ID   PEPS_STRTR              Reviewed;         413 AA.
AC   Q9X4A7;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Aminopeptidase PepS;
DE            EC=3.4.11.- {ECO:0000269|PubMed:10406960};
GN   Name=pepS;
OS   Streptococcus thermophilus.
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=1308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE, FUNCTION,
RP   CATALYTIC ACTIVITY, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC   STRAIN=CNRZ 302;
RX   PubMed=10406960; DOI=10.1046/j.1432-1327.1999.00528.x;
RA   Fernandez-Espla M.D., Rul F.;
RT   "PepS from Streptococcus thermophilus. A new member of the aminopeptidase T
RT   family of thermophilic bacteria.";
RL   Eur. J. Biochem. 263:502-510(1999).
CC   -!- FUNCTION: Exhibits a high specificity towards peptides possessing
CC       arginine or aromatic amino acids at the N-terminus. Could be involved
CC       both in bacterial growth by supplying amino acids.
CC       {ECO:0000269|PubMed:10406960}.
CC   -!- COFACTOR:
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000269|PubMed:10406960};
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000269|PubMed:10406960};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:10406960};
CC       Note=Binds 2 divalent metal cations per subunit (By similarity). Can
CC       use cobalt, zinc, and possibly also magnesium ions (PubMed:10406960).
CC       {ECO:0000250|UniProtKB:P42778, ECO:0000269|PubMed:10406960};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       pH dependence:
CC         Optimum pH is 7.5-8.5. {ECO:0000269|PubMed:10406960};
CC       Temperature dependence:
CC         Optimum temperature is 55 degrees Celsius.
CC         {ECO:0000269|PubMed:10406960};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10406960}.
CC   -!- SIMILARITY: Belongs to the peptidase M29 family. {ECO:0000305}.
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DR   EMBL; AF102860; AAD28348.1; -; Genomic_DNA.
DR   RefSeq; WP_014727288.1; NZ_WMLD01000019.1.
DR   AlphaFoldDB; Q9X4A7; -.
DR   SMR; Q9X4A7; -.
DR   STRING; 322159.STER_0096; -.
DR   MEROPS; M29.004; -.
DR   PRIDE; Q9X4A7; -.
DR   KEGG; ag:AAD28348; -.
DR   eggNOG; COG2309; Bacteria.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0008237; F:metallopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1830.10; -; 1.
DR   InterPro; IPR035097; M29_N-terminal.
DR   InterPro; IPR000787; Peptidase_M29.
DR   Pfam; PF02073; Peptidase_M29; 1.
DR   PRINTS; PR00919; THERMOPTASE.
PE   1: Evidence at protein level;
KW   Aminopeptidase; Direct protein sequencing; Hydrolase; Metal-binding;
KW   Metalloprotease; Protease.
FT   CHAIN           1..413
FT                   /note="Aminopeptidase PepS"
FT                   /id="PRO_0000079177"
FT   BINDING         253
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P42778"
FT   BINDING         319
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P42778"
FT   BINDING         319
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P42778"
FT   BINDING         343
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P42778"
FT   BINDING         343
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P42778"
FT   BINDING         348
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P42778"
FT   BINDING         381
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P42778"
FT   BINDING         383
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P42778"
SQ   SEQUENCE   413 AA;  45318 MW;  5E90C2D093CCBE20 CRC64;
     MVLPNFKENL EKYAKLLVTN GINVQPGHTV ALSIDVEQAE LAHLLVKEAY ALGAAEVIVQ
     WSDDTINRER FLHAEMNRIE EVPAYKKAEM EYLLEKKASR LGVRSSDPDA FNGVAPERLS
     AHAKAIGAAF KPMQVATQSN KVSWTVAAAA GKEWAKKVFP NASSDEEAVD LLWNQIFKTC
     RVYEKDPVRA WKEHADRLDA KARILNEAQF SALHYTAPGT DLTLGLPKNH VWESAGAINA
     QGESFLPNMP TEEVFTAPDF RRAYGYVSST KPLSYNGNII EGIKVTFKDG EIVDITADQG
     EKVMKNLVFN NNGARALGEC ALVPDSSPIS QSGITFFNTL FDENASNHLA IGAAYATSVE
     GGADMTEEEL KAAGLNRSDV HVDFIIGSNQ MNIDGIHHDG SRVPIFRNGD WVI