ID A0A347WNP3_9LACT Unreviewed; 355 AA.
AC A0A347WNP3;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Glutamyl aminopeptidase {ECO:0000313|EMBL:AXY26700.1};
GN ORFNames=CL176_03195 {ECO:0000313|EMBL:AXY26700.1};
OS Suicoccus acidiformans.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Suicoccus.
OX NCBI_TaxID=2036206 {ECO:0000313|EMBL:AXY26700.1, ECO:0000313|Proteomes:UP000263232};
RN [1] {ECO:0000313|EMBL:AXY26700.1, ECO:0000313|Proteomes:UP000263232}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ZY16052 {ECO:0000313|EMBL:AXY26700.1,
RC ECO:0000313|Proteomes:UP000263232};
RA Li F.;
RT "Complete genome sequence of Oxytococcus suis strain ZY16052.";
RL Submitted (SEP-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}.
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DR EMBL; CP023434; AXY26700.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A347WNP3; -.
DR KEGG; abae:CL176_03195; -.
DR OrthoDB; 9772053at2; -.
DR Proteomes; UP000263232; 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; IPR008007; Peptidase_M42.
DR InterPro; IPR023367; Peptidase_M42_dom2.
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:AXY26700.1}; 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:UP000263232}.
FT ACT_SITE 212
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 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 180
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 213
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 235
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001123-2"
FT BINDING 320
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; 38488 MW; 4A47352648E4D0EC CRC64;
MNESTFKHLM ALTELQSISG HESSVRQYMQ EAMSAYVDEC EVSGLGNLFG IKRAKQADAP
TVMLAGHMDE VGFMLSRIED NGTFRAVPIG GWNVYAVPAQ RFTLQTQQGD IPVISSAVPP
HLMKQNASKP IQVKDIYFDA GFESKEEAEG YGVRPGDPIV PEASTVVSAN GKSLISKAID
NRYGCALVLD VLEALKDVDL PFHLVAGATV QEEVGLRGVK GAVHRYAPDI FFAVDASPAG
DGEGDKTAQG QLGQGFLLRV QDPGHISHPP LWHYIQAQAE NAGIPYQYYF SQGGTDAGAA
HVMNDGVPSA VIGLPARYIH GHQSLMRLRD YEAARDIVLQ VFENLQPEII QEIKG
//
