ID G5GA54_9BACT Unreviewed; 732 AA.
AC G5GA54;
DT 25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT 25-JAN-2012, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE RecName: Full=S9 family peptidase {ECO:0008006|Google:ProtNLM};
GN ORFNames=HMPREF9332_00455 {ECO:0000313|EMBL:EHG24254.1};
OS Alloprevotella rava F0323.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Alloprevotella.
OX NCBI_TaxID=679199 {ECO:0000313|EMBL:EHG24254.1, ECO:0000313|Proteomes:UP000015993};
RN [1] {ECO:0000313|EMBL:EHG24254.1, ECO:0000313|Proteomes:UP000015993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0323 {ECO:0000313|EMBL:EHG24254.1,
RC ECO:0000313|Proteomes:UP000015993};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Izard J., Blanton J.M.,
RA Baranova O.V., Tanner A.C., Dewhirst F.E., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
RA Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C., Freedman E.,
RA Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.,
RA Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A., Murphy C.,
RA Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T., Shenoy N.,
RA Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Prevotella sp. oral taxon 302 str. F0323.";
RL Submitted (AUG-2011) 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:EHG24254.1}.
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DR EMBL; ACZK01000010; EHG24254.1; -; Genomic_DNA.
DR RefSeq; WP_009346866.1; NZ_JH376827.1.
DR AlphaFoldDB; G5GA54; -.
DR STRING; 679199.HMPREF9332_00455; -.
DR MEROPS; S09.013; -.
DR PATRIC; fig|679199.3.peg.474; -.
DR eggNOG; COG0823; Bacteria.
DR eggNOG; COG1506; Bacteria.
DR HOGENOM; CLU_006105_2_0_10; -.
DR OrthoDB; 9812921at2; -.
DR Proteomes; UP000015993; 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; 2.140.10.30; 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 Reference proteome {ECO:0000313|Proteomes:UP000015993};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..732
FT /note="S9 family peptidase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003476982"
FT DOMAIN 97..448
FT /note="Dipeptidylpeptidase IV N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00930"
FT DOMAIN 540..731
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 732 AA; 83532 MW; 0ABC031FB153D658 CRC64;
MNKLLVLATC AVLSVGNLAA QSEPLNLKDI TSGRYYAHRI YGVRPANDGN SYTQLSEDSR
RIIRRSFKNG EEIGTLFNAS TARGPIKLEH IDGYIMSPDE SRILLQTKTK SIYRRSFTAE
YYIFDVKNNR FTHLSEGGPQ QVPVFSPDGT MIAFARENNL FLVKLLFDNA ESQITKDGKF
NEVLNGIPDW VNEEEFSTNC SFTFSADSKM LAWIRYDESK VPIYSIQEFK GSHPTLKQYD
EYPGTYDYKY PVAGAKNSEV SVKTFDIKNR VTRTMAVPVD SDGYIPRIQF TSDPDRLAVV
TLNRHQDRMD IYMVNPRSTE VKLALRENGT KYIQESAYDA LTFYPGQFTF ISDRTGYQHV
YLYNLNGQLV RPLTQGNYDV TTFYGYDPKT GNCYYQSAQE SPLRRSIYMN DKNGRTRKLS
TETGTNSATF SKNFNYFMNV WSNSTTPYVT TLRDGNGKTL STLLDNKELK EKVASFTGQQ
EFFTFTTSEG VQLNGWMQKP KNFDATKKYP VIMYQYSGPG SQEVADNWKI GFSGGGIWES
YMNEQGYIFV IVDGRGTGVR GSEFEKCTYL KLGELESKDQ VEAAQYLGTL PYVDKNRIGI
WGWSFGGFNT LMAMSEGRPV FKAGVAVAAP TNWKYYDTVY TERYMRTPKE NEGYNINPIN
RVEKLHGNLL LIHGTADDNV HYRNCAEWAE AAVQANKQFQ MQIYTNRNHF ISGGNTRLHL
MTRISEFFKT NL
//