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Database: UniProt
Entry: Q9CIH3_LACLA
LinkDB: Q9CIH3_LACLA
Original site: Q9CIH3_LACLA 
ID   Q9CIH3_LACLA            Unreviewed;       355 AA.
AC   Q9CIH3;
DT   01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2001, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   SubName: Full=Glutamyl aminopeptidase {ECO:0000313|EMBL:AAK04485.1};
GN   Name=pepA {ECO:0000313|EMBL:AAK04485.1};
GN   ORFNames=L193909 {ECO:0000313|EMBL:AAK04485.1};
OS   Lactococcus lactis subsp. lactis (strain IL1403) (Streptococcus lactis).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus.
OX   NCBI_TaxID=272623 {ECO:0000313|EMBL:AAK04485.1, ECO:0000313|Proteomes:UP000002196};
RN   [1] {ECO:0000313|EMBL:AAK04485.1, ECO:0000313|Proteomes:UP000002196}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IL1403 {ECO:0000313|EMBL:AAK04485.1,
RC   ECO:0000313|Proteomes:UP000002196};
RX   PubMed=11337471; DOI=10.1101/gr.GR-1697R;
RA   Bolotin A., Wincker P., Mauger S., Jaillon O., Malarme K., Weissenbach J.,
RA   Ehrlich S.D., Sorokin A.;
RT   "The complete genome sequence of the lactic acid bacterium Lactococcus
RT   lactis ssp. lactis IL1403.";
RL   Genome Res. 11:731-753(2001).
CC   -!- COFACTOR:
CC       Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC         Evidence={ECO:0000256|PIRSR:PIRSR001123-2};
CC       Note=Binds 2 divalent metal cations per subunit.
CC       {ECO:0000256|PIRSR:PIRSR001123-2};
CC   -!- SIMILARITY: Belongs to the peptidase M42 family.
CC       {ECO:0000256|ARBA:ARBA00006272, ECO:0000256|PIRNR:PIRNR001123}.
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DR   EMBL; AE005176; AAK04485.1; -; Genomic_DNA.
DR   PIR; C86673; C86673.
DR   RefSeq; NP_266543.1; NC_002662.1.
DR   RefSeq; WP_010905311.1; NC_002662.1.
DR   AlphaFoldDB; Q9CIH3; -.
DR   MEROPS; M42.001; -.
DR   PaxDb; 272623-L193909; -.
DR   EnsemblBacteria; AAK04485; AAK04485; L193909.
DR   KEGG; lla:L193909; -.
DR   PATRIC; fig|272623.7.peg.421; -.
DR   eggNOG; COG1363; Bacteria.
DR   HOGENOM; CLU_047249_0_2_9; -.
DR   OrthoDB; 9772053at2; -.
DR   Proteomes; UP000002196; Chromosome.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   CDD; cd05656; M42_Frv; 1.
DR   Gene3D; 2.40.30.40; Peptidase M42, domain 2; 1.
DR   Gene3D; 3.40.630.10; Zn peptidases; 1.
DR   InterPro; IPR017538; Pept_M42_glutamyl_aminopept.
DR   InterPro; IPR008007; Peptidase_M42.
DR   InterPro; IPR023367; Peptidase_M42_dom2.
DR   NCBIfam; TIGR03107; glu_aminopep; 1.
DR   PANTHER; PTHR32481; AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR32481:SF0; AMINOPEPTIDASE YPDE-RELATED; 1.
DR   Pfam; PF05343; Peptidase_M42; 1.
DR   PIRSF; PIRSF001123; PepA_GA; 1.
DR   SUPFAM; SSF101821; Aminopeptidase/glucanase lid domain; 1.
DR   SUPFAM; SSF53187; Zn-dependent exopeptidases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW   ECO:0000313|EMBL:AAK04485.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR001123-2}; Protease {ECO:0000256|ARBA:ARBA00022670};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002196}.
FT   ACT_SITE        213
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT   BINDING         65
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         181
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         181
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         214
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         236
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT   BINDING         319
FT                   /ligand="Zn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29105"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ   SEQUENCE   355 AA;  38271 MW;  A922D5EB8ED177E5 CRC64;
     MELFDKVKAL TEIQATSGFE GSVRDYLKTR MIALGYQPEF DGLGGIFVTK TSKVANAPRI
     MIAAHMDEVG FMVSSIKADG TFRVVPLGGW NPLVVSGQRF TLFTRTGKKI PVVTGGLPPH
     LLRGTGVTPQ IPAISDIVFD GAFENAAEAT EFGIAQGDVI IPETETILSA NGKNIISKAW
     DNRYGCLMIL ELLGFLADKE LPATLIIGAN VQEEVGLRGA KVSTTMFKPD LFFAVDCSPA
     SDTFGDDNGR LGEGTTLRFF DPGHIMLPGM KNFLLETADK AKVKTQVYMA KGGTDAGAAH
     LANNGVPSTT IGVVARYIHS HQTIFNIDDF NQAQTFLRNI VTSLSTEKVA EIKNY
//
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