ID   A0A448N1H9_9ACTN        Unreviewed;       547 AA.
AC   A0A448N1H9;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Tripeptidyl aminopeptidase {ECO:0000313|EMBL:VEH71267.1};
DE            EC=3.4.14.- {ECO:0000313|EMBL:VEH71267.1};
GN   Name=tap {ECO:0000313|EMBL:VEH71267.1};
GN   ORFNames=NCTC12967_02585 {ECO:0000313|EMBL:VEH71267.1};
OS   Arachnia propionica.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; Arachnia.
OX   NCBI_TaxID=1750 {ECO:0000313|EMBL:VEH71267.1, ECO:0000313|Proteomes:UP000273044};
RN   [1] {ECO:0000313|EMBL:VEH71267.1, ECO:0000313|Proteomes:UP000273044}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC12967 {ECO:0000313|EMBL:VEH71267.1,
RC   ECO:0000313|Proteomes:UP000273044};
RG   Pathogen Informatics;
RL   Submitted (DEC-2018) to the EMBL/GenBank/DDBJ databases.
CC   -!- SIMILARITY: Belongs to the peptidase S33 family.
CC       {ECO:0000256|ARBA:ARBA00010088}.
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DR   EMBL; LR134406; VEH71267.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A448N1H9; -.
DR   Proteomes; UP000273044; Chromosome 1.
DR   GO; GO:0004177; F:aminopeptidase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.1820; alpha/beta hydrolase; 1.
DR   InterPro; IPR029058; AB_hydrolase.
DR   InterPro; IPR000073; AB_hydrolase_1.
DR   InterPro; IPR013595; Pept_S33_TAP-like_C.
DR   PANTHER; PTHR43248; 2-SUCCINYL-6-HYDROXY-2,4-CYCLOHEXADIENE-1-CARBOXYLATE SYNTHASE; 1.
DR   PANTHER; PTHR43248:SF29; AB HYDROLASE-1 DOMAIN-CONTAINING PROTEIN; 1.
DR   Pfam; PF00561; Abhydrolase_1; 1.
DR   Pfam; PF08386; Abhydrolase_4; 1.
DR   SUPFAM; SSF53474; alpha/beta-Hydrolases; 1.
PE   3: Inferred from homology;
KW   Aminopeptidase {ECO:0000313|EMBL:VEH71267.1};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:VEH71267.1};
KW   Protease {ECO:0000313|EMBL:VEH71267.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000273044}.
FT   DOMAIN          151..313
FT                   /note="AB hydrolase-1"
FT                   /evidence="ECO:0000259|Pfam:PF00561"
FT   DOMAIN          447..546
FT                   /note="Peptidase S33 tripeptidyl aminopeptidase-like C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF08386"
FT   REGION          32..81
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   547 AA;  57969 MW;  6A49D0C1C30930E4 CRC64;
     MRRGIVWVQG MLIFVAVGLV VAFFASGMLA PGRQASRTPS AEPSVQSPPA VGDQKPGVPA
     VPVSEHETWP HEPVENPDRQ LDVKASNPSV QLPAALGDDL TPYWQQSLNW QPCGSALCAT
     MKVPLDWDNP GKAALDIKVT KAPSENPTKG PLFVNPGGPG IEGGTFATNL GSDKWKGYDI
     IAWDPRGSGE STHVQCGTTE QTDKAYFADG TPDDEAEKTA LNDVWAAFAR ECREASGELL
     DHISTIENVR DLDLLRFLTG AEKLNYLGVS YGTFIGAMYA ELFPERTGHL VLDSAMDITN
     EGEVSQAEGF ELALGLYADW CAGEGSCSLG NSRDEVISRI NSFLHGLDAK PLKVGDRQVT
     QGQGANGIAL FLYSGKEAYP GLTQLLDSAM NGDGRVILKA SDLLSGRAEN GWETVAYAFP
     AIRCVDQPDA GVAATEEARK KVAEKAPVFG GNMGSELVCE RWTANSAPNL KLTGKGAAPI
     LVVGATGDSA TPYQQAVTMA KQLESGHLLT YDGPGHGSVT SGNACVDETV TAYFEDGTLP
     EDGKTCS
//