ID U1JJU5_9GAMM Unreviewed; 719 AA.
AC U1JJU5;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=prolyl oligopeptidase {ECO:0000256|ARBA:ARBA00011897};
DE EC=3.4.21.26 {ECO:0000256|ARBA:ARBA00011897};
GN ORFNames=PMAN_14064 {ECO:0000313|EMBL:ERG25413.1};
OS Pseudoalteromonas marina DSM 17587.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Pseudoalteromonadaceae; Pseudoalteromonas.
OX NCBI_TaxID=1117316 {ECO:0000313|EMBL:ERG25413.1, ECO:0000313|Proteomes:UP000016528};
RN [1] {ECO:0000313|EMBL:ERG25413.1, ECO:0000313|Proteomes:UP000016528}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17587 {ECO:0000313|Proteomes:UP000016528};
RX PubMed=22535931; DOI=10.1128/JB.00265-12;
RA Xie B.B., Shu Y.L., Qin Q.L., Rong J.C., Zhang X.Y., Chen X.L., Shi M.,
RA He H.L., Zhou B.C., Zhang Y.Z.;
RT "Genome sequences of type strains of seven species of the marine bacterium
RT Pseudoalteromonas.";
RL J. Bacteriol. 194:2746-2747(2012).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of Pro-|-Xaa >> Ala-|-Xaa in oligopeptides.;
CC EC=3.4.21.26; Evidence={ECO:0000256|ARBA:ARBA00001070};
CC -!- SIMILARITY: Belongs to the peptidase S9A family.
CC {ECO:0000256|ARBA:ARBA00005228}.
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:ERG25413.1}.
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DR EMBL; AHCB02000040; ERG25413.1; -; Genomic_DNA.
DR AlphaFoldDB; U1JJU5; -.
DR Proteomes; UP000016528; Unassembled WGS sequence.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.130.10.120; Prolyl oligopeptidase, N-terminal domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR002471; Pept_S9_AS.
DR InterPro; IPR023302; Pept_S9A_N.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002470; Peptidase_S9A.
DR PANTHER; PTHR42881; PROLYL ENDOPEPTIDASE; 1.
DR PANTHER; PTHR42881:SF2; PROLYL ENDOPEPTIDASE; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR Pfam; PF02897; Peptidase_S9_N; 1.
DR PRINTS; PR00862; PROLIGOPTASE.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF50993; Peptidase/esterase 'gauge' domain; 1.
DR PROSITE; PS00708; PRO_ENDOPEP_SER; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..719
FT /note="prolyl oligopeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004613232"
FT DOMAIN 43..443
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 500..715
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 719 AA; 79573 MW; 326B041FDE9ED04F CRC64;
MLLKRTLACA VLLALSGCSE PTNTSDQKEV KSSMNQVNSV VYPETKKGDV VDTYFGENVA
DPYRWLEDDM SAETADWVKA QNTATFSYLE QIPYRNKLKE RLEKLMNYEK IGAPFEEGGY
TYFYKNDGLQ NQYVLYRSKG DKAPEVFLDP NKFSDDGTTS MSGLSFSKDG SLLAYQVSEG
GSDWREIIVI DTHTKEQVEQ ALVDVKFSGI DWLGNEGFYY SSYDKPKGSE LSAKTDQHKV
YYHALGTSQD DDRVVFGDSE AQKHRYVGAD VTDDGKYLLI SASVSTSGNK LFIKDLSKEN
SDFVTVVGNS DSDTSVIDND GEKLYLVTNL NAPNKKVVTV NANNPAPENW VDFISETDNV
LSLSKGGDTF FANYMVDAIS HVKQYNKQGE LIREINLPGV GSARGFRGKK DQSTLYYSFT
NYKTPGTTFS FDVSSGESKV YRESAIDFNS NDYTSEQVFY TSKDGTKVPM IITYKTGIKL
DGSNPTILYG YGGFNASLTP SFSPINALWL EQGGVYAVAN IRGGGEYGKD WHNAGTKMQK
QNVFDDFIAA AEYLKDKKYT SKKRLALRGG SNGGLLVGAV MTQRPDLFQV ALPAVGVLDM
LRYHTFTAGA GWAYDYGTSE QSKEMFEYIK AYSPLHNVKA GVEYPATMVT TGDHDDRVVP
SHSFKFAAEL QAKQAGNNPT LIRIETNAGH GAGTPTSKVI DLYADMFGFT LYNMGVKEL
//
