ID R2PTD8_9ENTE Unreviewed; 354 AA.
AC R2PTD8;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Xaa-Pro dipeptidase {ECO:0000313|EMBL:EOH87847.1};
GN ORFNames=UAU_04702 {ECO:0000313|EMBL:EOH87847.1};
OS Enterococcus pallens ATCC BAA-351.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1158607 {ECO:0000313|EMBL:EOH87847.1, ECO:0000313|Proteomes:UP000013782};
RN [1] {ECO:0000313|EMBL:EOH87847.1, ECO:0000313|Proteomes:UP000013782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-351 {ECO:0000313|EMBL:EOH87847.1,
RC ECO:0000313|Proteomes:UP000013782};
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 pallens BAA-351.";
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:EOH87847.1}.
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DR EMBL; AJAQ01000046; EOH87847.1; -; Genomic_DNA.
DR RefSeq; WP_010759637.1; NZ_KB946311.1.
DR AlphaFoldDB; R2PTD8; -.
DR STRING; 160454.RV10_GL000137; -.
DR PATRIC; fig|1158607.3.peg.4686; -.
DR eggNOG; COG0006; Bacteria.
DR HOGENOM; CLU_017266_4_0_9; -.
DR OrthoDB; 9806388at2; -.
DR Proteomes; UP000013782; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000013782}.
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; 38224 MW; 2905FE1D51414283 CRC64;
MLERINKLRA LMKKEVLDGY LIMSPENLRY LTNFTGSAGV AMITPVSAYF ITDFRYVEQA
ADQVSGMTII QHQGAIGEVV ADLVEKDQLS ALGFEDDFLT FADYSVYEEI IQAEFAPAGG
LIEKLREQKD ESEIAIIEKA CSIADAGFEH VLKMIRPGMT EIEIANQLDF FMRSLGATGT
SFDTIVASGV RSALPHGVAS QKTIEKGEMI TLDFGCIYQG YVSDITRTFA IGDPGQQLKD
VYAIVLEAQL QVLSQAQAGV TGAQLDASAR SVITDAGYGD AFGHSTGHGI GLAIHEGPNL
SWTNDEPLQA GNIVTNEPGI YIGGLGGVRI EDDLVILENG NRVLTHSPKD LIIL
//
