ID A0A1H1DMT8_9BACI Unreviewed; 297 AA.
AC A0A1H1DMT8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 14.
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=SAMN05216231_2488 {ECO:0000313|EMBL:SDQ77713.1};
OS Virgibacillus salinus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Virgibacillus.
OX NCBI_TaxID=553311 {ECO:0000313|EMBL:SDQ77713.1, ECO:0000313|Proteomes:UP000199444};
RN [1] {ECO:0000313|EMBL:SDQ77713.1, ECO:0000313|Proteomes:UP000199444}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.10449 {ECO:0000313|EMBL:SDQ77713.1,
RC ECO:0000313|Proteomes:UP000199444};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088, ECO:0000256|PIRNR:PIRNR005539}.
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DR EMBL; FNKD01000003; SDQ77713.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H1DMT8; -.
DR STRING; 553311.SAMN05216231_2488; -.
DR Proteomes; UP000199444; Unassembled WGS sequence.
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 PANTHER; PTHR43798; MONOACYLGLYCEROL LIPASE; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF005539; Pept_S33_TRI_F1; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR PRINTS; PR00793; PROAMNOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|PIRNR:PIRNR005539};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR005539, ECO:0000313|EMBL:SDQ77713.1};
KW Protease {ECO:0000256|PIRNR:PIRNR005539};
KW Reference proteome {ECO:0000313|Proteomes:UP000199444}.
FT DOMAIN 39..280
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 113
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 297 AA; 33879 MW; 6B4248069E183F8F CRC64;
MKNEALNSIE RTQGFIGSEN CKTYYEVHTP RHPNSELTPI ILLAGGPGLS CKTLTPLLNV
AETRPVIAYD QIGSGKSTRS EQFTSLDIKD FIKQFNNVVT ELNLSRFHIL GHSWGTILGV
NIALQYPENT RSLILHSGIA DWKKCLEARL NFEEEYFPKE LKRVLKKYND GVKVSSDEME
EAINKYNSLF YCRAEYPKYL SEALNGKDFE TNQLIWNPVK KKEMASYNIC DRLNEIKCPT
LIMSGKYDGI SVGQAELFNT GIKNSRHVEF INSAHYSHIE QEMEFITQVK GFLKGFV
//
