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Database: UniProt
Entry: B0N4L2_9FIRM
LinkDB: B0N4L2_9FIRM
Original site: B0N4L2_9FIRM 
ID   B0N4L2_9FIRM            Unreviewed;       495 AA.
AC   B0N4L2;
DT   08-APR-2008, integrated into UniProtKB/TrEMBL.
DT   08-APR-2008, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   RecName: Full=Peptidase S9 prolyl oligopeptidase catalytic domain-containing protein {ECO:0000259|Pfam:PF00326};
GN   ORFNames=CLORAM_01563 {ECO:0000313|EMBL:EDS18614.1};
OS   Thomasclavelia ramosa DSM 1402.
OC   Bacteria; Bacillota; Erysipelotrichia; Erysipelotrichales;
OC   Coprobacillaceae; Thomasclavelia.
OX   NCBI_TaxID=445974 {ECO:0000313|EMBL:EDS18614.1, ECO:0000313|Proteomes:UP000005798};
RN   [1] {ECO:0000313|EMBL:EDS18614.1, ECO:0000313|Proteomes:UP000005798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1402 {ECO:0000313|EMBL:EDS18614.1,
RC   ECO:0000313|Proteomes:UP000005798};
RA   Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA   Gordon J.;
RT   "Draft genome sequence of Clostridium ramosum(DSM 1402).";
RL   Submitted (NOV-2007) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EDS18614.1, ECO:0000313|Proteomes:UP000005798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 1402 {ECO:0000313|EMBL:EDS18614.1,
RC   ECO:0000313|Proteomes:UP000005798};
RA   Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA   Thiruvilangam P., Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL   Submitted (NOV-2007) 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:EDS18614.1}.
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DR   EMBL; ABFX02000005; EDS18614.1; -; Genomic_DNA.
DR   RefSeq; WP_003537022.1; NZ_DS499656.1.
DR   AlphaFoldDB; B0N4L2; -.
DR   GeneID; 64197934; -.
DR   eggNOG; COG4099; Bacteria.
DR   HOGENOM; CLU_550647_0_0_9; -.
DR   Proteomes; UP000005798; 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   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR001375; Peptidase_S9.
DR   PANTHER; PTHR43037:SF1; BLL1128 PROTEIN; 1.
DR   PANTHER; PTHR43037; UNNAMED PRODUCT-RELATED; 1.
DR   Pfam; PF00326; Peptidase_S9; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000005798}.
FT   DOMAIN          217..388
FT                   /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT                   /evidence="ECO:0000259|Pfam:PF00326"
FT   REGION          441..464
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        444..464
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   495 AA;  54940 MW;  5EF1A7B3EAF18D23 CRC64;
     MRKIKKLFAM MMTLVMTLGI ITTNISAIEE LKVTSIVANT YVGDGQREVS SFEITVNDIN
     LVNDLKAEDF DITNNVSSVP YDVATNALAD DYLDDGISLE IKGNTIILNV KAFDYTGRYN
     PDFSKNPWQV TCNKYGVLSF NKDNVTTLKT KTLDDAIRGT FTYAGLTREY ALYLPKNSDG
     TNMKNVPLVV WNHGGGEYAG QLENTLVANR GLTAWVEAGY NTAVLQIQVS NPNYSYGTAF
     DEDKKSLIDQ NNALQAALIK KLIAEGTVDQ NRVYVTGASS GGGATMRFIM QYPELFAGAI
     ACCSMDPIVW VHYNYQDSYE QIVENFETAF QGQVYTWDET KEMMVSKQVD TASLVELPIY
     FTHAQNDTTC NVNSSKAMYE ALNNLGAKNN HLTIWSNQEM ADEGIAEGLL HWSWVKVLNH
     NEEGSPMNWL FKQTNASENI PVEKEESNNS KTETTASEEA KKAVKTGDDS TVELMAMMTG
     LSLLAGTVVL SKKYY
//
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