ID U5N790_9BURK Unreviewed; 227 AA.
AC U5N790;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
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=Cenrod_1169 {ECO:0000313|EMBL:AGX87262.1};
OS Candidatus Symbiobacter mobilis CR.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae.
OX NCBI_TaxID=946483 {ECO:0000313|EMBL:AGX87262.1, ECO:0000313|Proteomes:UP000017184};
RN [1] {ECO:0000313|EMBL:AGX87262.1, ECO:0000313|Proteomes:UP000017184}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CR {ECO:0000313|EMBL:AGX87262.1};
RX PubMed=24267588; DOI=10.1186/gb-2013-14-11-r127;
RA Liu Z., Muller J., Li T., Alvey R.M., Vogl K., Frigaard N.U.,
RA Rockwell N.C., Boyd E.S., Tomsho L.P., Schuster S.C., Henke P., Rohde M.,
RA Overmann J., Bryant D.A.;
RT "Genomic analysis reveals key aspects of prokaryotic symbiosis in the
RT phototrophic consortium "Chlorochromatium aggregatum".";
RL Genome Biol. 14:R127-R127(2013).
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 -!- 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}.
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DR EMBL; CP004885; AGX87262.1; -; Genomic_DNA.
DR AlphaFoldDB; U5N790; -.
DR STRING; 946483.Cenrod_1169; -.
DR KEGG; cbx:Cenrod_1169; -.
DR PATRIC; fig|946483.4.peg.1171; -.
DR eggNOG; COG0193; Bacteria.
DR HOGENOM; CLU_062456_4_2_4; -.
DR OrthoDB; 9800507at2; -.
DR Proteomes; UP000017184; Chromosome.
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 {ECO:0000256|HAMAP-Rule:MF_00083};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00083};
KW Reference proteome {ECO:0000313|Proteomes:UP000017184}.
FT REGION 199..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 227 AA; 25072 MW; 5D2E87C41FB75D0D CRC64;
MIQLIVGLGN PGPQYQETRH NVGFWWVDAL AASLRCVWAA DKGFQAWVAT ASVDAHPLRL
LKPQTFMNLS GRSVASLARF YKIDPTEILV VHDDLDFEPG RVQCKLGGGH AGHNGLRDVH
AQLGTDRYWR LRLGIGHPGH KSEVVSWVLH QPEADDRVAI ERAIERSLAA LPDLLAGHTT
LAMQAMQVPK EKPILARQAE HPRKAEPVQQ VEVRTALSTD ASSEVNL
//