ID   PTH_FRATT               Reviewed;         191 AA.
AC   Q5NGZ6;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-2005, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Peptidyl-tRNA hydrolase {ECO:0000255|HAMAP-Rule:MF_00083};
DE            Short=PTH {ECO:0000255|HAMAP-Rule:MF_00083};
DE            EC=3.1.1.29 {ECO:0000255|HAMAP-Rule:MF_00083};
GN   Name=pth {ECO:0000255|HAMAP-Rule:MF_00083}; OrderedLocusNames=FTT_0680c;
OS   Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC   Francisellaceae; Francisella.
OX   NCBI_TaxID=177416;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCHU S4 / Schu 4;
RX   PubMed=15640799; DOI=10.1038/ng1499;
RA   Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA   Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA   Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA   Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA   Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT   "The complete genome sequence of Francisella tularensis, the causative
RT   agent of tularemia.";
RL   Nat. Genet. 37:153-159(2005).
CC   -!- FUNCTION: The natural substrate for this enzyme may be peptidyl-tRNAs
CC       which drop off the ribosome during protein synthesis.
CC       {ECO:0000255|HAMAP-Rule:MF_00083}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=an N-acyl-L-alpha-aminoacyl-tRNA + H2O = a tRNA + an N-acyl-L-
CC         amino acid + H(+); Xref=Rhea:RHEA:54448, Rhea:RHEA-COMP:10123,
CC         Rhea:RHEA-COMP:13883, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:59874, ChEBI:CHEBI:78442, ChEBI:CHEBI:138191;
CC         EC=3.1.1.29; Evidence={ECO:0000255|HAMAP-Rule:MF_00083};
CC   -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00083}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00083}.
CC   -!- SIMILARITY: Belongs to the PTH family. {ECO:0000255|HAMAP-
CC       Rule:MF_00083}.
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DR   EMBL; AJ749949; CAG45313.1; -; Genomic_DNA.
DR   RefSeq; WP_003020470.1; NZ_CP010290.1.
DR   RefSeq; YP_169696.1; NC_006570.2.
DR   PDB; 3NEA; X-ray; 2.25 A; A=1-188.
DR   PDBsum; 3NEA; -.
DR   AlphaFoldDB; Q5NGZ6; -.
DR   SMR; Q5NGZ6; -.
DR   STRING; 177416.FTT_0680c; -.
DR   DNASU; 3191676; -.
DR   EnsemblBacteria; CAG45313; CAG45313; FTT_0680c.
DR   KEGG; ftu:FTT_0680c; -.
DR   eggNOG; COG0193; Bacteria.
DR   OMA; HVLSKFH; -.
DR   Proteomes; UP000001174; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006412; P:translation; IEA:UniProtKB-UniRule.
DR   CDD; cd00462; PTH; 1.
DR   Gene3D; 3.40.50.1470; -; 1.
DR   HAMAP; MF_00083; Pept_tRNA_hydro_bact; 1.
DR   InterPro; IPR001328; Pept_tRNA_hydro.
DR   InterPro; IPR018171; Pept_tRNA_hydro_CS.
DR   InterPro; IPR036416; Pept_tRNA_hydro_sf.
DR   PANTHER; PTHR17224; PTHR17224; 1.
DR   Pfam; PF01195; Pept_tRNA_hydro; 1.
DR   SUPFAM; SSF53178; SSF53178; 1.
DR   TIGRFAMs; TIGR00447; pth; 1.
DR   PROSITE; PS01196; PEPT_TRNA_HYDROL_2; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Hydrolase; Reference proteome.
FT   CHAIN           1..191
FT                   /note="Peptidyl-tRNA hydrolase"
FT                   /id="PRO_0000187740"
FT   STRAND          6..9
FT                   /evidence="ECO:0007829|PDB:3NEA"
FT   TURN            15..19
FT                   /evidence="ECO:0007829|PDB:3NEA"
FT   HELIX           21..23
FT                   /evidence="ECO:0007829|PDB:3NEA"
FT   HELIX           24..35
FT                   /evidence="ECO:0007829|PDB:3NEA"
FT   STRAND          41..43
FT                   /evidence="ECO:0007829|PDB:3NEA"
FT   HELIX           44..46
FT                   /evidence="ECO:0007829|PDB:3NEA"
FT   STRAND          48..55
FT                   /evidence="ECO:0007829|PDB:3NEA"
FT   STRAND          58..67
FT                   /evidence="ECO:0007829|PDB:3NEA"
FT   HELIX           69..71
FT                   /evidence="ECO:0007829|PDB:3NEA"
FT   HELIX           72..83
FT                   /evidence="ECO:0007829|PDB:3NEA"
FT   HELIX           87..89
FT                   /evidence="ECO:0007829|PDB:3NEA"
FT   STRAND          90..99
FT                   /evidence="ECO:0007829|PDB:3NEA"
FT   STRAND          104..109
FT                   /evidence="ECO:0007829|PDB:3NEA"
FT   HELIX           116..125
FT                   /evidence="ECO:0007829|PDB:3NEA"
FT   STRAND          130..136
FT                   /evidence="ECO:0007829|PDB:3NEA"
FT   HELIX           143..145
FT                   /evidence="ECO:0007829|PDB:3NEA"
FT   HELIX           146..150
FT                   /evidence="ECO:0007829|PDB:3NEA"
FT   HELIX           156..171
FT                   /evidence="ECO:0007829|PDB:3NEA"
FT   HELIX           173..177
FT                   /evidence="ECO:0007829|PDB:3NEA"
SQ   SEQUENCE   191 AA;  21137 MW;  983F0CCC7718660A CRC64;
     MPKIKMIIGL GNIGKEYQDT RHNVGEWFIA KIAQDNNQSF SSNPKLNCNL AKVSIDYNNV
     VLVFPTTYMN NSGLAVSKVA NFYKIAPAEI LVVHDELDID SGEIRLKKGG GHGGHNGLRS
     INQHLGTNDY LRLRIGIGHP GHKSKVANYV LSNPSIAQKK DIDSAIDNGI CFLDDIINYK
     LEPVMQKLHT K