PEPT_SALTY
ID PEPT_SALTY Reviewed; 409 AA.
AC P26311;
DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1992, sequence version 1.
DT 03-AUG-2022, entry version 146.
DE RecName: Full=Peptidase T;
DE EC=3.4.11.4;
DE AltName: Full=Aminotripeptidase;
DE Short=Tripeptidase;
DE AltName: Full=Tripeptide aminopeptidase;
GN Name=pepT; OrderedLocusNames=STM1227;
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], AND PROTEIN SEQUENCE OF 1-22.
RX PubMed=1904438; DOI=10.1128/jb.173.11.3554-3558.1991;
RA Miller C.G., Miller J.L., Bagga D.A.;
RT "Cloning and nucleotide sequence of the anaerobically regulated pepT gene
RT of Salmonella typhimurium.";
RL J. Bacteriol. 173:3554-3558(1991).
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).
RN [3]
RP FUNCTION, CHARACTERIZATION, SUBSTRATE SPECIFICITY, AND ACTIVITY REGULATION.
RX PubMed=6341363; DOI=10.1128/jb.154.2.763-771.1983;
RA Strauch K.L., Miller C.G.;
RT "Isolation and characterization Salmonella typhimurium mutants lacking a
RT tripeptidase (peptidase T).";
RL J. Bacteriol. 154:763-771(1983).
RN [4]
RP CRYSTALLIZATION.
RX PubMed=10930847; DOI=10.1107/s0907444900006375;
RA Hakansson K., Broder D., Wang A.H., Miller C.G.;
RT "Crystallization of peptidase T from Salmonella typhimurium.";
RL Acta Crystallogr. D 56:924-926(2000).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.4 ANGSTROMS) IN COMPLEX WITH ZINC, COFACTOR, AND
RP SUBUNIT.
RX PubMed=11856302; DOI=10.1046/j.0014-2956.2001.02665.x;
RA Hakansson K., Miller C.G.;
RT "Structure of peptidase T from Salmonella typhimurium.";
RL Eur. J. Biochem. 269:443-450(2002).
CC -!- FUNCTION: Cleaves the N-terminal amino acid of tripeptides. Hydrolyzes
CC tripeptides containing N-terminal methionine, leucine, or
CC phenylalanine. Displays little or no activity against dipeptides, N-
CC blocked or C-blocked tripeptides, and tetrapeptides.
CC {ECO:0000269|PubMed:6341363}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of the N-terminal residue from a tripeptide.;
CC EC=3.4.11.4;
CC -!- COFACTOR:
CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC Evidence={ECO:0000269|PubMed:11856302};
CC Note=Binds 2 Zn(2+) ions per subunit. {ECO:0000269|PubMed:11856302};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA. {ECO:0000269|PubMed:6341363}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11856302}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the peptidase M20B family. {ECO:0000305}.
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DR EMBL; M62725; AAA27183.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20156.1; -; Genomic_DNA.
DR PIR; A42363; A42363.
DR RefSeq; NP_460197.1; NC_003197.2.
DR RefSeq; WP_000359410.1; NC_003197.2.
DR PDB; 1FNO; X-ray; 2.40 A; A=1-409.
DR PDBsum; 1FNO; -.
DR AlphaFoldDB; P26311; -.
DR SMR; P26311; -.
DR STRING; 99287.STM1227; -.
DR MEROPS; M20.003; -.
DR PaxDb; P26311; -.
DR EnsemblBacteria; AAL20156; AAL20156; STM1227.
DR GeneID; 1252745; -.
DR KEGG; stm:STM1227; -.
DR PATRIC; fig|99287.12.peg.1298; -.
DR HOGENOM; CLU_053676_0_0_6; -.
DR OMA; GHNFHGK; -.
DR PhylomeDB; P26311; -.
DR BioCyc; SENT99287:STM1227-MON; -.
DR EvolutionaryTrace; P26311; -.
DR Proteomes; UP000001014; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0045148; F:tripeptide aminopeptidase activity; IBA:GO_Central.
DR GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR GO; GO:0043171; P:peptide catabolic process; IEA:UniProtKB-UniRule.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-UniRule.
DR HAMAP; MF_00550; Aminopeptidase_M20; 1.
DR InterPro; IPR001261; ArgE/DapE_CS.
DR InterPro; IPR036264; Bact_exopeptidase_dim_dom.
DR InterPro; IPR002933; Peptidase_M20.
DR InterPro; IPR011650; Peptidase_M20_dimer.
DR InterPro; IPR010161; Peptidase_M20B.
DR PANTHER; PTHR42994:SF1; PTHR42994:SF1; 1.
DR Pfam; PF07687; M20_dimer; 1.
DR Pfam; PF01546; Peptidase_M20; 1.
DR PIRSF; PIRSF037215; Peptidase_M20B; 1.
DR SUPFAM; SSF55031; SSF55031; 1.
DR TIGRFAMs; TIGR01882; peptidase-T; 1.
DR PROSITE; PS00758; ARGE_DAPE_CPG2_1; 1.
DR PROSITE; PS00759; ARGE_DAPE_CPG2_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Aminopeptidase; Cytoplasm; Direct protein sequencing;
KW Hydrolase; Metal-binding; Metalloprotease; Protease; Reference proteome;
KW Zinc.
FT CHAIN 1..409
FT /note="Peptidase T"
FT /id="PRO_0000185312"
FT REGION 1..207
FT /note="Catalytic N-terminal"
FT REGION 208..318
FT /note="Dimerization"
FT REGION 319..409
FT /note="Catalytic C-terminal"
FT ACT_SITE 80
FT /evidence="ECO:0000250"
FT ACT_SITE 173
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 78
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11856302"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11856302"
FT BINDING 140
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11856302"
FT BINDING 174
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11856302"
FT BINDING 196
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:11856302"
FT BINDING 379
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:11856302"
FT HELIX 4..12
FT /evidence="ECO:0007829|PDB:1FNO"
FT STRAND 23..28
FT /evidence="ECO:0007829|PDB:1FNO"
FT HELIX 29..45
FT /evidence="ECO:0007829|PDB:1FNO"
FT STRAND 48..52
FT /evidence="ECO:0007829|PDB:1FNO"
FT STRAND 58..62
FT /evidence="ECO:0007829|PDB:1FNO"
FT STRAND 73..78
FT /evidence="ECO:0007829|PDB:1FNO"
FT STRAND 93..95
FT /evidence="ECO:0007829|PDB:1FNO"
FT STRAND 106..109
FT /evidence="ECO:0007829|PDB:1FNO"
FT TURN 114..116
FT /evidence="ECO:0007829|PDB:1FNO"
FT HELIX 118..122
FT /evidence="ECO:0007829|PDB:1FNO"
FT STRAND 128..130
FT /evidence="ECO:0007829|PDB:1FNO"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:1FNO"
FT HELIX 139..156
FT /evidence="ECO:0007829|PDB:1FNO"
FT STRAND 157..159
FT /evidence="ECO:0007829|PDB:1FNO"
FT STRAND 165..171
FT /evidence="ECO:0007829|PDB:1FNO"
FT HELIX 173..175
FT /evidence="ECO:0007829|PDB:1FNO"
FT TURN 178..181
FT /evidence="ECO:0007829|PDB:1FNO"
FT HELIX 184..187
FT /evidence="ECO:0007829|PDB:1FNO"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:1FNO"
FT STRAND 202..204
FT /evidence="ECO:0007829|PDB:1FNO"
FT STRAND 209..218
FT /evidence="ECO:0007829|PDB:1FNO"
FT HELIX 224..226
FT /evidence="ECO:0007829|PDB:1FNO"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:1FNO"
FT HELIX 234..243
FT /evidence="ECO:0007829|PDB:1FNO"
FT HELIX 251..253
FT /evidence="ECO:0007829|PDB:1FNO"
FT STRAND 260..268
FT /evidence="ECO:0007829|PDB:1FNO"
FT STRAND 270..283
FT /evidence="ECO:0007829|PDB:1FNO"
FT HELIX 284..301
FT /evidence="ECO:0007829|PDB:1FNO"
FT TURN 302..304
FT /evidence="ECO:0007829|PDB:1FNO"
FT STRAND 311..319
FT /evidence="ECO:0007829|PDB:1FNO"
FT HELIX 323..327
FT /evidence="ECO:0007829|PDB:1FNO"
FT HELIX 331..342
FT /evidence="ECO:0007829|PDB:1FNO"
FT STRAND 352..354
FT /evidence="ECO:0007829|PDB:1FNO"
FT HELIX 357..361
FT /evidence="ECO:0007829|PDB:1FNO"
FT TURN 362..365
FT /evidence="ECO:0007829|PDB:1FNO"
FT STRAND 374..377
FT /evidence="ECO:0007829|PDB:1FNO"
FT STRAND 384..386
FT /evidence="ECO:0007829|PDB:1FNO"
FT HELIX 387..406
FT /evidence="ECO:0007829|PDB:1FNO"
SQ SEQUENCE 409 AA; 44849 MW; 7943CBFAD74017A9 CRC64;
MDKLLERFLH YVSLDTQSKS GVRQVPSTEG QWKLLRLLKQ QLEEMGLVNI TLSEKGTLMA
TLPANVEGDI PAIGFISHVD TSPDFSGKNV NPQIVENYRG GDIALGIGDE VLSPVMFPVL
HQLLGQTLIT TDGKTLLGAD DKAGVAEIMT ALAVLKGNPI PHGDIKVAFT PDEEVGKGAK
HFDVEAFGAQ WAYTVDGGGV GELEFENFNA ASVNIKIVGN NVHPGTAKGV MVNALSLAAR
IHAEVPADEA PETTEGYEGF YHLASMKGTV DRAEMHYIIR DFDRKQFEAR KRKMMEIAKK
VGKGLHPDCY IELVIEDSYY NMREKVVEHP HILDIAQQAM RDCHITPEMK PIRGGTDGAQ
LSFMGLPCPN LFTGGYNYHG KHEFVTLEGM EKAVQVIVRI AELTAKRGQ
