PTH_CHLMU
ID PTH_CHLMU Reviewed; 179 AA.
AC P49607;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 3.
DT 25-MAY-2022, entry version 119.
DE RecName: Full=Peptidyl-tRNA hydrolase {ECO:0000255|HAMAP-Rule:MF_00083};
DE Short=PTH {ECO:0000255|HAMAP-Rule:MF_00083};
DE EC=3.1.1.29 {ECO:0000255|HAMAP-Rule:MF_00083};
GN Name=pth {ECO:0000255|HAMAP-Rule:MF_00083}; OrderedLocusNames=TC_0183;
OS Chlamydia muridarum (strain MoPn / Nigg).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=243161;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=MoPn;
RX PubMed=8635758; DOI=10.1016/0378-1119(95)00823-3;
RA de la Vega F.M., Galindo J.M., Old I.G., Guarneros G.;
RT "Microbial genes homologous to the peptidyl-tRNA hydrolase-encoding gene of
RT Escherichia coli.";
RL Gene 169:97-100(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MoPn / Nigg;
RX PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA Salzberg S.L., Eisen J.A., Fraser C.M.;
RT "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT AR39.";
RL Nucleic Acids Res. 28:1397-1406(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 27-179.
RC STRAIN=MoPn;
RX PubMed=2254267; DOI=10.1128/jb.172.12.6959-6972.1990;
RA Engel J.N., Pollack J., Perara E., Ganem D.;
RT "Heat shock response of murine Chlamydia trachomatis.";
RL J. Bacteriol. 172:6959-6972(1990).
CC -!- FUNCTION: The natural substrate for this enzyme may be peptidyl-tRNAs
CC which drop off the ribosome during protein synthesis.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_00083};
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00083}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00083}.
CC -!- SIMILARITY: Belongs to the PTH family. {ECO:0000255|HAMAP-
CC Rule:MF_00083}.
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DR EMBL; U31570; AAB06184.1; -; Genomic_DNA.
DR EMBL; AE002160; AAF39057.1; -; Genomic_DNA.
DR EMBL; M62820; AAA23133.1; -; Genomic_DNA.
DR PIR; C37840; C37840.
DR PIR; C81732; C81732.
DR RefSeq; WP_010229742.1; NZ_CP027217.1.
DR AlphaFoldDB; P49607; -.
DR SMR; P49607; -.
DR STRING; 243161.TC_0183; -.
DR EnsemblBacteria; AAF39057; AAF39057; TC_0183.
DR GeneID; 1246309; -.
DR KEGG; cmu:TC_0183; -.
DR eggNOG; COG0193; Bacteria.
DR HOGENOM; CLU_062456_3_1_0; -.
DR OMA; HVLSKFH; -.
DR OrthoDB; 1676462at2; -.
DR Proteomes; UP000000800; 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; -; 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 PANTHER; PTHR17224; PTHR17224; 1.
DR Pfam; PF01195; Pept_tRNA_hydro; 1.
DR SUPFAM; SSF53178; SSF53178; 1.
DR TIGRFAMs; TIGR00447; pth; 1.
DR PROSITE; PS01195; PEPT_TRNA_HYDROL_1; 1.
DR PROSITE; PS01196; PEPT_TRNA_HYDROL_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Hydrolase.
FT CHAIN 1..179
FT /note="Peptidyl-tRNA hydrolase"
FT /id="PRO_0000187717"
FT CONFLICT 146
FT /note="V -> G (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 161
FT /note="S -> G (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 178..179
FT /note="GF -> AFNLKGIYCSLFEKKSS (in Ref. 1 and 3)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 179 AA; 19915 MW; 5D682B5269C0564B CRC64;
MVKLVVGIGN PGRQYVWTRH NIGFLFLDML ASRFSGAFRE APRLFSSFMK VETSCGVIVL
IKPSTYVNLT GKAVLAAKRF FGVSVEGILI VADDINREFG SIRFRQDCGA GGHNGLKNTT
QVLQSNHYWQ LRLGVGRPSN PESEGVADYV LSNFSFNERK SLNGFFEKGI EEISPWLGF
