ID   TAP_STRCO               Reviewed;         541 AA.
AC   Q9FCD7;
DT   02-NOV-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   25-MAY-2022, entry version 87.
DE   RecName: Full=Tripeptidyl aminopeptidase {ECO:0000250|UniProtKB:Q54410};
DE            Short=Tap {ECO:0000250|UniProtKB:Q54410};
DE            EC=3.4.14.-;
DE   Flags: Precursor;
GN   Name=tap {ECO:0000250|UniProtKB:Q54410}; OrderedLocusNames=SCO1230;
GN   ORFNames=2SCG1.05c;
OS   Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145).
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces; Streptomyces albidoflavus group.
OX   NCBI_TaxID=100226;
RN   [1] {ECO:0000312|EMBL:CAC01454.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-471 / A3(2) / M145;
RX   PubMed=12000953; DOI=10.1038/417141a;
RA   Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L.,
RA   Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D.,
RA   Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A.,
RA   Fraser A., Goble A., Hidalgo J., Hornsby T., Howarth S., Huang C.-H.,
RA   Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E.,
RA   Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D.,
RA   Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A.,
RA   Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A.;
RT   "Complete genome sequence of the model actinomycete Streptomyces coelicolor
RT   A3(2).";
RL   Nature 417:141-147(2002).
CC   -!- FUNCTION: Cleaves tripeptides from the N-termini of proteins. Does not
CC       cleave mono- or dipeptides, or N-terminally blocked peptides (By
CC       similarity). {ECO:0000250|UniProtKB:Q54410}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000250|UniProtKB:Q54410}.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family.
CC       {ECO:0000250|UniProtKB:Q54410}.
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DR   EMBL; AL939108; CAC01454.1; -; Genomic_DNA.
DR   RefSeq; NP_625518.1; NC_003888.3.
DR   RefSeq; WP_011027660.1; NZ_VNID01000006.1.
DR   AlphaFoldDB; Q9FCD7; -.
DR   SMR; Q9FCD7; -.
DR   STRING; 100226.SCO1230; -.
DR   ESTHER; strco-TAP; AlphaBeta_hydrolase.
DR   MEROPS; S33.002; -.
DR   GeneID; 1096653; -.
DR   KEGG; sco:SCO1230; -.
DR   PATRIC; fig|100226.15.peg.1229; -.
DR   eggNOG; COG0596; Bacteria.
DR   HOGENOM; CLU_013364_3_2_11; -.
DR   InParanoid; Q9FCD7; -.
DR   OMA; LPCATWP; -.
DR   PhylomeDB; Q9FCD7; -.
DR   Proteomes; UP000001973; Chromosome.
DR   GO; GO:0005576; C:extracellular region; ISS:UniProtKB.
DR   GO; GO:0045148; F:tripeptide aminopeptidase activity; ISS:UniProtKB.
DR   GO; GO:0006508; P:proteolysis; ISS: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   3: Inferred from homology;
KW   Aminopeptidase; Hydrolase; Protease; Reference proteome; Secreted; Signal.
FT   SIGNAL          1..36
FT                   /evidence="ECO:0000255"
FT   PROPEP          37..39
FT                   /evidence="ECO:0000250|UniProtKB:Q54410"
FT                   /id="PRO_0000401061"
FT   CHAIN           40..541
FT                   /note="Tripeptidyl aminopeptidase"
FT                   /evidence="ECO:0000250|UniProtKB:Q54410, ECO:0000255"
FT                   /id="PRO_0000401062"
FT   DOMAIN          123..501
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000255"
FT   ACT_SITE        249
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        474
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        503
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   541 AA;  58536 MW;  01BA2E6F70B124DB CRC64;
     MRKSSIRRRA TAFGTAGALV TATLIAGAVS APAASAAPAD GHGHGHGHGR SWDREARGAA
     IAAARAARAG IDWEDCAADW NLPKPIQCGY VTVPMDYAKP YGKQIRLAVD RIGNTGTRSE
     RQGALIYNPG GPGGSGLRFP ARVTSKSAVW ANTAKAYDFV GFDPRGVGHS APISCVDPQE
     FVKAPKADPV PGSEADKRAQ RKLAREYAEG CFERSGEMLP HMTTPNTARD LDVIRAALGE
     KKLNYLGVSY GTYLGAVYGT LFPDHVRRMV VDSVVNPSRD KIWYQANLDQ DVAFEGRWKD
     WQDWVAANDA AYHLGDTRAE VQDQWLKLRA AAAKKPLGGV VGPAELISFF QSAPYYDSAW
     APTAEIFSKY VAGDTQALVD AAAPDLSDTA GNASAENGNA VYTAVECTDA KWPANWRTWD
     RDNTRLHRDH PFMTWANAWM NLPCATWPVK QQTPLNVKTG KGLPPVLIVQ SERDAATPYE
     GAVELHQRFR GSRLITERDA GSHGVTGLVN PCINDRVDTY LLTGGTDARD VTCAPHATPR
     P