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Database: UniProt
Entry: M4ZU39_9FLAO
LinkDB: M4ZU39_9FLAO
Original site: M4ZU39_9FLAO 
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
//
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