ID M4ZU39_9FLAO Unreviewed; 192 AA.
AC M4ZU39;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 41.
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:BAM99858.1};
GN ORFNames=BPAA_592 {ECO:0000313|EMBL:BAM99858.1};
OS Blattabacterium cuenoti BPAA.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Blattabacteriaceae; Blattabacterium.
OX NCBI_TaxID=1229512 {ECO:0000313|EMBL:BAM99858.1, ECO:0000313|Proteomes:UP000011815};
RN [1] {ECO:0000313|EMBL:BAM99858.1, ECO:0000313|Proteomes:UP000011815}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BPAA {ECO:0000313|EMBL:BAM99858.1,
RC ECO:0000313|Proteomes:UP000011815};
RX PubMed=23515978; DOI=10.1098/rsbl.2012.1153;
RA Tokuda G., Elbourne L.D.H., Kinjo Y., Saitoh S., Sabree Z., Hojo M.,
RA Yamada A., Hayashi Y., Shigenobu S., Bandi C., Paulsen I.T., Watanabe H.,
RA Lo N.;
RT "Maintenance of essential amino acid synthesis pathways in the
RT Blattabacterium cuenoti symbiont of a wood-feeding cockroach.";
RL Biol. Lett. 9:20121153-20121153(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 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}.
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DR EMBL; AP012548; BAM99858.1; -; Genomic_DNA.
DR RefSeq; WP_015430177.1; NC_020510.1.
DR AlphaFoldDB; M4ZU39; -.
DR STRING; 1229512.BPAA_592; -.
DR KEGG; blp:BPAA_592; -.
DR PATRIC; fig|1229512.3.peg.574; -.
DR eggNOG; COG0193; Bacteria.
DR HOGENOM; CLU_062456_4_1_10; -.
DR Proteomes; UP000011815; 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; 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; 22549 MW; 9454D6D6DF44B907 CRC64;
MNYLSPIEKF LIIGLGNPGY LYRKTRHNLG FMILDQISKK YRFSFSKKKL GFISEFIYND
KLLFFLKPST YMNRSGEAVK YWMIKEKIIL KNILIISDDI YLNFGSFRLR EKGGSGGHNG
LKNIEIEIGT THYARLRFGI KKNHFDQKID SYVLENWKDE EIDDLFSKLD IGIKIIFSFV
TNGLQKTMNL FN
//