ID A0ZA31_NODSP Unreviewed; 684 AA.
AC A0ZA31;
DT 23-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 23-JAN-2007, sequence version 1.
DT 24-JAN-2024, entry version 65.
DE RecName: Full=prolyl oligopeptidase {ECO:0000256|ARBA:ARBA00011897};
DE EC=3.4.21.26 {ECO:0000256|ARBA:ARBA00011897};
GN ORFNames=NSP_4320 {ECO:0000313|EMBL:AHJ26782.1};
OS Nodularia spumigena CCY9414.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Aphanizomenonaceae;
OC Nodularia.
OX NCBI_TaxID=313624 {ECO:0000313|EMBL:AHJ26782.1, ECO:0000313|Proteomes:UP000019325};
RN [1] {ECO:0000313|EMBL:AHJ26782.1, ECO:0000313|Proteomes:UP000019325}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCY9414 {ECO:0000313|EMBL:AHJ26782.1};
RX PubMed=23555932;
RA Voss B., Bolhuis H., Fewer D.P., Kopf M., Moke F., Haas F., El-Shehawy R.,
RA Hayes P., Bergman B., Sivonen K., Dittmann E., Scanlan D.J., Hagemann M.,
RA Stal L.J., Hess W.R.;
RT "Insights into the physiology and ecology of the brackish-water-adapted
RT Cyanobacterium Nodularia spumigena CCY9414 based on a genome-transcriptome
RT analysis.";
RL PLoS ONE 8:E60224-E60224(2013).
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; CP007203; AHJ26782.1; -; Genomic_DNA.
DR RefSeq; WP_006194263.1; NZ_CP007203.1.
DR AlphaFoldDB; A0ZA31; -.
DR GeneID; 78015580; -.
DR PATRIC; fig|313624.11.peg.432; -.
DR eggNOG; COG1505; Bacteria.
DR HOGENOM; CLU_011290_1_1_3; -.
DR Proteomes; UP000019325; 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:AHJ26782.1}.
FT DOMAIN 6..408
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 465..678
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 684 AA; 77310 MW; FBF1CCDC4ECDC87A CRC64;
MSYPISNKSD QVDNYHGTLV ADPYRWLEDP DSAETRNWIS AENQITFAYL NEIPAREKIK
QRLTKLWDYE KYGIPFKEGN NYFYFKNNGL QNQSVLYTLK TLDAEPKVLI DPNKLSTDGT
IALSGLAISE NGKLLAYGLS TSGSDWQEWK VRDVETGEDL EDHLKWIKFS GASWTKDNQG
FFYSRYDEPN EKTKLEDVNY YQKLYYHQLG TPQSEDVLIY HRDDQKEWGF SGNVTEDGSY
LIISVWLGTD AKNLVFYKDL TNPDAEVVEL INQFEADYSF IEHDEHIFYL RTDLNAPRGR
LIAIDTKNPA QENWQEIIPQ SVATLESANI LNNQFVVDFL QDARTQIKIF DLNGALVREV
ELPGLGSAGG FGGKRDDTET FYSFTSFTTP GTIYRYNMVT GKSELFRQSQ VDFNPDDYET
KQIFYSSKDG TQVPMFITHK KGMQLDGNNP TYLYAYGGFN VSMTPSFSVS TLVWMEMGGV
YAMPNIRGGG EYGEEWHQAG MKEKKQNVFD DFIAAAEWLI DNNYTRHARL AIAGGSNGGL
LVGACMTQRP ELFGAALPAV GVMDMLRFHK FTIGWAWVPE YGSPDKPEEF PALYSYSPLH
NLKPGTAYPA TLITTADHDD RVVPAHSFKF AATLQANHAG DAPVLIRIET KAGHGAGKPT
AKIIEEAADK WAFLVQTLEV IRNS
//
