ID A8F5S4_PSELT Unreviewed; 628 AA.
AC A8F5S4;
DT 13-NOV-2007, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2007, sequence version 1.
DT 27-MAR-2024, entry version 70.
DE SubName: Full=Acylaminoacyl-peptidase {ECO:0000313|EMBL:ABV33508.1};
DE EC=3.4.19.1 {ECO:0000313|EMBL:ABV33508.1};
GN OrderedLocusNames=Tlet_0942 {ECO:0000313|EMBL:ABV33508.1};
OS Pseudothermotoga lettingae (strain ATCC BAA-301 / DSM 14385 / NBRC 107922 /
OS TMO) (Thermotoga lettingae).
OC Bacteria; Thermotogota; Thermotogae; Thermotogales; Thermotogaceae;
OC Pseudothermotoga.
OX NCBI_TaxID=416591 {ECO:0000313|EMBL:ABV33508.1, ECO:0000313|Proteomes:UP000002016};
RN [1] {ECO:0000313|EMBL:ABV33508.1, ECO:0000313|Proteomes:UP000002016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO
RC {ECO:0000313|Proteomes:UP000002016};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Foster B., Bruce D., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Nelson K., Gogarten J.P., Noll K.,
RA Richardson P.;
RT "Complete sequence of Thermotoga lettingae TMO.";
RL Submitted (AUG-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABV33508.1, ECO:0000313|Proteomes:UP000002016}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-301 / DSM 14385 / NBRC 107922 / TMO
RC {ECO:0000313|Proteomes:UP000002016};
RX PubMed=19307556; DOI=10.1073/pnas.0901260106;
RA Zhaxybayeva O., Swithers K.S., Lapierre P., Fournier G.P., Bickhart D.M.,
RA DeBoy R.T., Nelson K.E., Nesbo C.L., Doolittle W.F., Gogarten J.P.,
RA Noll K.M.;
RT "On the chimeric nature, thermophilic origin, and phylogenetic placement of
RT the Thermotogales.";
RL Proc. Natl. Acad. Sci. U.S.A. 106:5865-5870(2009).
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DR EMBL; CP000812; ABV33508.1; -; Genomic_DNA.
DR RefSeq; WP_012002989.1; NZ_BSDV01000001.1.
DR AlphaFoldDB; A8F5S4; -.
DR STRING; 416591.Tlet_0942; -.
DR MEROPS; S09.071; -.
DR KEGG; tle:Tlet_0942; -.
DR eggNOG; COG0823; Bacteria.
DR eggNOG; COG1506; Bacteria.
DR HOGENOM; CLU_008615_2_2_0; -.
DR OrthoDB; 108903at2; -.
DR Proteomes; UP000002016; Chromosome.
DR GO; GO:0008242; F:omega peptidase activity; IEA:UniProtKB-EC.
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; IPR011659; PD40.
DR InterPro; IPR001375; Peptidase_S9.
DR PANTHER; PTHR42776:SF28; DIPEPTIDYL-PEPTIDASE 5; 1.
DR PANTHER; PTHR42776; SERINE PEPTIDASE S9 FAMILY MEMBER; 1.
DR Pfam; PF07676; PD40; 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, ECO:0000313|EMBL:ABV33508.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000002016}.
FT DOMAIN 414..614
FT /note="Peptidase S9 prolyl oligopeptidase catalytic"
FT /evidence="ECO:0000259|Pfam:PF00326"
SQ SEQUENCE 628 AA; 71753 MW; 1ED273E6F22C5251 CRC64;
MKWECSTFTK FVVPVEVKIS RDGRWIAYTL KKISPAENKT IRQITIKNLS TGESFYLPQE
TSKPRFSPDG KKLAFIRKIN DSNILSMIEL AHFSEKEILK VDSLTAIDWS SDSKKLLIMF
AKKRNDKDLY FEDTLPVWFD GKGFLDSSID VVQIIDLESC QVLDQMEERN IANILWIEND
IVYAKYSEKK PFTEFDIFLY IDGKKRLILE KVGLIPTSAE GKKIIMLGRE QKSAFQHEYA
YLYENGKLHP LTEKYALNNS GHISAEIWAS DSEVYPLIRN NTVYFKSGSG GKILLEKLNL
EETEKQTIIS DNSIITAFDA SDNGKIVFVK VSPEKPAEVY LYENGKENKV TELNQSIISK
LKVRPMKHLD VTSFDGTNID AWYIKPDSAP APAVVFVHGG PKGAYGYNLY FLGQLLAEEG
FFVLFTNPRG SDNYSEQFAL TVTEKTGKED FKDILAAIDN LRKNEQIASV GITGISYGGY
MTNWAITQTD LFKAAVSENG ISYWFTSYAF SDIGFWFDKS LIGNDPLSNP NYRELSPIFY
VKNIKTPLLL IHSLEDFRCP LDQSLMFYTI LKDFGKEVYL AIFKKGAHGH SVQGSYTHRL
KRYKLIVEFF KQKLLEEKEG FDVNKCFE
//
