ID L9M971_9GAMM Unreviewed; 192 AA.
AC L9M971;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE RecName: Full=Peptidyl-tRNA hydrolase {ECO:0000256|ARBA:ARBA00013260, ECO:0000256|HAMAP-Rule:MF_00083};
DE Short=PTH {ECO:0000256|HAMAP-Rule:MF_00083};
DE EC=3.1.1.29 {ECO:0000256|ARBA:ARBA00013260, ECO:0000256|HAMAP-Rule:MF_00083};
GN Name=pth {ECO:0000256|HAMAP-Rule:MF_00083,
GN ECO:0000313|EMBL:ELW83484.1};
GN ORFNames=ACINWC743_1239 {ECO:0000313|EMBL:ELW83484.1};
OS Acinetobacter sp. WC-743.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter.
OX NCBI_TaxID=903945 {ECO:0000313|EMBL:ELW83484.1, ECO:0000313|Proteomes:UP000011515};
RN [1] {ECO:0000313|EMBL:ELW83484.1, ECO:0000313|Proteomes:UP000011515}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WC-743 {ECO:0000313|EMBL:ELW83484.1,
RC ECO:0000313|Proteomes:UP000011515};
RA Harkins D.M., Brinkac L.M., Durkin A.S., Beck E., Fedorova N.B., Kim M.,
RA Onuska J., Radune D., DePew J., Koroleva G.I., Singh I., Chahine M.A.,
RA Cash D.M., Huang X.-Z., Nikolich M.P., Nierman W.C., Fouts D.E.;
RL Submitted (SEP-2012) 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:0000256|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:0000256|HAMAP-Rule:MF_00083,
CC ECO:0000256|RuleBase:RU000673};
CC -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00083}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00083}.
CC -!- SIMILARITY: Belongs to the PTH family. {ECO:0000256|ARBA:ARBA00038063,
CC ECO:0000256|HAMAP-Rule:MF_00083, ECO:0000256|RuleBase:RU004320}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:ELW83484.1}.
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DR EMBL; AMFQ01000085; ELW83484.1; -; Genomic_DNA.
DR RefSeq; WP_004828267.1; NZ_AMFQ01000085.1.
DR AlphaFoldDB; L9M971; -.
DR GeneID; 69461426; -.
DR PATRIC; fig|903945.3.peg.2308; -.
DR Proteomes; UP000011515; Unassembled WGS sequence.
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; PS01195; PEPT_TRNA_HYDROL_1; 1.
DR PROSITE; PS01196; PEPT_TRNA_HYDROL_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00083};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00083}.
SQ SEQUENCE 192 AA; 20968 MW; 3CF3AE9D1C997AF7 CRC64;
MSKLSLIVGL GNPGSEYAQT RHNAGFWFVE RLAEQYGITL KTDSKYKGIS GRGNIEGQDV
RLLLPTTFMN LSGQSVVPFA KFYQIKPEEI LIAHDELDMD PGVIRLKTGG GHGGHNGLRD
IVPHIGSNFH RLRIGIGHPG AKEKVSGHVL GKAPSSEQTL MDDAIHHALA RTKLLVNGEI
QQAMNQINAY KP
//
