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Database: UniProt
Entry: A0A0R1RL25_9LACO
LinkDB: A0A0R1RL25_9LACO
Original site: A0A0R1RL25_9LACO 
ID   A0A0R1RL25_9LACO        Unreviewed;       185 AA.
AC   A0A0R1RL25;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 25.
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   ORFNames=FD35_GL002429 {ECO:0000313|EMBL:KRL54978.1};
OS   Furfurilactobacillus rossiae DSM 15814.
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Furfurilactobacillus.
OX   NCBI_TaxID=1114972 {ECO:0000313|EMBL:KRL54978.1, ECO:0000313|Proteomes:UP000051999};
RN   [1] {ECO:0000313|EMBL:KRL54978.1, ECO:0000313|Proteomes:UP000051999}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15814 {ECO:0000313|EMBL:KRL54978.1,
RC   ECO:0000313|Proteomes:UP000051999};
RX   PubMed=26415554; DOI=10.1038/ncomms9322;
RA   Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA   Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA   Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA   Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA   de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA   Zhang H., O'Toole P.W.;
RT   "Expanding the biotechnology potential of lactobacilli through comparative
RT   genomics of 213 strains and associated genera.";
RL   Nat. Commun. 6:8322-8322(2015).
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:KRL54978.1}.
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DR   EMBL; AZFF01000007; KRL54978.1; -; Genomic_DNA.
DR   RefSeq; WP_017260490.1; NZ_AZFF01000007.1.
DR   AlphaFoldDB; A0A0R1RL25; -.
DR   STRING; 1114972.FD35_GL002429; -.
DR   PATRIC; fig|1114972.6.peg.2493; -.
DR   eggNOG; COG0193; Bacteria.
DR   OrthoDB; 9800507at2; -.
DR   Proteomes; UP000051999; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051999}.
SQ   SEQUENCE   185 AA;  20663 MW;  7E077F5B7CF760C0 CRC64;
     MKMIVGLGNI GPQYDRTRHN VGFMVIDHVA EEYGVTFKRA KQEALIGSTL ISGEKVLLVK
     PTTYMNDSGR AVRPLMDYYD IPLEDVMIVH DDMDLPIGKI RLRQKGSAGG HNGIKSIIAY
     LGTQAFKRVR VGIDHPTRMS VVDYVLGRFT ATQTIGIRSG MDEAQAAIEK WVEGTKFDEV
     MNEFN
//
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