ID Q2JRS3_SYNJA Unreviewed; 683 AA.
AC Q2JRS3;
DT 07-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 07-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE RecName: Full=prolyl oligopeptidase {ECO:0000256|ARBA:ARBA00011897};
DE EC=3.4.21.26 {ECO:0000256|ARBA:ARBA00011897};
GN OrderedLocusNames=CYA_2555 {ECO:0000313|EMBL:ABD00673.1};
OS Synechococcus sp. (strain JA-3-3Ab) (Cyanobacteria bacterium Yellowstone
OS A-Prime).
OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Synechococcaceae;
OC Synechococcus.
OX NCBI_TaxID=321327 {ECO:0000313|EMBL:ABD00673.1, ECO:0000313|Proteomes:UP000008818};
RN [1] {ECO:0000313|EMBL:ABD00673.1, ECO:0000313|Proteomes:UP000008818}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA-3-3Ab {ECO:0000313|EMBL:ABD00673.1,
RC ECO:0000313|Proteomes:UP000008818};
RX PubMed=18059494; DOI=10.1038/ismej.2007.46;
RA Bhaya D., Grossman A.R., Steunou A.S., Khuri N., Cohan F.M., Hamamura N.,
RA Melendrez M.C., Bateson M.M., Ward D.M., Heidelberg J.F.;
RT "Population level functional diversity in a microbial community revealed by
RT comparative genomic and metagenomic analyses.";
RL ISME J. 1:703-713(2007).
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}.
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DR EMBL; CP000239; ABD00673.1; -; Genomic_DNA.
DR RefSeq; WP_011431346.1; NC_007775.1.
DR AlphaFoldDB; Q2JRS3; -.
DR ESTHER; synja-q2jrs3; S9N_PPCE_Peptidase_S9.
DR KEGG; cya:CYA_2555; -.
DR eggNOG; COG1505; Bacteria.
DR HOGENOM; CLU_011290_1_1_3; -.
DR OrthoDB; 9801421at2; -.
DR Proteomes; UP000008818; Chromosome.
DR GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:ABD00673.1}.
FT DOMAIN 5..408
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 466..679
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 683 AA; 76817 MW; 9AD13F452802E83B CRC64;
MLNYPPSHPD PTVVDFYHGQ AVPDPYRWLE DLDSEQTRAW IEAQNRLTFD YLQRIPARQR
LLERLRQLWN YEKYSQPFKE GNRYFYFKND GLQNQSVLYT QESLEGEARV LLDPNTLSED
GTVALSGIAI SRDGRYLAYG LSRSGSDWQE WKVRDIETGE DLPDHLRWIK FSGASWTLDG
QGFFYSRYDE PAPGSEYESA NYFQKLYYHR LGTPQSEDLL VYHRPDQKEW GFAGGVTEDG
DYLIISVWRG TDPKNLLFYK DLRDPSSPVV ELIREFQAEY AFVGNDGSRF WLLTDLQAPR
RRLVAIDLDN PGQLQEVIPE AEETLQGVSL IHNQFVAFYL KDAHTQIRTF ALDGTYLGEI
PLPGLGSASG FGGKRHDTET FYTFTSFTTP PTIYRYDFTS GRSTLFRQPQ VDFDPQAYEV
QQVFYASQDG TRIPMFLVHR RGLARTGDHP TLLYGYGGFG ISLTPSFSVG LVAWLEMGGV
YAQPSLRGGG EYGEAWHQAG TKLNKQKVFD DFIAAAEWLM ANGYTNPSKL AIAGGSNGGL
LVGACLTQRP DLFAAALPAV GVFDMLRFHK FTIGWAWISE YGSPEDPEEF KALYAYSPLH
NLKPGTAYPA TLITTADHDD RVVPAHSFKF AAALQAAQGG SQPILIRIDT KAGHGAGKPT
AKLIEETADR WAFLVQVLGI QAG
//
