STM0847-MON; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0004067; F:asparaginase activity; IBA:GO_Central.
DR GO; GO:0008798; F:beta-aspartyl-peptidase activity; IBA:GO_Central.
DR GO; GO:0016540; P:protein autoprocessing; IBA:GO_Central.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR InterPro; IPR000246; Peptidase_T2.
DR PANTHER; PTHR10188; PTHR10188; 1.
DR Pfam; PF01112; Asparaginase_2; 1.
DR SUPFAM; SSF56235; SSF56235; 1.
PE 1: Evidence at protein level;
KW Autocatalytic cleavage; Direct protein sequencing; Hydrolase; Protease;
KW Reference proteome.
FT CHAIN 1..178
FT /note="Isoaspartyl peptidase subunit alpha"
FT /id="PRO_0000344061"
FT CHAIN 179..313
FT /note="Isoaspartyl peptidase subunit beta"
FT /id="PRO_0000344062"
FT ACT_SITE 179
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT BINDING 207..210
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 230..233
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 178..179
FT /note="Cleavage; by autolysis"
SQ SEQUENCE 313 AA; 32473 MW; D37BD85830F9D83E CRC64;
MNKAVIAIHG GAGAIARAQM SHEQELRYIQ ALSEIVESGQ KMLEAGDSAL DVVTEAVRLL
EACPLFNAGI GAVYTRDGTH ELDACVMDGN TLKAGAVAGV SHVRHPVLAA RLVMERSPHV
LMVGEGAENF AFSQGMARVS PDIFSTPARY EQLLAARAAG EMALDHSGAP LDETKKMGTV
GAVARDKFGN LAAATSTGGM TNKLPGRVGD SPLVGAGCYA NNASVAVSCT GTGEVFIRTL
AAYDIAALME YGGLSLADAC ERVVMEKLPA LGGSGGLIAV DHEGNVALPF NSEGMYRAWG
YAGDTPTTGI YRE
