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Database: UniProt
Entry: R2VH90_9ENTE
LinkDB: R2VH90_9ENTE
Original site: R2VH90_9ENTE 
ID   R2VH90_9ENTE            Unreviewed;       357 AA.
AC   R2VH90;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Glutamyl aminopeptidase {ECO:0000313|EMBL:EOI57180.1};
GN   ORFNames=UKC_01394 {ECO:0000313|EMBL:EOI57180.1};
OS   Enterococcus gilvus ATCC BAA-350.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1158614 {ECO:0000313|EMBL:EOI57180.1, ECO:0000313|Proteomes:UP000013750};
RN   [1] {ECO:0000313|EMBL:EOI57180.1, ECO:0000313|Proteomes:UP000013750}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-350 {ECO:0000313|EMBL:EOI57180.1,
RC   ECO:0000313|Proteomes:UP000013750};
RG   The Broad Institute Genome Sequencing Platform;
RG   The Broad Institute Genome Sequencing Center for Infectious Disease;
RA   Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q.,
RA   Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA   Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Enterococcus gilvus ATCC BAA-350.";
RL   Submitted (FEB-2013) 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:EOI57180.1}.
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DR   EMBL; AJDQ01000006; EOI57180.1; -; Genomic_DNA.
DR   RefSeq; WP_010779813.1; NZ_KB946874.1.
DR   AlphaFoldDB; R2VH90; -.
DR   MEROPS; M42.001; -.
DR   PATRIC; fig|1158614.3.peg.1406; -.
DR   eggNOG; COG1363; Bacteria.
DR   HOGENOM; CLU_047249_0_2_9; -.
DR   OrthoDB; 9772053at2; -.
DR   Proteomes; UP000013750; 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:EOI57180.1}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR001123-2}; Protease {ECO:0000256|ARBA:ARBA00022670}.
FT   ACT_SITE        212
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR001123-1"
FT   BINDING         66
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   357 AA;  38844 MW;  1E4613C37550F131 CRC64;
     MEEKTFQRIK ELTELQGTSG FEEDIRSYMR DAITPLVDDV QQDGLGGIFG LRQADESKPR
     VMVAAHMDEV GFMLTEITPR GLFKVVPLGG WNPYVVSAQR FTLKTAKGNY PCISSSVPPH
     LLRGTSGQGQ VKVEDILFDA GFESKDEALA YGVLPGDTIV PQTETVKTAN GKNIISKAWD
     NRYGCTVVLE ALEALQKETL DYTLIAGANV QEEVGLRGAK PAVTKFQPDL FFAVDCSAAD
     DLVTSNGTFG HLGEGTLLRI QDPGMILLPR LREYLLDTAE THNIPYQYFV SKGGTDAGAA
     HTANEGIPST VIGVCGRYIH THQTMFSIAD FDAAREMLIH VLKGLDESTI KTIVAGN
//
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