ID C2M1L8_CAPGI Unreviewed; 717 AA.
AC C2M1L8;
DT 16-JUN-2009, integrated into UniProtKB/TrEMBL.
DT 16-JUN-2009, sequence version 1.
DT 24-JAN-2024, entry version 53.
DE RecName: Full=prolyl oligopeptidase {ECO:0000256|ARBA:ARBA00011897};
DE EC=3.4.21.26 {ECO:0000256|ARBA:ARBA00011897};
GN ORFNames=CAPGI0001_1756 {ECO:0000313|EMBL:EEK15776.1};
OS Capnocytophaga gingivalis.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=553178 {ECO:0000313|EMBL:EEK15776.1, ECO:0000313|Proteomes:UP000003622};
RN [1] {ECO:0000313|EMBL:EEK15776.1, ECO:0000313|Proteomes:UP000003622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33624 / DSM 3290 / CIP 102945 / JCM 12953 / NCTC 12372 /
RC 27 {ECO:0000313|Proteomes:UP000003622};
RA Sebastian Y., Madupu R., Durkin A.S., Torralba M., Methe B., Sutton G.G.,
RA Strausberg R.L., Nelson K.E.;
RL Submitted (APR-2009) 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:EEK15776.1}.
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DR EMBL; ACLQ01000001; EEK15776.1; -; Genomic_DNA.
DR RefSeq; WP_002665395.1; NZ_ACLQ01000001.1.
DR AlphaFoldDB; C2M1L8; -.
DR STRING; 553178.CAPGI0001_1756; -.
DR eggNOG; COG1505; Bacteria.
DR Proteomes; UP000003622; 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, ECO:0000313|EMBL:EEK15776.1}.
FT DOMAIN 37..435
FT /note="Peptidase S9A N-terminal"
FT /evidence="ECO:0000259|Pfam:PF02897"
FT DOMAIN 499..709
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 717 AA; 81277 MW; 2306E2A1D9CAB424 CRC64;
MRQFFIPLSC VLVLSACHDK VQKEENTQEA WEQITYPETK KENVEDTYFG EKVIDPYRWL
EDDQSAETEA WVKAQNAVTF GYLHSIPFRD KIKAQAEKLW NHEQLTAPFR VGEYTYYYKN
NGLQNQDVLY RKGKDGKEEL FLDPNGFASD GTTSLAEVNF SKDGSLVCYL ISEGGSDWRK
AIVMNTQTRE QVGDTIVNIK YSGGYWYKNE GFYYCSYDKP KGSELSEKTD QNKLYYHKLG
TPQSSDALIF GGKPEEKNRF VGGYVSNDEN YLIIRGEETT SGGKLWIKDL RKPNSPLVNI
LNDYSSDTFV LAIKGEKIYF QTNLNAPNGK IVVADLKDPT PTHWKDLIPE TENVITPVVA
GKYILAHYMK DAISEVKQYD FEGKFIREIK LPALGTVTLE SAKEEENESY FSFENFYTPS
SIYKLHLEKG DTELYWAPKM DFNPNDFESK QVFYTSKDGT KVPMIITYKK GTPLDGTAPA
TLYGYGGFNI SYTPWFAVTY AIWMNNGGVF AVANIRGGGE YGKKWHDAGT KFQKQNVFDD
FIGACEYLID NKYTSKEKLA IKGGSNGGLL IGAVMTQRPD LIRVALPYVG VMDMLRYHKF
TSGAGWAYDY GTSDDSKEMF EYLKGYSPVH NVKEGTCYPA TLIFTGDHDD RVVPAHSFKF
AAQLQSKQSC KNPVFIRIET NAGHGAGTPV SKIIDQTADW QAFALWNMGY KKLPNEK
//
