ID R2Y5D8_9ENTE Unreviewed; 354 AA.
AC R2Y5D8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE SubName: Full=Xaa-Pro dipeptidase {ECO:0000313|EMBL:EOI57577.1};
GN ORFNames=UKC_01797 {ECO:0000313|EMBL:EOI57577.1};
OS Enterococcus gilvus ATCC BAA-350.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1158614 {ECO:0000313|EMBL:EOI57577.1, ECO:0000313|Proteomes:UP000013750};
RN [1] {ECO:0000313|EMBL:EOI57577.1, ECO:0000313|Proteomes:UP000013750}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-350 {ECO:0000313|EMBL:EOI57577.1,
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 -!- 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:EOI57577.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AJDQ01000006; EOI57577.1; -; Genomic_DNA.
DR RefSeq; WP_010780205.1; NZ_KB946874.1.
DR AlphaFoldDB; R2Y5D8; -.
DR PATRIC; fig|1158614.3.peg.1808; -.
DR eggNOG; COG0006; Bacteria.
DR HOGENOM; CLU_017266_4_0_9; -.
DR OrthoDB; 9806388at2; -.
DR Proteomes; UP000013750; 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..127
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 136..336
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
SQ SEQUENCE 354 AA; 38512 MW; CB27319930BD01FC CRC64;
MIKRIEKLRE LMKNDGIDAY LVTSPANLRY LTNFTGTAGL AFITLKEAFF ITDFRYTEQA
SEQVQGMTIL QHQGDIVGEV IKLMEREGIR VLGFEDAFVT YAEYSVFEEV IDAELAPASG
LTERLREQKD EGEIAIIEKA CAIADEGFDH VLKMIRPGMT EIELANQLDF FMRSLGASGT
SFETIVASGL RSALPHGVAS EKVIEQGDMI TLDFGCVYQG YVSDITRTFA IGDPGQSLKD
IYQIVLNAQL KVIEAAQPGV TGAQLDAVAR TFISEAGYGD AFGHSTGHGI GMEIHEGPTV
SRSNEEALAV GNVITDEPGI YIPGLGGVRI EDDLVIVADG NRLLTHSPKE LIIL
//
