ID PTH_ACIF5 Reviewed; 189 AA.
AC B5EKJ0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-OCT-2008, sequence version 1.
DT 27-MAR-2024, entry version 74.
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=Lferr_1804;
OS Acidithiobacillus ferrooxidans (strain ATCC 53993 / BNL-5-31)
OS (Leptospirillum ferrooxidans (ATCC 53993)).
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=380394;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53993 / BNL-5-31;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA Borole A.P.;
RT "Complete sequence of Acidithiobacillus ferrooxidans ATCC 53993.";
RL Submitted (AUG-2008) to the EMBL/GenBank/DDBJ databases.
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; CP001132; ACH84025.1; -; Genomic_DNA.
DR RefSeq; WP_012537005.1; NC_011206.1.
DR AlphaFoldDB; B5EKJ0; -.
DR SMR; B5EKJ0; -.
DR GeneID; 66432912; -.
DR KEGG; afe:Lferr_1804; -.
DR eggNOG; COG0193; Bacteria.
DR HOGENOM; CLU_062456_3_1_6; -.
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; Peptidyl-tRNA hydrolase; 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 NCBIfam; TIGR00447; pth; 1.
DR PANTHER; PTHR17224; PEPTIDYL-TRNA HYDROLASE; 1.
DR PANTHER; PTHR17224:SF1; PEPTIDYL-TRNA HYDROLASE-RELATED; 1.
DR Pfam; PF01195; Pept_tRNA_hydro; 1.
DR SUPFAM; SSF53178; Peptidyl-tRNA hydrolase-like; 1.
DR PROSITE; PS01196; PEPT_TRNA_HYDROL_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase.
FT CHAIN 1..189
FT /note="Peptidyl-tRNA hydrolase"
FT /id="PRO_1000092900"
SQ SEQUENCE 189 AA; 20542 MW; A9247CD022071E9D CRC64;
MDWLLAGLGN PGAEYARTRH NAGFWTLQTL ADRVGASLRM EKRWHCLAAT ARASGLELGL
CMPQDFMNRS GGPVQAMAAF YKVAAERILV MHDELDLPPG AARLKRGGGH GGHNGLRDLD
RALGTRDYWR LRIGIGHPGH KDAVIPYVLS APPPADKTLI DEAIERSLGV LPDFLCGRTD
AAQKSLHSD
//
