ID A0A117KGJ0_9FLAO Unreviewed; 803 AA.
AC A0A117KGJ0;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-2016, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Aminoacyl peptidase {ECO:0000313|EMBL:KUJ63794.1};
GN ORFNames=AR687_01005 {ECO:0000313|EMBL:KUJ63794.1};
OS Flavobacteriaceae bacterium CRH.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae.
OX NCBI_TaxID=1742859 {ECO:0000313|EMBL:KUJ63794.1, ECO:0000313|Proteomes:UP000053826};
RN [1] {ECO:0000313|EMBL:KUJ63794.1, ECO:0000313|Proteomes:UP000053826}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRH {ECO:0000313|EMBL:KUJ63794.1,
RC ECO:0000313|Proteomes:UP000053826};
RA Newman J.D., Miller J.R., Jacobs K.T.;
RT "Genome Sequence of Flavobacterium sp. CHR.";
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KUJ63794.1}.
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DR EMBL; LMAJ01000001; KUJ63794.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A117KGJ0; -.
DR STRING; 1742859.AR687_01005; -.
DR OrthoDB; 6388416at2; -.
DR Proteomes; UP000053826; Unassembled WGS sequence.
DR GO; GO:0008236; F:serine-type peptidase activity; IEA:InterPro.
DR GO; GO:0006508; P:proteolysis; IEA:InterPro.
DR Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR Gene3D; 2.120.10.30; TolB, C-terminal domain; 1.
DR InterPro; IPR011042; 6-blade_b-propeller_TolB-like.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR PANTHER; PTHR42776:SF28; GLUTAMYL ENDOPEPTIDASE, CHLOROPLASTIC-RELATED; 1.
DR PANTHER; PTHR42776; SERINE PEPTIDASE S9 FAMILY MEMBER; 1.
DR Pfam; PF00326; Peptidase_S9; 1.
DR SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
DR SUPFAM; SSF82171; DPP6 N-terminal domain-like; 1.
PE 4: Predicted;
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..803
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007150406"
FT DOMAIN 648..802
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
FT REGION 192..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 197..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 803 AA; 91073 MW; A75125C62EA93F04 CRC64;
MKLKVTLLLF LNIGFIAFAQ ESLTYQKPSK SILDLADYER APTVSMDTKK EYLLLAYRST
YKTLDDLNQE ELRLGGLRIN PVTNISSTVT YINNLKVRKI NGKDEIQVSG LPANPKISNI
LWSPNDKKIL FSHTTASGVQ LWILDVASAK ANKLTEATVN ANLGNPFSWF LDNETILVKM
LPKNRQPLLD SKKDLPTGPI ISNTSGTKSQ NRTYPDMLKN QNDEINFENI ITSELYKVNI
NGTATLFKDA AMYAGERISP DGNYVLLTTI QKPFSYVVPL NRFPSKTIVY DSRGKEIKVV
NEVPLNEVIP KGFMAVRKGK REMAWRNDKP ATLSYVVALD EGDPANKVDF RDEVFLWDAP
FTNNATTLVK TPQRYSGILW GNENIAFLTD EWYDTRNTKT YLINPSNPSQ QAKVITDRNQ
QDVYSDPGNF ETKKNEYNKN VLAIENDNAF RIGDGYTKEG QFPFIDEFNL KTLKTKRVYT
STYKDKKEDL LEIEDFKTGK VLVQIQSKSE FPNYYFRNIK KQNSLTPITA FKNPFESIKD
VSKEVIKYKR KDGVELSGTL YLPAGYDKVK KEKLPLLIWA YPAEYKDKNS AGQSTQNSNE
FTFPYYGSFV YWVTKGYVVL DDAAFPIIGE GTTEPNDNFI SQLVDNAEAA INAVDALGYI
NRKKVAVGGH SYGAFMTANL LTHSNLFACG IARSGAYNRT LTPFGFQTEQ RNYWEVPEVY
NTMSPFMNAD KMKTPILLVH GEADNNPGTF TLQTERYFQA LKGLGAPARM VILPKEAHGY
VAKENILHLL WEQDQFLEKY LKN
//