ID   PTH_BACC1               Reviewed;         186 AA.
AC   Q73FF7;
DT   21-JUN-2005, integrated into UniProtKB/Swiss-Prot.
DT   21-JUN-2005, sequence version 2.
DT   03-AUG-2022, entry version 96.
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}; Synonyms=spoVC;
GN   OrderedLocusNames=BCE_0049;
OS   Bacillus cereus (strain ATCC 10987 / NRS 248).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC   Bacillus cereus group.
OX   NCBI_TaxID=222523;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10987 / NRS 248;
RX   PubMed=14960714; DOI=10.1093/nar/gkh258;
RA   Rasko D.A., Ravel J., Oekstad O.A., Helgason E., Cer R.Z., Jiang L.,
RA   Shores K.A., Fouts D.E., Tourasse N.J., Angiuoli S.V., Kolonay J.F.,
RA   Nelson W.C., Kolstoe A.-B., Fraser C.M., Read T.D.;
RT   "The genome sequence of Bacillus cereus ATCC 10987 reveals metabolic
RT   adaptations and a large plasmid related to Bacillus anthracis pXO1.";
RL   Nucleic Acids Res. 32:977-988(2004).
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}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAS38985.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE017194; AAS38985.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q73FF7; -.
DR   SMR; Q73FF7; -.
DR   EnsemblBacteria; AAS38985; AAS38985; BCE_0049.
DR   KEGG; bca:BCE_0049; -.
DR   HOGENOM; CLU_062456_4_1_9; -.
DR   Proteomes; UP000002527; 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; PS01195; PEPT_TRNA_HYDROL_1; 1.
DR   PROSITE; PS01196; PEPT_TRNA_HYDROL_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase.
FT   CHAIN           1..186
FT                   /note="Peptidyl-tRNA hydrolase"
FT                   /id="PRO_0000187684"
SQ   SEQUENCE   186 AA;  21024 MW;  9F16EEF6D814BC8B CRC64;
     MKLIVGLGNP GREYELTRHN IGFMAIDELA KRWNISLNEQ KFKGVFGAGF VNGEKVILLK
     PLTYMNLSGE SIRPLMDYYK IDVEDFVVLY DDLDIPVGKL RLRMKGSAGG HNGVKSTISH
     LGTQEFQRIR MGIDRPKNGM KVVDYVLGRF TSEEIPGVNH SIEKAADACE EWLNKPFLQI
     MNTFNS