ID A0A433N5N6_CHLFR Unreviewed; 690 AA.
AC A0A433N5N6;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 24-JAN-2024, entry version 13.
DE RecName: Full=prolyl oligopeptidase {ECO:0000256|ARBA:ARBA00011897};
DE EC=3.4.21.26 {ECO:0000256|ARBA:ARBA00011897};
GN ORFNames=PCC6912_41360 {ECO:0000313|EMBL:RUR76732.1};
OS Chlorogloeopsis fritschii PCC 6912.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Nostocales; Chlorogloeopsidaceae;
OC Chlorogloeopsis.
OX NCBI_TaxID=211165 {ECO:0000313|EMBL:RUR76732.1, ECO:0000313|Proteomes:UP000268857};
RN [1] {ECO:0000313|EMBL:RUR76732.1, ECO:0000313|Proteomes:UP000268857}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6912 {ECO:0000313|EMBL:RUR76732.1,
RC ECO:0000313|Proteomes:UP000268857};
RX PubMed=30590650;
RA Will S.E., Henke P., Boedeker C., Huang S., Brinkmann H., Rohde M.,
RA Jarek M., Friedl T., Seufert S., Schumacher M., Overmann J.,
RA Neumann-Schaal M., Petersen J.;
RT "Day and night: Metabolic profiles and evolutionary relationships of six
RT axenic non-marine cyanobacteria.";
RL Genome Biol. Evol. 0:0-0(2018).
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:RUR76732.1}.
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DR EMBL; RSCJ01000019; RUR76732.1; -; Genomic_DNA.
DR RefSeq; WP_016876373.1; NZ_RSCJ01000019.1.
DR AlphaFoldDB; A0A433N5N6; -.
DR STRING; 211165.GCA_000317285_02640; -.
DR OrthoDB; 9801421at2; -.
DR Proteomes; UP000268857; 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:UP000268857}.
FT DOMAIN 10..414
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 472..685
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 690 AA; 77618 MW; 651B133EACEF97A1 CRC64;
MPAAKPLTYP STRKSNQIDS YHGAPVADPY RWLEDPDSEE TKAWVEAQNK VTFGYLEEIP
AREKIKQRLT KLWDYEKYSV PFKEGERYFY FKNDGLQNQS VLYTLKSLNE EPTVLLDPNT
LSEDGTVALA GLAISEDGKL LAYGLSTAGS DWQEWKVRDI ETCQDLEDHL KWIKFSGASW
TNDRKGFFYS RYDEPNEKSK LADVNYYQKL YYHRLGTPQS EDILIYHRPD EKEWGFDGSV
TEDGQYLIIS VWLGTDPKNL VFYKDLTNPN SEVIELINKF EANYGFIDND GNVFYFRTDL
DAPRGRLIAI DTQKPALENR QEIIPQAAET LESVGIINNQ FVADYLKDAH SQIKIFNLNG
EFVREVELPG IGSAGGFGGK RYDTETFYSF TSFTTPATIY RYDMVSGKSE IFRQPNVDFN
PADYETKQIF YNSKDGTQVP MFITHKKGIK LDGNNPTYLY GYGGFNASLT PAFSVSNLVW
MEMGGVYAVP NIRGGGEYGE EWHQAGMKLK KQNVFDDFIA AAEWLIANGY TKPAKLAIGG
GSNGGLLVGA CMTQRPDLFA AALPAVGVMD MLRFPKFTIG WAWVSEYGSP ENPEEFKALY
AYSPLHNLKP GTAYPATLIT TADHDDRVVP AHSFKFAAAL QAAHAGDVPV LIRIETKAGH
GAGKPTTKMI EEVADKWAFL VRTLDMEVES
//
