ID L1PQI9_9FLAO Unreviewed; 734 AA.
AC L1PQI9;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Peptidase, S9A/B/C family, catalytic domain protein {ECO:0000313|EMBL:EKY17866.1};
GN ORFNames=HMPREF9073_01349 {ECO:0000313|EMBL:EKY17866.1};
OS Capnocytophaga sp. oral taxon 326 str. F0382.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Capnocytophaga.
OX NCBI_TaxID=1035193 {ECO:0000313|EMBL:EKY17866.1, ECO:0000313|Proteomes:UP000010441};
RN [1] {ECO:0000313|EMBL:EKY17866.1, ECO:0000313|Proteomes:UP000010441}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0382 {ECO:0000313|EMBL:EKY17866.1,
RC ECO:0000313|Proteomes:UP000010441};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (MAY-2012) 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:EKY17866.1}.
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DR EMBL; AMEU01000097; EKY17866.1; -; Genomic_DNA.
DR AlphaFoldDB; L1PQI9; -.
DR STRING; 1035193.HMPREF9073_01349; -.
DR PATRIC; fig|1035193.3.peg.1245; -.
DR eggNOG; COG0823; Bacteria.
DR eggNOG; COG1506; Bacteria.
DR HOGENOM; CLU_006105_2_0_10; -.
DR OrthoDB; 9812921at2; -.
DR Proteomes; UP000010441; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 15..35
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 110..448
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 538..734
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 734 AA; 84858 MW; E1721A2A11D0B12B CRC64;
MTKYTLHKNL YGRKALYFCA LLLICYLLPA TYYLLPAQTL QEIWTKGTFY PERMFNLKAL
QHTPQYTVLE YNREKRAQEI NLYDFATLTK VQTLFQANDR VSRIEGYDFS ADEKKLLIAT
RKEDIYRHSF IADYFLYDLT TGDLKKVSDK RIQVPTFSPN GKQLAFVYEN NLYLYDLATG
EETQITTDGQ KNAIINGTAD WVYEEEFGIV KLFAWNADGS QLAFIRSDER KVPEFSMDIY
GYDLYPTPYT FKYPKAGEAN SAVSLHIYTV ANQSVAEIPL NAYYIPRLQW TNDPHKLTVQ
TLNRHQNDWQ LLQVNSQTKA TTSLVKETSA TYVSINKDIL FLPDNSFIYQ SEKDGHNHFY
YCNAKGKLVR QLTRGNWEVT DCYGYDPKTQ QLFYQSTQIG STRRGLYAVS LKGKAPRALS
TEAGTNKGTF SGDYTMYIHA FANATTPPRY TLNDTKNGKQ LKEIISNAEY TQRLKAYNLP
EKEFMELKTA KGTFNAYMLK PKDFDPKKQY PLLMYQYSGP GSQEVADQWW DMNDFWHAML
TQKGYIVLCV DGRGTGYKGT DFKKCTYQQL GKYEVEDQAD VAQLVGDYPY IDKSRIGIWG
WSFGGFMSSN CLFQKGDIFK MAIAVAPVTN WRFYDTIYTE RFMRTPQENA KGYDENSPLF
HAAKLKGKYL LIHGSADDNV HVQNAMVLIE TLVSLQKDFD WLIYPDKNHG IYDNTGSTRF
QLYTKMTNFI EQNL
//