ID B4R875_PHEZH Unreviewed; 378 AA.
AC B4R875;
DT 23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT 23-SEP-2008, sequence version 1.
DT 27-MAR-2024, entry version 60.
DE RecName: Full=Proline iminopeptidase {ECO:0000256|ARBA:ARBA00021843};
DE EC=3.4.11.5 {ECO:0000256|ARBA:ARBA00012568};
DE AltName: Full=Prolyl aminopeptidase {ECO:0000256|ARBA:ARBA00029605};
GN OrderedLocusNames=PHZ_c2784 {ECO:0000313|EMBL:ACG79193.1};
OS Phenylobacterium zucineum (strain HLK1).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Phenylobacterium.
OX NCBI_TaxID=450851 {ECO:0000313|EMBL:ACG79193.1, ECO:0000313|Proteomes:UP000001868};
RN [1] {ECO:0000313|EMBL:ACG79193.1, ECO:0000313|Proteomes:UP000001868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLK1 {ECO:0000313|EMBL:ACG79193.1,
RC ECO:0000313|Proteomes:UP000001868};
RX PubMed=18700039; DOI=10.1186/1471-2164-9-386;
RA Luo Y., Xu X., Ding Z., Liu Z., Zhang B., Yan Z., Sun J., Hu S., Hu X.;
RT "Complete genome of Phenylobacterium zucineum - a novel facultative
RT intracellular bacterium isolated from human erythroleukemia cell line
RT K562.";
RL BMC Genomics 9:386-386(2008).
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 -!- SIMILARITY: Belongs to the peptidase S33 family.
CC {ECO:0000256|ARBA:ARBA00010088}.
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DR EMBL; CP000747; ACG79193.1; -; Genomic_DNA.
DR RefSeq; WP_012523331.1; NC_011144.1.
DR AlphaFoldDB; B4R875; -.
DR STRING; 450851.PHZ_c2784; -.
DR ESTHER; phezh-b4r875; Proline_iminopeptidase.
DR KEGG; pzu:PHZ_c2784; -.
DR eggNOG; COG2267; Bacteria.
DR HOGENOM; CLU_049285_1_1_5; -.
DR OrthoDB; 9796770at2; -.
DR Proteomes; UP000001868; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:InterPro.
DR GO; GO:0004177; F:aminopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR022742; Hydrolase_4.
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; PF12146; Hydrolase_4; 1.
DR PRINTS; PR00793; PROAMNOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000313|EMBL:ACG79193.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001868};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..21
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 22..378
FT /note="Proline iminopeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002825116"
FT DOMAIN 102..347
FT /note="Serine aminopeptidase S33"
FT /evidence="ECO:0000259|Pfam:PF12146"
SQ SEQUENCE 378 AA; 41865 MW; DA919BD9FF437905 CRC64;
MRPTALALGL LAALAALPAS AQSEPKPFSR DDARAIIRDA RKIVSPQGIE ELRAVEINGL
PQWISVRGRD RRNPILLFIH GGPASTEMPV SWLYQSPWED FFTVVQWDQR AAGKTAVGAD
HAAVGPTVTV EQMTADGEAM VAHLRERYGK EKVFVLGHSW GSVIGLNLAR RRPEWLHAYV
GMGQIVDWNA NEAAGYDFAL RMARADGNAQ AVRELEALAP YPPAEGVLSF EQVVTQRKWV
IHYGGLTMGR SDFAYDLNAR KISPDYTDRD LSPGVPDGDA LIRLLPGMTA LDFAQVNRVE
TPVFLFLGRR DYQTPSKVAA DWHARLQAPQ KGLFWFERSA HMMHLEQPGK VLMHLVNDIR
PIAERAGDVA PPDRPGVD
//
