ID   ARFB_PSEPU              Reviewed;         137 AA.
AC   P45388;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Peptidyl-tRNA hydrolase ArfB;
DE            Short=PTH;
DE            EC=3.1.1.29;
DE   AltName: Full=Alternative ribosome-rescue factor B;
GN   Name=arfB;
OS   Pseudomonas putida (Arthrobacter siderocapsulatus).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=303;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=PRS2000;
RX   PubMed=1624453; DOI=10.1128/jb.174.14.4657-4666.1992;
RA   Parales R.E., Harwood C.S.;
RT   "Characterization of the genes encoding beta-ketoadipate: succinyl-coenzyme
RT   A transferase in Pseudomonas putida.";
RL   J. Bacteriol. 174:4657-4666(1992).
CC   -!- FUNCTION: Rescues stalled ribosomes. Can hydrolyze peptidyl-tRNA on
CC       ribosomes stalled by both non-stop mRNAs and mRNAs that contain rare
CC       codon clusters (By similarity). {ECO:0000250}.
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;
CC   -!- SUBUNIT: Associated with 70S ribosomes and polysomes. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the prokaryotic/mitochondrial release factor
CC       family. {ECO:0000305}.
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DR   EMBL; M88763; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; WP_016498873.1; NZ_UGUX01000003.1.
DR   AlphaFoldDB; P45388; -.
DR   SMR; P45388; -.
DR   GeneID; 45523297; -.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IEA:UniProtKB-EC.
DR   GO; GO:0003747; F:translation release factor activity; IEA:InterPro.
DR   InterPro; IPR000352; Pep_chain_release_fac_I.
DR   InterPro; IPR045853; Pep_chain_release_fac_I_sf.
DR   Pfam; PF00472; RF-1; 1.
DR   SUPFAM; SSF75620; SSF75620; 1.
DR   PROSITE; PS00745; RF_PROK_I; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Hydrolase; Translation regulation.
FT   CHAIN           1..137
FT                   /note="Peptidyl-tRNA hydrolase ArfB"
FT                   /id="PRO_0000166859"
FT   REGION          102..137
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   137 AA;  15181 MW;  BBDAF2B68986A2EC CRC64;
     MLTISNNVHL PDAEIELTYI RAQGAGGQNV NKVSSAVHLR FDIPASSLPE FYKERLLALR
     DSRITGDGVL IIKAQQYRTQ DQNRADALAR LAELIIAAGK TEKKRRPTKP TLGSKTRRLE
     GKARRSTVKA GRGKVDF