ID E1L860_9FIRM Unreviewed; 192 AA.
AC E1L860;
DT 30-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2010, sequence version 1.
DT 24-JAN-2024, entry version 46.
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:EFL55462.1};
GN ORFNames=HMPREF9321_1555 {ECO:0000313|EMBL:EFL55462.1};
OS Veillonella atypica ACS-049-V-Sch6.
OC Bacteria; Bacillota; Negativicutes; Veillonellales; Veillonellaceae;
OC Veillonella.
OX NCBI_TaxID=866776 {ECO:0000313|EMBL:EFL55462.1, ECO:0000313|Proteomes:UP000004211};
RN [1] {ECO:0000313|EMBL:EFL55462.1, ECO:0000313|Proteomes:UP000004211}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ACS-049-V-Sch6 {ECO:0000313|EMBL:EFL55462.1,
RC ECO:0000313|Proteomes:UP000004211};
RA Durkin A.S., Madupu R., Torralba M., Gillis M., Methe B., Sutton G.,
RA Nelson K.E.;
RL Submitted (AUG-2010) 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:EFL55462.1}.
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DR EMBL; AEDR01000057; EFL55462.1; -; Genomic_DNA.
DR RefSeq; WP_005378490.1; NZ_AEDR01000057.1.
DR AlphaFoldDB; E1L860; -.
DR GeneID; 57773310; -.
DR eggNOG; COG0193; Bacteria.
DR Proteomes; UP000004211; 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; 21298 MW; 426F7DE518443875 CRC64;
MKLVVGLGNP GKQYEATKHN IGFMVIDAIA DSVSHTPWRE EQKAEVCSIN VAGEKVLLVK
PQTFMNASGE SVGPLMRYYK IDPSDVYCIY DDMDLPVGKL RIRPNGSSGG HNGIKSLISH
IGTENFPRFR VGIGRPLPQW TVIDHVLAPF SEENQEKVQK GIKDTVKAVL GTLEVGIDKG
MNQFNPKRRP QR
//