ID   A0A3M7LFX3_9FLAO        Unreviewed;       683 AA.
AC   A0A3M7LFX3;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   SubName: Full=S9 family peptidase {ECO:0000313|EMBL:RMZ60970.1};
GN   ORFNames=D1632_03080 {ECO:0000313|EMBL:RMZ60970.1};
OS   Chryseobacterium nematophagum.
OC   Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC   Chryseobacterium group; Chryseobacterium.
OX   NCBI_TaxID=2305228 {ECO:0000313|EMBL:RMZ60970.1, ECO:0000313|Proteomes:UP000267524};
RN   [1] {ECO:0000313|EMBL:RMZ60970.1, ECO:0000313|Proteomes:UP000267524}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JUb275 {ECO:0000313|EMBL:RMZ60970.1,
RC   ECO:0000313|Proteomes:UP000267524};
RA   Page A., Roberts M., Felix M.-A., Weir W.;
RT   "Chryseobacterium nematophagum: a novel matrix digesting pathogen of
RT   nematodes.";
RL   Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
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:RMZ60970.1}.
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DR   EMBL; QWIV01000005; RMZ60970.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M7LFX3; -.
DR   Proteomes; UP000267524; 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; PTHR11757:SF19; PROLYL ENDOPEPTIDASE-LIKE; 1.
DR   PANTHER; PTHR11757; PROTEASE FAMILY S9A OLIGOPEPTIDASE; 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}.
FT   DOMAIN          4..403
FT                   /note="Peptidase S9A N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02897"
FT   DOMAIN          464..677
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
SQ   SEQUENCE   683 AA;  79750 MW;  807A051BB6E2A9C6 CRC64;
     MKAPQAKKIQ KTLEIHHNKR VDNYFWLNER ENPEVIEYLN EENAYADFVM KDTEDLQELL
     FEEMKSRYKK DDESLPYFFN EYWYMVRYEE GKEYPIFCRK YKSLHHHEEI VLDVNILAEG
     KTFFETGSIA VSPNNQLVSF SSDSVGRRIY SIYFKNLKTG EILQDEIPNT TGKAVWANDN
     EHIFYIRKDD SLRAFQVYRH KLGTPSSEDI LIFHEKDETF DVNVFKTKSL QYIFIASSSS
     ISDEHWFIPS DNVFADWAVI QPRIEDLEYS VEHYKDEFYI ITNAHEATNF KIVKTKIAKC
     GMENWIDVIP HRPEVLLEGF EIFKEFLVLE EREKGLLQIK IIDEKNNQYH YLPFSDPTYT
     SYIGINLEFD TEVLRYGYTS LTQPSSTYEY NMREKTTKLL KQQEVLGGKF FPENYISERI
     WANSRDGKSK IPISLVYHKD TKKNKDTPLL LYGYGSYGHT VDASFSNVRL SILDRGFIYA
     IAHIRGGEYL GREWYEEGKM LFKKNTFFDF IDAGKHLIKE NYTSSKHLYA MGGSAGGLLV
     GAAINYEPNL FNGVVAQVPF VDVVTTMLDE TIPLTTGEYD EWGNPNNEEY YHYIKEYSPY
     DNVEAKAYPN ILITAGLHDS QVQYWEPAKW TAKLRELKTD DNILIFKTDM SAGHGGASGR
     FESLKEEALE FAFLLKLEKE KND
//