ID   PEPA_LACLM              Reviewed;         355 AA.
AC   Q48677; A2RIB3;
DT   15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 103.
DE   RecName: Full=Glutamyl aminopeptidase;
DE            EC=3.4.11.7;
GN   Name=pepA; OrderedLocusNames=llmg_0403;
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RX   PubMed=8535515; DOI=10.1099/13500872-141-11-2873;
RA   L'Anson K.J.A., Movahedi S., Griffin H.G., Gasson M.J., Mulholland F.;
RT   "A non-essential glutamyl aminopeptidase is required for optimal growth of
RT   Lactococcus lactis MG1363 in milk.";
RL   Microbiology 141:2873-2881(1995).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Release of N-terminal glutamate (and to a lesser extent
CC         aspartate) from a peptide.; EC=3.4.11.7;
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000250};
CC       Note=Binds 2 divalent metal cations per subunit. {ECO:0000250};
CC   -!- SIMILARITY: Belongs to the peptidase M42 family. {ECO:0000305}.
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DR   EMBL; X81089; CAA56994.1; -; Genomic_DNA.
DR   EMBL; AM406671; CAL97008.1; -; Genomic_DNA.
DR   RefSeq; WP_011834455.1; NZ_WJVF01000001.1.
DR   AlphaFoldDB; Q48677; -.
DR   SMR; Q48677; -.
DR   STRING; 416870.llmg_0403; -.
DR   MEROPS; M42.001; -.
DR   EnsemblBacteria; CAL97008; CAL97008; llmg_0403.
DR   KEGG; llm:llmg_0403; -.
DR   eggNOG; COG1363; Bacteria.
DR   HOGENOM; CLU_047249_0_2_9; -.
DR   OMA; FGWPAIH; -.
DR   PhylomeDB; Q48677; -.
DR   BioCyc; LLAC416870:LLMG_RS02065-MON; -.
DR   Proteomes; UP000000364; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.30.40; -; 1.
DR   InterPro; IPR017538; Pept_M42_glutamyl_aminopept.
DR   InterPro; IPR008007; Peptidase_M42.
DR   InterPro; IPR023367; Peptidase_M42_dom2.
DR   Pfam; PF05343; Peptidase_M42; 1.
DR   PIRSF; PIRSF001123; PepA_GA; 1.
DR   TIGRFAMs; TIGR03107; glu_aminopep; 1.
PE   1: Evidence at protein level;
KW   Aminopeptidase; Direct protein sequencing; Hydrolase; Metal-binding;
KW   Protease.
FT   CHAIN           1..355
FT                   /note="Glutamyl aminopeptidase"
FT                   /id="PRO_0000071653"
FT   ACT_SITE        213
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   BINDING         65
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         181
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         181
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         214
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
FT   BINDING         236
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250"
FT   BINDING         319
FT                   /ligand="a divalent metal cation"
FT                   /ligand_id="ChEBI:CHEBI:60240"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   355 AA;  38324 MW;  6D6A65BF5600A3EF CRC64;
     MELFDKVKAL TEIQATSGFE GPVRDYLKAR MVELGYQPEF DGLGGIFVTK ASKVENAPRI
     MVAAHMDEVG FMVSSIKADG TFRVVPLGGW NPLVVSGQRF TLFTRTGKKI PVVTGGLPPH
     LLRGTGVTPQ IPAISDIIFD GAFENAAEAA EFGIAQGDLI IPETETILSA NGKNIISKAW
     DNRYGCLMIL ELLEFLADKE LPVTLIIGAN VQEEVGLRGA KVSTTKFNPD LFFAVDCSPA
     SDTFGDDNGR LGEGTTLRFF DPGHIMLPGM KNFLLDTANH AKVKTQVYMA KGGTDAGAAH
     LANGGVPSTT IGVVARYIHS HQTIFNIDDF LQAQTFLRAI ITSLNTEKVA EIKNY