ID T2NA45_PORGN Unreviewed; 723 AA.
AC T2NA45;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 27.
DE SubName: Full=Peptidase, S9A/B/C family, catalytic domain protein {ECO:0000313|EMBL:EOA11390.1};
DE EC=3.4.-.- {ECO:0000313|EMBL:EOA11390.1};
GN ORFNames=A343_0979 {ECO:0000313|EMBL:EOA11390.1};
OS Porphyromonas gingivalis JCVI SC001.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Porphyromonadaceae;
OC Porphyromonas.
OX NCBI_TaxID=1195243 {ECO:0000313|EMBL:EOA11390.1};
RN [1] {ECO:0000313|EMBL:EOA11390.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCVI SC001 {ECO:0000313|EMBL:EOA11390.1};
RX PubMed=23564253; DOI=10.1101/gr.150433.112;
RA McLean J.S., Lombardo M.J., Ziegler M.G., Novotny M., Yee-Greenbaum J.,
RA Badger J.H., Tesler G., Nurk S., Lesin V., Brami D., Hall A.P., Edlund A.,
RA Allen L.Z., Durkin S., Reed S., Torriani F., Nealson K.H., Pevzner P.A.,
RA Friedman R., Venter J.C., Lasken R.S.;
RT "Genome of the pathogen Porphyromonas gingivalis recovered from a biofilm
RT in a hospital sink using a high-throughput single-cell genomics platform.";
RL Genome Res. 23:867-877(2013).
RN [2] {ECO:0000313|EMBL:EOA11390.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=JCVI SC001 {ECO:0000313|EMBL:EOA11390.1};
RA McLean J., Yee-Greenbaum J., Durkin A.S., Lasken R.;
RL Submitted (MAR-2013) 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:EOA11390.1}.
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DR EMBL; APMB01000062; EOA11390.1; -; Genomic_DNA.
DR AlphaFoldDB; T2NA45; -.
DR MEROPS; S09.013; -.
DR PATRIC; fig|1195243.10.peg.1755; -.
DR HOGENOM; CLU_006105_2_0_10; -.
DR Proteomes; UP000016542; Chromosome.
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; 2.140.10.30; Dipeptidylpeptidase IV, N-terminal domain; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR001375; Peptidase_S9.
DR InterPro; IPR002469; Peptidase_S9B_N.
DR PANTHER; PTHR11731:SF193; DIPEPTIDYL PEPTIDASE 9; 1.
DR PANTHER; PTHR11731; PROTEASE FAMILY S9B,C DIPEPTIDYL-PEPTIDASE IV-RELATED; 1.
DR Pfam; PF00930; DPPIV_N; 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:0000313|EMBL:EOA11390.1}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..723
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004592315"
FT DOMAIN 98..440
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 524..722
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 723 AA; 81952 MW; 3D7CC3D799EC32EC CRC64;
MKRPVIILLL GIVTMCAMAQ TGNKPVDLKE ITSGMFYARS AGSGIRSMPD GEHYTEMNRE
RTAIIRYNYA SGKAVDTLFS VERARECPFK QIQNYEVSST GHHILLFTDM ESIYRHSYRA
AVYDYDVRRN LVKPLSEHVG KVMIPTFSPD GRMVAFVRDN NIFIKKFDFD TEVQVTTDGQ
INSILNGATD WVYEEEFGVT NLMSWSADNA FLAFVRSDES AVPEYRMPMY EDKLYPEDYT
YKYPKAGEKN STVSLHLYNV ADRNTKSVSL PIDADGYIPR IAFTDNADEL AVMTLNRLQN
DFKMYYVHPK SLVPKLILQD MNKRYVDSDW IQALKFTTGG GFAYVSEKDG FAHIYLYDNK
GVMHRRITSG NWDVTKLYGV DASGTVFYQS AEESPIRRAV YAIDAKGRKT KLSLNVGTND
ALFSGNYAYY INTYSSAATP TVVSVFRSKG AKELRTLEDN VALRERLKAY RYNPKEFTII
KTQSGLELNA WIVKPIDFDP SRHYPVLMVQ YSGPNSQQVL DRYSFDWEHY LASKGYVVAC
VDGRGTGARG EEWRKCTYMQ LGVFESDDQI AAATAIGQLP YVDAARIGIW GWSYGGYTTL
MSLCRGNGTF KAGIAVAPVA DWRFYDSVYT ERFMRTPKEN ASGYKMSSAL DVASQLQGNL
LIVSGSADDN VHLQNTMLFT EALVQANIPF DMAIYMDKNH SIYGGNTRYH LYTRKAKFLF
DNL
//
