ID A0A430AGE9_9ENTE Unreviewed; 358 AA.
AC A0A430AGE9;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 11.
DE SubName: Full=Glutamyl aminopeptidase {ECO:0000313|EMBL:RSU06971.1};
GN ORFNames=CBF30_06840 {ECO:0000313|EMBL:RSU06971.1};
OS Vagococcus entomophilus.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae; Vagococcus.
OX NCBI_TaxID=1160095 {ECO:0000313|EMBL:RSU06971.1, ECO:0000313|Proteomes:UP000288669};
RN [1] {ECO:0000313|EMBL:RSU06971.1, ECO:0000313|Proteomes:UP000288669}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 24756 {ECO:0000313|EMBL:RSU06971.1,
RC ECO:0000313|Proteomes:UP000288669};
RA Gulvik C.A.;
RT "Vagococcus spp. assemblies.";
RL Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RSU06971.1}.
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DR EMBL; NGJZ01000002; RSU06971.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A430AGE9; -.
DR OrthoDB; 9772053at2; -.
DR Proteomes; UP000288669; Unassembled WGS sequence.
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:RSU06971.1}; 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:UP000288669}.
FT ACT_SITE 213
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT BINDING 67
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 321
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
SQ SEQUENCE 358 AA; 39594 MW; BC36DDB0A594695A CRC64;
MEEKLFQRIK TMTELQGTSG FEEDIRQVMT KELTPLVDRV EYDGLGGVFG IRENQVADAP
RVMVAAHMDE VGFMLTHIMD NGLFRVVPLG GWNPYVVSAQ RFTLKTRHAE YPVISSSIPP
HLLRGTSGQT SLNVADILFD AGFESKEEAE SYGVRPGDSI VPKVETIKTA NGKNIISKAW
DNRYGCTVVL EALEALKEVE LAHTLIAGAN VQEEVGLRGT RPSVHKFKPD LFFAVDCSAA
DDINGKKDTF GHLGEGFLLR IFDPGMITLK RMREFLLDTA ETNKIPYQYF VSKGGTDAGQ
AHLMNDGVPS AVIGVCARYI HTHQTMFNIT DYDAAKEMLI TVLKSLDKTT VNTIVYGK
//