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Database: UniProt
Entry: J9A029_ENTFC
LinkDB: J9A029_ENTFC
Original site: J9A029_ENTFC 
ID   J9A029_ENTFC            Unreviewed;       354 AA.
AC   J9A029;
DT   31-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   31-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   SubName: Full=Putative Xaa-Pro dipeptidase {ECO:0000313|EMBL:EJV55710.1};
GN   ORFNames=HMPREF1345_00691 {ECO:0000313|EMBL:EJV55710.1};
OS   Enterococcus faecium TX1337RF.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC   Enterococcus.
OX   NCBI_TaxID=1134802 {ECO:0000313|EMBL:EJV55710.1, ECO:0000313|Proteomes:UP000003117};
RN   [1] {ECO:0000313|EMBL:EJV55710.1, ECO:0000313|Proteomes:UP000003117}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TX1337RF {ECO:0000313|EMBL:EJV55710.1,
RC   ECO:0000313|Proteomes:UP000003117};
RA   Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA   Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA   Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA   Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA   Mardis E.R., Wilson R.K.;
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase M24B family.
CC       {ECO:0000256|RuleBase:RU000590}.
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:EJV55710.1}.
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DR   EMBL; AMAA01000031; EJV55710.1; -; Genomic_DNA.
DR   RefSeq; WP_002310265.1; NZ_JH804714.1.
DR   AlphaFoldDB; J9A029; -.
DR   PATRIC; fig|1134802.3.peg.645; -.
DR   HOGENOM; CLU_017266_4_0_9; -.
DR   Proteomes; UP000003117; Unassembled WGS sequence.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   CDD; cd01092; APP-like; 1.
DR   Gene3D; 3.90.230.10; Creatinase/methionine aminopeptidase superfamily; 1.
DR   Gene3D; 3.40.350.10; Creatinase/prolidase N-terminal domain; 1.
DR   InterPro; IPR029149; Creatin/AminoP/Spt16_NTD.
DR   InterPro; IPR036005; Creatinase/aminopeptidase-like.
DR   InterPro; IPR000587; Creatinase_N.
DR   InterPro; IPR000994; Pept_M24.
DR   InterPro; IPR001131; Peptidase_M24B_aminopep-P_CS.
DR   PANTHER; PTHR46112; AMINOPEPTIDASE; 1.
DR   PANTHER; PTHR46112:SF3; AMINOPEPTIDASE YPDF; 1.
DR   Pfam; PF01321; Creatinase_N; 1.
DR   Pfam; PF00557; Peptidase_M24; 1.
DR   SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR   SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
DR   PROSITE; PS00491; PROLINE_PEPTIDASE; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|RuleBase:RU000590}.
FT   DOMAIN          4..128
FT                   /note="Creatinase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01321"
FT   DOMAIN          136..338
FT                   /note="Peptidase M24"
FT                   /evidence="ECO:0000259|Pfam:PF00557"
SQ   SEQUENCE   354 AA;  39182 MW;  F04A16FEDCF5C171 CRC64;
     MMLRVEKLRK KMQEENLDSF LVTSPYNLRY LTNFTGTTGL AVITLEKAFF ITDFRYTEQA
     AAQAQGFEII KNVGPIFDEV ANLVRKEELH SLAFEETTVS FLEYSVLEEI IDAELVPVSQ
     MIEELREVKD EEEIAIIEKA CNIADMAYDH ILKMIQPGMT EIEVANQLDF YMRSLGASGV
     SFDTIVASGL RSAMPHGVAS KKLIEQGDLI TLDFGCYYEG YVSDMTRTFA IGDPGEKLKE
     IYQVVLDAQL AVIDAAKPGV TGVQLDAVAR DYISKHGYGE AFGHSTGHGI GLEIHEGPNV
     SSRAEKQFVP GNVITDEPGI YLPGIGGVRI EDDLLITEDG NRVLTRSPKE LIIL
//
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