ID A0A0Q5DWH3_9MICO Unreviewed; 318 AA.
AC A0A0Q5DWH3;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=Proline iminopeptidase {ECO:0000256|PIRNR:PIRNR006431};
DE Short=PIP {ECO:0000256|PIRNR:PIRNR006431};
DE EC=3.4.11.5 {ECO:0000256|PIRNR:PIRNR006431};
DE AltName: Full=Prolyl aminopeptidase {ECO:0000256|PIRNR:PIRNR006431};
GN ORFNames=ASF68_16245 {ECO:0000313|EMBL:KQQ49446.1};
OS Plantibacter sp. Leaf314.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Plantibacter.
OX NCBI_TaxID=1736333 {ECO:0000313|EMBL:KQQ49446.1, ECO:0000313|Proteomes:UP000051200};
RN [1] {ECO:0000313|EMBL:KQQ49446.1, ECO:0000313|Proteomes:UP000051200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf314 {ECO:0000313|EMBL:KQQ49446.1,
RC ECO:0000313|Proteomes:UP000051200};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQQ49446.1, ECO:0000313|Proteomes:UP000051200}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf314 {ECO:0000313|EMBL:KQQ49446.1,
RC ECO:0000313|Proteomes:UP000051200};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
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:PIRNR006431};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|PIRNR:PIRNR006431}.
CC -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088, ECO:0000256|PIRNR:PIRNR006431}.
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:KQQ49446.1}.
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DR EMBL; LMOB01000003; KQQ49446.1; -; Genomic_DNA.
DR RefSeq; WP_056013622.1; NZ_LMOB01000003.1.
DR AlphaFoldDB; A0A0Q5DWH3; -.
DR STRING; 1736333.ASF68_16245; -.
DR OrthoDB; 9796770at2; -.
DR Proteomes; UP000051200; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-UniRule.
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; IPR005944; Pro_iminopeptidase.
DR PANTHER; PTHR43722; PROLINE IMINOPEPTIDASE; 1.
DR PANTHER; PTHR43722:SF1; PROLINE IMINOPEPTIDASE; 1.
DR Pfam; PF00561; Abhydrolase_1; 1.
DR PIRSF; PIRSF006431; Pept_S33; 1.
DR PRINTS; PR00793; PROAMNOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|PIRNR:PIRNR006431};
KW Cytoplasm {ECO:0000256|PIRNR:PIRNR006431};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR006431};
KW Protease {ECO:0000256|PIRNR:PIRNR006431};
KW Reference proteome {ECO:0000313|Proteomes:UP000051200}.
FT DOMAIN 38..300
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 114
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
FT ACT_SITE 269
FT /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
FT ACT_SITE 297
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
SQ SEQUENCE 318 AA; 34984 MW; E56F815934A9FDE7 CRC64;
MTDEHAGPYA TGFVEVEGGA SIFWEESGVP DGVPALWLHG GPGGSLGSGW YRSHFDLSRY
RLIGIDQRGS GKSVPNILDA RDRLDEHTTQ RLIADIEQVR VAMGVERWVV AGVSWGTTLA
LAYAQEHPDH VIALGLVAVT TTSREEVDWI TEGVGRVFPE EWARFERDSR RRDGERVVEA
YARRLREGDA AERTAAAAAW DRWESAHVSL DSPERVGQLF ADARTREAFA TLVTHFWSRD
GFLTGEQAVL ARMGRIADIP GALVHGRRDI SGPAVTAWRL HQLWSASELT IVEAEGHGGA
EESAVLRAAL DRFKTLAP
//
