ID V7HYF4_9LACO Unreviewed; 306 AA.
AC V7HYF4;
DT 19-FEB-2014, integrated into UniProtKB/TrEMBL.
DT 19-FEB-2014, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE RecName: Full=Proline iminopeptidase {ECO:0000256|ARBA:ARBA00021843, ECO:0000256|PIRNR:PIRNR005539};
DE Short=PIP {ECO:0000256|PIRNR:PIRNR005539};
DE EC=3.4.11.5 {ECO:0000256|ARBA:ARBA00012568, ECO:0000256|PIRNR:PIRNR005539};
DE AltName: Full=Prolyl aminopeptidase {ECO:0000256|ARBA:ARBA00029605, ECO:0000256|PIRNR:PIRNR005539};
GN ORFNames=LEQ_0497 {ECO:0000313|EMBL:ETA74253.1};
OS Ligilactobacillus equi DPC 6820.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Ligilactobacillus.
OX NCBI_TaxID=1392007 {ECO:0000313|EMBL:ETA74253.1, ECO:0000313|Proteomes:UP000018559};
RN [1] {ECO:0000313|EMBL:ETA74253.1, ECO:0000313|Proteomes:UP000018559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DPC 6820 {ECO:0000313|EMBL:ETA74253.1,
RC ECO:0000313|Proteomes:UP000018559};
RX PubMed=24435863;
RA O'Donnell M.M., Harris H.M., O'Toole P.W., Ross R.P.;
RT "The Genome of the Predominant Equine Lactobacillus Species, Lactobacillus
RT equi, Is Reflective of Its Lifestyle Adaptations to an Herbivorous Host.";
RL Genome Announc. 2:e01155-e01113(2014).
CC -!- FUNCTION: Releases the N-terminal proline from various substrates.
CC {ECO:0000256|PIRNR:PIRNR005539}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001585,
CC ECO:0000256|PIRNR:PIRNR005539};
CC -!- SUBCELLULAR LOCATION: Cell envelope {ECO:0000256|ARBA:ARBA00004196}.
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088, ECO:0000256|PIRNR:PIRNR005539}.
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:ETA74253.1}.
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DR EMBL; AWWH01000106; ETA74253.1; -; Genomic_DNA.
DR RefSeq; WP_023859513.1; NZ_AWWH01000106.1.
DR AlphaFoldDB; V7HYF4; -.
DR PATRIC; fig|1392007.3.peg.930; -.
DR Proteomes; UP000018559; Unassembled WGS sequence.
DR GO; GO:0031975; C:envelope; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR002410; Peptidase_S33.
DR InterPro; IPR005945; Pro_imino_pep.
DR NCBIfam; TIGR01250; pro_imino_pep_2; 1.
DR PANTHER; PTHR43798; MONOACYLGLYCEROL LIPASE; 1.
DR PANTHER; PTHR43798:SF33; SERINE HYDROLASE-LIKE PROTEIN DDB_G0286239; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF005539; Pept_S33_TRI_F1; 1.
DR PRINTS; PR00793; PROAMNOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|ARBA:ARBA00022438,
KW ECO:0000256|PIRNR:PIRNR005539}; Hydrolase {ECO:0000256|PIRNR:PIRNR005539};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR005539};
KW Reference proteome {ECO:0000313|Proteomes:UP000018559}.
FT DOMAIN 27..281
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 111
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR005539-1"
FT ACT_SITE 248
FT /evidence="ECO:0000256|PIRSR:PIRSR005539-1"
FT ACT_SITE 275
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR005539-1"
SQ SEQUENCE 306 AA; 35302 MW; 92D6C97F9C25EBA9 CRC64;
MKQGTTIITL DNGYHLWTNT QGQGTVHLLA LHGGPGGNHE YWEDTADQLK KQGLDVQVHM
YDQLGSLYSD QPDYDNPAIA EKYLTYDYFL DEVEEVRQKL GLDNFYLIGQ SWGGALVQMY
AHKYGDHLKG AIISSMVDEI DEYVANINRL REETLPKEAV DFMLECEEKN DYANPKYQEY
VQIMNENFID RKQPSKLYHL KDLGGTKVYN TFQGDNEFVI KGKLDQWHFR DKLKDITTPT
LLTFGEHESM PIKTAHTMNR LLPNSRLVTT PNGGHHHMID NAEVYYKHLA DFIKDVEAGT
FQNEEE
//