ID A0A0R1W780_9LACO Unreviewed; 365 AA.
AC A0A0R1W780;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=Xaa-Pro dipeptidase {ECO:0000313|EMBL:KRM13437.1};
GN ORFNames=FD16_GL000004 {ECO:0000313|EMBL:KRM13437.1};
OS Paucilactobacillus suebicus DSM 5007 = KCTC 3549.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Paucilactobacillus.
OX NCBI_TaxID=1423807 {ECO:0000313|EMBL:KRM13437.1, ECO:0000313|Proteomes:UP000051820};
RN [1] {ECO:0000313|EMBL:KRM13437.1, ECO:0000313|Proteomes:UP000051820}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 5007 {ECO:0000313|EMBL:KRM13437.1,
RC ECO:0000313|Proteomes:UP000051820};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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:KRM13437.1}.
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DR EMBL; AZGF01000001; KRM13437.1; -; Genomic_DNA.
DR RefSeq; WP_010622758.1; NZ_BACO01000063.1.
DR AlphaFoldDB; A0A0R1W780; -.
DR STRING; 1423807.FD16_GL000004; -.
DR PATRIC; fig|1423807.3.peg.4; -.
DR eggNOG; COG0006; Bacteria.
DR OrthoDB; 9806388at2; -.
DR Proteomes; UP000051820; Unassembled WGS sequence.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProt.
DR GO; GO:0008235; F:metalloexopeptidase activity; IEA:UniProt.
DR GO; GO:0046914; F:transition metal ion binding; IEA:UniProt.
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; IPR001714; Pept_M24_MAP.
DR PANTHER; PTHR46112; AMINOPEPTIDASE; 1.
DR PANTHER; PTHR46112:SF10; DIPEPTIDASE YKVY-RELATED; 1.
DR Pfam; PF01321; Creatinase_N; 1.
DR Pfam; PF00557; Peptidase_M24; 1.
DR PRINTS; PR00599; MAPEPTIDASE.
DR SUPFAM; SSF55920; Creatinase/aminopeptidase; 1.
DR SUPFAM; SSF53092; Creatinase/prolidase N-terminal domain; 1.
PE 4: Predicted;
FT DOMAIN 4..138
FT /note="Creatinase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01321"
FT DOMAIN 146..348
FT /note="Peptidase M24"
FT /evidence="ECO:0000259|Pfam:PF00557"
SQ SEQUENCE 365 AA; 40449 MW; EC04F3A5BE5664B0 CRC64;
MTQLEKVQQT VADLNLDVAY LSDPMTINYL TGFGSDPIER VLALLVFPDH DPFIFAPALE
VEAIKDTGWK YPVYGYLDHE KPFDIITTQI KKRNPNPKNW GIEQSQLTVD RLHSLTDQFP
KADFSRDLTP NIQQLRLIKT EDEIKKLDEA GKWADFAFKV GFEAVKVGQS EQQIAATLEY
ALKQHGIMQM SFETLVQAGA HAAEPHGATS VNKVNGDELV LFDLGTVYEG YISDASRTIA
VGKLNEKQQD IYNVCLEAQL TAQAAAKPGI TAAQLDKVAR DIIDKAGYGE YFIHRLGHGM
GMSEHEFPSI MEGNDLVLEP GMCFSIEPGI YIPGVAGVRI EDCVHITDNG CLPFTHTSKD
LTFIG
//
