PIP_LACDA
ID PIP_LACDA Reviewed; 295 AA.
AC Q1G8L9;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Proline iminopeptidase {ECO:0000312|EMBL:CAI98634.1};
DE Short=PIP {ECO:0000250|UniProtKB:P46544};
DE EC=3.4.11.5;
DE AltName: Full=Prolyl aminopeptidase {ECO:0000250|UniProtKB:P46544};
DE Short=PAP {ECO:0000250|UniProtKB:P46544};
GN Name=pepIP {ECO:0000312|EMBL:CAI98634.1}; OrderedLocusNames=Ldb1896;
OS Lactobacillus delbrueckii subsp. bulgaricus (strain ATCC 11842 / DSM 20081
OS / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB 11778 / NCTC 12712 / WDCM
OS 00102 / Lb 14).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=390333;
RN [1] {ECO:0000312|EMBL:CAI98634.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11842 / DSM 20081 / BCRC 10696 / JCM 1002 / NBRC 13953 / NCIMB
RC 11778 / NCTC 12712 / WDCM 00102 / Lb 14;
RX PubMed=16754859; DOI=10.1073/pnas.0603024103;
RA van de Guchte M., Penaud S., Grimaldi C., Barbe V., Bryson K., Nicolas P.,
RA Robert C., Oztas S., Mangenot S., Couloux A., Loux V., Dervyn R., Bossy R.,
RA Bolotin A., Batto J.-M., Walunas T., Gibrat J.-F., Bessieres P.,
RA Weissenbach J., Ehrlich S.D., Maguin E.;
RT "The complete genome sequence of Lactobacillus bulgaricus reveals extensive
RT and ongoing reductive evolution.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:9274-9279(2006).
CC -!- FUNCTION: Releases the N-terminal proline from various substrates.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Release of N-terminal proline from a peptide.; EC=3.4.11.5;
CC Evidence={ECO:0000250|UniProtKB:P46544};
CC -!- SUBCELLULAR LOCATION: Cell envelope {ECO:0000250|UniProtKB:P46544}.
CC -!- SIMILARITY: Belongs to the peptidase S33 family. {ECO:0000255}.
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DR EMBL; CR954253; CAI98634.1; -; Genomic_DNA.
DR AlphaFoldDB; Q1G8L9; -.
DR SMR; Q1G8L9; -.
DR STRING; 390333.Ldb1896; -.
DR ESTHER; lacdl-pip; Proline_iminopeptidase.
DR MEROPS; S33.021; -.
DR EnsemblBacteria; CAI98634; CAI98634; Ldb1896.
DR KEGG; ldb:Ldb1896; -.
DR eggNOG; COG2267; Bacteria.
DR HOGENOM; CLU_020336_15_0_9; -.
DR OMA; TWYRVTG; -.
DR Proteomes; UP000001259; Chromosome.
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; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR InterPro; IPR002410; Peptidase_S33.
DR InterPro; IPR005945; Pro_imino_pep.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF005539; Pept_S33_TRI_F1; 1.
DR PRINTS; PR00793; PROAMNOPTASE.
DR SUPFAM; SSF53474; SSF53474; 1.
DR TIGRFAMs; TIGR01250; pro_imino_pep_2; 1.
PE 3: Inferred from homology;
KW Aminopeptidase; Hydrolase; Protease; Reference proteome.
FT CHAIN 1..295
FT /note="Proline iminopeptidase"
FT /id="PRO_0000406324"
FT DOMAIN 29..279
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000255"
FT ACT_SITE 107
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P96084"
FT ACT_SITE 246
FT /evidence="ECO:0000250|UniProtKB:O32449"
FT ACT_SITE 273
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P96084"
SQ SEQUENCE 295 AA; 33027 MW; 97CF3AAD9FAFF900 CRC64;
MMQITEKYLP FGNWQTYCRI VGEATDRAPL LLLHGGPGSS HNYFEVLDQV AEKSGRQVIM
YDQLGCGNSS IPDDQAETAY TAQTWVKELE NVREQLGLDQ IHLLGQSWGG MLALIYLCDY
QPEGVKSLIL SSTLASAKLW SQELHRLIKY LPKGEQAAIK EAETTGNYDS LAYQAANAHF
MDQHAIKLTP DLPEPVLRKK KGGSLAYLTG WGPNEYTPIG NLHGYEYTDR LKDLHLPALI
TSGTDDLCTP LVAKSMYDNL PNARWELFAG CGHMPFVQEN AKYQELLSDW LISQD
