ID Q48570_LACHE Unreviewed; 304 AA.
AC Q48570;
DT 01-NOV-1996, integrated into UniProtKB/TrEMBL.
DT 01-NOV-1996, sequence version 1.
DT 27-MAR-2024, entry version 100.
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=DM470_09040 {ECO:0000313|EMBL:PXZ12629.1}, IMAU30003_01596
GN {ECO:0000313|EMBL:NRO35346.1}, Lh22155_09030
GN {ECO:0000313|EMBL:AUI76797.1};
OS Lactobacillus helveticus (Lactobacillus suntoryeus).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=1587 {ECO:0000313|EMBL:CAA83195.1};
RN [1] {ECO:0000313|EMBL:CAA83195.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=53/7 {ECO:0000313|EMBL:CAA83195.1};
RX PubMed=8936308;
RA Varmanen P., Steele J., Palva A.;
RT "Characterization of a prolinase gene and its product and an adjacent ABC
RT transporter gene from Lactobacillus helveticus.";
RL Microbiology 142:809-816(1996).
RN [2] {ECO:0000313|Proteomes:UP000234533}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FAM22155 {ECO:0000313|Proteomes:UP000234533};
RA Ahrens C., Schmid M.;
RT "Genome sequence of Lactobacillus helveticus FAM22155.";
RL Submitted (MAY-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AUI76797.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=FAM22155 {ECO:0000313|EMBL:AUI76797.1};
RX PubMed=29441050;
RA Schmid M., Muri J., Melidis D., Varadarajan A.R., Somerville V., Wicki A.,
RA Moser A., Bourqui M., Wenzel C., Eugster-Meier E., Frey J.E., Irmler S.,
RA Ahrens C.H.;
RT "Comparative Genomics of Completely Sequenced Lactobacillus helveticus
RT Genomes Provides Insights into Strain-Specific Genes and Resolves
RT Metagenomics Data Down to the Strain Level.";
RL Front. Microbiol. 9:63-63(2018).
RN [4] {ECO:0000313|EMBL:PXZ12629.1, ECO:0000313|Proteomes:UP000247635}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FAM19188 {ECO:0000313|EMBL:PXZ12629.1,
RC ECO:0000313|Proteomes:UP000247635};
RA Moser A.I., Irmler S., Wuethrich D., Bruggmann R., Eugster-Meier E.,
RA Berthoud H.;
RT "Cell lysis in Lactobacillus helveticus.";
RL Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN [5] {ECO:0000313|EMBL:NRO35346.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=IMAU30003 {ECO:0000313|EMBL:NRO35346.1};
RA Zhang H., Chen Y., Zhong Z.;
RT "Comparative genomic analysis of Lactobacillus helveticus.";
RL Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; CP015498; AUI76797.1; -; Genomic_DNA.
DR EMBL; Z30709; CAA83195.1; -; Genomic_DNA.
DR EMBL; WCHB01000057; NRO35346.1; -; Genomic_DNA.
DR EMBL; QJOO01000081; PXZ12629.1; -; Genomic_DNA.
DR PIR; B59088; B59088.
DR RefSeq; WP_012212214.1; NZ_WCHB01000057.1.
DR ESTHER; lache-prolinase; Proline_iminopeptidase.
DR MEROPS; S33.004; -.
DR OMA; TWYRVTG; -.
DR Proteomes; UP000234533; Chromosome.
DR Proteomes; UP000247635; Unassembled WGS sequence.
DR Proteomes; UP000651333; 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};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR005539, ECO:0000313|EMBL:PXZ12629.1};
KW Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PIRNR:PIRNR005539}.
FT DOMAIN 27..282
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 304 AA; 35041 MW; 956B35C3621555ED CRC64;
MKTGTKIITL DNGYHLWTNT QGEGDIHLLA LHGGPGGNHE YWEDTAEQLK KQGLNVQVTM
YDQLGSLYSD QPDYSDPEIA KKYLTYEYFL DEVDEVREKL GLDNFYLIGQ SWGGLLVQEY
AVKYGQHLKG AIISSMVDEI DEYVASVNRR RQEVLPQTEI DFMHECEKNN DYDNQRYQDD
VQILNINFVD RKQPSKLYHL KNIGGSAVYH AFQGDNEFVI TGKLKDWHFR DQLKNIKVPT
LLTFGENETM PISTAKIMQK EIPNSRLVTT PDGGHHHMVD NPDVYYKHLA DFIREVENGT
FKGE
//
