UniProt: F4LTI5

Database: UniProt
Entry: F4LTI5_TEPAE

LinkDB:  F4LTI5_TEPAE 
Original site:  F4LTI5_TEPAE

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Ontology (3)   
   GO (3)   
Chemical reaction (1)   
   KEGG ENZYME (1)   
Gene (2)   
   KEGG GENES (2)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (11)   
   InterPro (6)   
   Pfam (1)   
   PROSITE (4)   
Literature (1)   
   PubMed (1)   
All databases (20)   

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ID   F4LTI5_TEPAE            Unreviewed;       989 AA.
AC   F4LTI5; L0RVZ6;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=Tripeptidyl-peptidase II {ECO:0000313|EMBL:CCP25026.1};
DE            EC=3.4.14.10 {ECO:0000313|EMBL:CCP25026.1};
GN   OrderedLocusNames=TEPIRE1_0349 {ECO:0000313|EMBL:CCP25026.1};
OS   Tepidanaerobacter acetatoxydans (strain DSM 21804 / JCM 16047 / Re1).
OC   Bacteria; Bacillota; Clostridia; Thermosediminibacterales;
OC   Tepidanaerobacteraceae; Tepidanaerobacter.
OX   NCBI_TaxID=1209989 {ECO:0000313|EMBL:CCP25026.1, ECO:0000313|Proteomes:UP000010802};
RN   [1] {ECO:0000313|Proteomes:UP000010802}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Re1 {ECO:0000313|Proteomes:UP000010802};
RX   PubMed=23469343; DOI=10.1128/genomeA.00213-12;
RA   Manzoor S., Bongcam-Rudloff E., Schnurer A., Muller B.;
RT   "First genome sequence of a syntrophic acetate-oxidizing bacterium,
RT   Tepidanaerobacter acetatoxydans strain Re1.";
RL   Genome Announc. 1:E00213-E00213(2013).
CC   -!- SIMILARITY: Belongs to the peptidase S8 family.
CC       {ECO:0000256|ARBA:ARBA00011073, ECO:0000256|PROSITE-ProRule:PRU01240,
CC       ECO:0000256|RuleBase:RU003355}.
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DR   EMBL; HF563609; CCP25026.1; -; Genomic_DNA.
DR   RefSeq; WP_013777439.1; NC_019954.2.
DR   AlphaFoldDB; F4LTI5; -.
DR   STRING; 1209989.TepRe1_0313; -.
DR   KEGG; tae:TepiRe1_0349; -.
DR   KEGG; tep:TepRe1_0313; -.
DR   PATRIC; fig|1209989.3.peg.366; -.
DR   eggNOG; COG1404; Bacteria.
DR   HOGENOM; CLU_282117_0_0_9; -.
DR   OrthoDB; 9798386at2; -.
DR   Proteomes; UP000010802; Chromosome.
DR   GO; GO:0004252; F:serine-type endopeptidase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008240; F:tripeptidyl-peptidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.120.380; -; 1.
DR   Gene3D; 3.40.50.200; Peptidase S8/S53 domain; 2.
DR   InterPro; IPR000209; Peptidase_S8/S53_dom.
DR   InterPro; IPR036852; Peptidase_S8/S53_dom_sf.
DR   InterPro; IPR023827; Peptidase_S8_Asp-AS.
DR   InterPro; IPR022398; Peptidase_S8_His-AS.
DR   InterPro; IPR023828; Peptidase_S8_Ser-AS.
DR   InterPro; IPR015500; Peptidase_S8_subtilisin-rel.
DR   PANTHER; PTHR43806:SF59; CEREVISIN-RELATED; 1.
DR   PANTHER; PTHR43806; PEPTIDASE S8; 1.
DR   Pfam; PF00082; Peptidase_S8; 1.
DR   PRINTS; PR00723; SUBTILISIN.
DR   SUPFAM; SSF52743; Subtilisin-like; 1.
DR   PROSITE; PS51892; SUBTILASE; 1.
DR   PROSITE; PS00136; SUBTILASE_ASP; 1.
DR   PROSITE; PS00137; SUBTILASE_HIS; 1.
DR   PROSITE; PS00138; SUBTILASE_SER; 1.
PE   3: Inferred from homology;
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|PROSITE-
KW   ProRule:PRU01240};
KW   Protease {ECO:0000256|ARBA:ARBA00022670, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}; Reference proteome {ECO:0000313|Proteomes:UP000010802};
KW   Serine protease {ECO:0000256|ARBA:ARBA00022825, ECO:0000256|PROSITE-
KW   ProRule:PRU01240}.
FT   DOMAIN          53..448
FT                   /note="Peptidase S8/S53"
FT                   /evidence="ECO:0000259|Pfam:PF00082"
FT   ACT_SITE        62
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        236
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
FT   ACT_SITE        411
FT                   /note="Charge relay system"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU01240"
SQ   SEQUENCE   989 AA;  108504 MW;  07B2F099DFBA7132 CRC64;
     MKKKLCLLII IFIVCFTGLA KGQGLNFNVN TGMVEALRSI KADEFRKQYG VDGNGIKVAV
     IDTGVDVSHP DLQRTPNGST KVINYIDLTN EGYVDTKATA IPEKNLVNIE EQKYNVEGIR
     SMSGSFHVGV FKEQQLDKDS PICQDVNRNN KNNDAFGVLV IDSVLPKIYD TVYVDTNKNF
     DFTDEIPLRV YSTDYKWASF GRDNPATDYV EESSFVITNV DINGSFVKLG FDGNGHGTHV
     TGIIGANGNL MGTAPGAQII AIKVMGSSGD GNWEDIFKAI EYAVKQGADV INVSIGNLAS
     SKEGHKTQLE LLKKLSLESN AIIVIAAGNS GPGLATAYDV GGADNIITVG AYMSPRLWDI
     NYNAKVPDET LWYYTGVGHS SSRPTVVAPS SVISTVNRWD SGGYFLMDGT SMAAPFVSGS
     CALLREQAKK EGIEISPANL KKAIEAGTQK IEGYLEIEQG NGLIDVVKSW NVLKHGTGDL
     FGLPRIAINL TDSSEDIDGV TFRDQLKAQL KLLLTNMSPG SQVIRLESDQ EWLSIGENKN
     EVVLPQGKPQ SMMLSYRFPQ QPGLYTARTT GYNIESGKAV MNFLTTAAVP YDLAKTCNIS
     INGELSPSHW ERYFFKTVPG MSEIDLTLTV LEKNNSMGRA LIYVYDPEGH KVYEDVAGAD
     YISTKQSSCF KAAKPKPGIW EVVVVSDYNL SDFGADVTSY RLSAKAFGIF TDIKELTFAV
     KKGESYISQE IMLKNGDNVF DGRLEGVGLA EKNEGISFAK VKVKDGELTK GPIIKVPVNA
     MDLNINLIPQ NNQKCDMDLY LYKKNTDGLY EEVALSAKID VLQENIHLTS PEPGEYIVYI
     DGFSIPEGTA DIEVKTQILT DKMNVYIQDI YGKLNPNHQW NAGLFVNIPT TGSEFIGYIA
     VENANGNEIS HIPLKFVVGR KMLEIEITSD GYILVKEKDT GNPVNTDIIV NGIEYLVIDG
     KAVIPIDTVV ETIEIYDERY APLVFRKNF
//

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