ID E7PHR9_PSESG Unreviewed; 323 AA.
AC E7PHR9;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 62.
DE RecName: Full=Proline iminopeptidase {ECO:0000256|ARBA:ARBA00021843, ECO:0000256|PIRNR:PIRNR006431};
DE Short=PIP {ECO:0000256|PIRNR:PIRNR006431};
DE EC=3.4.11.5 {ECO:0000256|ARBA:ARBA00012568, ECO:0000256|PIRNR:PIRNR006431};
DE AltName: Full=Prolyl aminopeptidase {ECO:0000256|PIRNR:PIRNR006431};
GN ORFNames=Pgy4_00510 {ECO:0000313|EMBL:EGH06166.1};
OS Pseudomonas savastanoi pv. glycinea str. race 4.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=875330 {ECO:0000313|EMBL:EGH06166.1, ECO:0000313|Proteomes:UP000005466};
RN [1] {ECO:0000313|EMBL:EGH06166.1, ECO:0000313|Proteomes:UP000005466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 4 {ECO:0000313|Proteomes:UP000005466};
RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132;
RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S.,
RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.;
RT "Dynamic evolution of pathogenicity revealed by sequencing and comparative
RT genomics of 19 Pseudomonas syringae isolates.";
RL PLoS Pathog. 7:E1002132-e1002132(2011).
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, ECO:0000256|RuleBase:RU003421};
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 ECO:0000256|RuleBase:RU003421}.
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:EGH06166.1}.
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DR EMBL; ADWY01000023; EGH06166.1; -; Genomic_DNA.
DR RefSeq; WP_004654190.1; NZ_AEGH01000039.1.
DR AlphaFoldDB; E7PHR9; -.
DR ESTHER; psesy-PIP; Proline_iminopeptidase.
DR MEROPS; S33.001; -.
DR PATRIC; fig|875330.5.peg.1053; -.
DR HOGENOM; CLU_043739_2_2_6; -.
DR BioCyc; PSYR875330:G11XH-92-MONOMER; -.
DR Proteomes; UP000005466; 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 NCBIfam; TIGR01249; pro_imino_pep_1; 1.
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; PR00111; ABHYDROLASE.
DR PRINTS; PR00793; PROAMNOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Aminopeptidase {ECO:0000256|PIRNR:PIRNR006431,
KW ECO:0000256|RuleBase:RU003421}; Cytoplasm {ECO:0000256|PIRNR:PIRNR006431};
KW Hydrolase {ECO:0000256|PIRNR:PIRNR006431, ECO:0000256|RuleBase:RU003421};
KW Protease {ECO:0000256|PIRNR:PIRNR006431, ECO:0000256|RuleBase:RU003421}.
FT DOMAIN 36..297
FT /note="AB hydrolase-1"
FT /evidence="ECO:0000259|Pfam:PF00561"
FT ACT_SITE 110
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
FT ACT_SITE 265
FT /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
FT ACT_SITE 293
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR006431-1"
SQ SEQUENCE 323 AA; 36564 MW; 2DB907AC648396D3 CRC64;
MQTLYPQIKP YARHDLAVEQ PHVLYVDESG SPEGLPVVFI HGGPGSGCDA HSRCYFDPNL
YRIVTFDQRG CGRSTPHASL ENNTTWKLVE DLERIREHLG IDKWVLFGGS WGSTLALAYA
QTHPDRVHAL ILRGIFLARQ QEIDWFYQAG ASRLFPDYWQ DYVAPIPLDE RDNILAAFHK
RLTGPDQIAQ MHAAKAWSTW EGRCATLRPN PQVVDRFAEP HRALSIARIE CHYFMNKAFL
EENQLIRDMP KIAHLPAIIV HGRYDVICPL DNAWELHQNW PGSELQVIRE AGHSASESGI
ADALVRAAAE IARNLLDLPP EEA
//
