ID   TAP_STRLI               Reviewed;         537 AA.
AC   Q54410;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 55.
DE   RecName: Full=Tripeptidyl aminopeptidase {ECO:0000303|PubMed:7487044};
DE            Short=Tap {ECO:0000303|PubMed:7487044};
DE            EC=3.4.14.-;
DE   Flags: Precursor;
GN   Name=tap {ECO:0000303|PubMed:7487044};
OS   Streptomyces lividans.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=1916;
RN   [1] {ECO:0000305, ECO:0000312|EMBL:AAA92338.1}
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 40-50, FUNCTION, AND
RP   SUBCELLULAR LOCATION.
RC   STRAIN=66 / 1326 {ECO:0000269|PubMed:7487044};
RX   PubMed=7487044; DOI=10.1128/aem.61.8.3145-3150.1995;
RA   Butler M.J., Binnie C., DiZonno M.A., Krygsman P., Soltes G.A.,
RA   Soostmeyer G., Walczyk E., Malek L.T.;
RT   "Cloning and characterization of a gene encoding a secreted tripeptidyl
RT   aminopeptidase from Streptomyces lividans 66.";
RL   Appl. Environ. Microbiol. 61:3145-3150(1995).
CC   -!- FUNCTION: Cleaves tripeptides from the N-termini of proteins. Does not
CC       cleave mono- or dipeptides, or N-terminally blocked peptides.
CC       {ECO:0000269|PubMed:7487044}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:7487044}.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family. {ECO:0000305}.
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DR   EMBL; L27466; AAA92338.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q54410; -.
DR   SMR; Q54410; -.
DR   ESTHER; strco-TAP; AlphaBeta_hydrolase.
DR   MEROPS; S33.002; -.
DR   GO; GO:0005576; C:extracellular region; IDA:UniProtKB.
DR   GO; GO:0045148; F:tripeptide aminopeptidase activity; IDA:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; IDA:UniProtKB.
DR   Gene3D; 3.40.50.1820; -; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   SUPFAM; SSF53474; SSF53474; 1.
PE   1: Evidence at protein level;
KW   Aminopeptidase; Direct protein sequencing; Hydrolase; Protease; Secreted;
KW   Signal.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000255"
FT   PROPEP          37..39
FT                   /evidence="ECO:0000255, ECO:0000269|PubMed:7487044"
FT                   /id="PRO_0000401063"
FT   CHAIN           40..537
FT                   /note="Tripeptidyl aminopeptidase"
FT                   /evidence="ECO:0000269|PubMed:7487044"
FT                   /id="PRO_5000142441"
FT   DOMAIN          119..497
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        245
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        470
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        499
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   537 AA;  58273 MW;  850703374BC4DEC9 CRC64;
     MRKSSIRRRA TAFGTAGALV TATLIAGAVS APAASAAPAD GHGHGRSWDR EARGAAIAAA
     RAARAGIDWE DCAADWNLPK PIQCGYVTVP MDYAKPYGKQ IRLAVDRIGN TGTRSERQGA
     LIYNPGGPGG SGLRFPARVT NKSAVWANTA KAYDFVGFDP RGVGHSAPIS CVDPQEFVKA
     PKADPVPGSE ADKRAQRKLA REYAEGCFER SGEMLPHMTT PNTARDLDVI RAALGEKKLN
     YLGVSYGTYL GAVYGTLFPD HVRRMVVDSV VNPSRDKIWY QANLDQDVAF EGRWKDWQDW
     VAANDAAYHL GDTRAEVQDQ WLKLRAAAAK KPLGGVVGPA ELISFFQSAP YYDSAWAPTA
     EIFSKYVAGD TQALVDAAAP DLSDTAGNAS AENGNAVYTA VECTDAKWPA NWRTWDRDNT
     RLHRDHPFMT WANAWMNLPC ATWPVKQQTP LNVKTGKGLP PVLIVQSERD AATPYEGAVE
     LHQRFRGSRL ITERDAGSHG VTGLVNPCIN DRVDTYLLTG RTDARDVTCA PHATPRP