ID U2YJ58_9SPHN Unreviewed; 734 AA.
AC U2YJ58;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=prolyl oligopeptidase {ECO:0000256|ARBA:ARBA00011897};
DE EC=3.4.21.26 {ECO:0000256|ARBA:ARBA00011897};
GN ORFNames=NT2_02_02940 {ECO:0000313|EMBL:GAD48212.1};
OS Caenibius tardaugens NBRC 16725.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Caenibius.
OX NCBI_TaxID=1219035 {ECO:0000313|EMBL:GAD48212.1, ECO:0000313|Proteomes:UP000016568};
RN [1] {ECO:0000313|EMBL:GAD48212.1, ECO:0000313|Proteomes:UP000016568}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 16725 {ECO:0000313|EMBL:GAD48212.1,
RC ECO:0000313|Proteomes:UP000016568};
RA Isaki S., Hosoyama A., Tsuchikane K., Katsumata H., Ando Y., Yamazaki S.,
RA Fujita N.;
RT "Whole genome shotgun sequence of Novosphingobium tardaugens NBRC 16725.";
RL Submitted (SEP-2013) to the EMBL/GenBank/DDBJ databases.
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:GAD48212.1}.
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DR EMBL; BASZ01000002; GAD48212.1; -; Genomic_DNA.
DR AlphaFoldDB; U2YJ58; -.
DR eggNOG; COG1505; Bacteria.
DR Proteomes; UP000016568; 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.
PE 3: Inferred from homology;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Reference proteome {ECO:0000313|Proteomes:UP000016568};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..24
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 25..734
FT /note="prolyl oligopeptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004636310"
FT DOMAIN 48..453
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 515..727
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 734 AA; 81111 MW; 542BCC1C0345BFA8 CRC64;
MRSLTRPVAG ALVLSLATVQ LAIAADMANP VSAGAAPVPA TNPAITYPQT RRDNVNDVLF
GETIADPYRW LENDVRNTPE VADWVARENV VTDAYLRTLP GRAWFSEKIG QLMNYERFSI
PVKAGGQYFY ERNEGLQNQP QLFVRKGLNG KPRLLLDPVQ WSKDGTSALD AWKPSPDGRY
VLYSVQEDGS DWRRLEVLDV RTGKRLSDTV RWAKFTSLAW VGEEGFLYSR FPEPEGGQDF
QALNYNQAVY FHRLGTDQSV DERVFATPDH KERSHTAEVT YDGRWAVITS AIGTDSKYEV
HAIDLAKRAQ KGWFARPLIT GFDNAWNLIE GTGGVLWFTT NEDAPRFRIV AIDLDAGAPR
WYEVVRQSPE TINAASLVGN RLVVSYLKDA ASRALIFELG GTRVDEIRLN GLGTANGFTG
KPGDPETFYS FASFNRPAGI YRMDLATGRM QPFALPKLTF DPDAYAVEQR FFTSKDGTNV
PMFVVRKRSV AEAGKAVPTM LYGYGGFDVS VTPGFSAVRM AWLEAGGAFA LANIRGGGEY
GKAWHDAGRL ANKQNVFDDF IAAGEYLKRE GITSPDGLAI EGRSNGGLLM GAVTNQRPDL
FNAVHAAVGV MDMLRFDRWT AGRYWVDDYG HPDRKEDFTI LRSYSPYHNI RAGVDYPAII
VTTADTDDRV VPGHSFKYAA ALQAAPIGNK PHLIRIETGA GHGSGKPTDK QIAEGADVLA
FLARWTGLDV RSEK
//