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Database: UniProt
Entry: C6S660_NEIML
LinkDB: C6S660_NEIML
Original site: C6S660_NEIML 
ID   C6S660_NEIML            Unreviewed;       192 AA.
AC   C6S660;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   27-MAR-2024, entry version 70.
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:CBA04985.1};
GN   OrderedLocusNames=NMO_0683 {ECO:0000313|EMBL:CBA04985.1};
OS   Neisseria meningitidis (strain alpha14).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=662598 {ECO:0000313|EMBL:CBA04985.1, ECO:0000313|Proteomes:UP000002054};
RN   [1] {ECO:0000313|EMBL:CBA04985.1, ECO:0000313|Proteomes:UP000002054}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=alpha14 {ECO:0000313|Proteomes:UP000002054};
RX   PubMed=18305155; DOI=10.1073/pnas.0800151105;
RA   Schoen C., Blom J., Claus H., Schramm-Glueck A., Brandt P., Mueller T.,
RA   Goesmann A., Joseph B., Konietzny S., Kurzai O., Schmitt C., Friedrich T.,
RA   Linke B., Vogel U., Frosch M.;
RT   "Whole-genome comparison of disease and carriage strains provides insights
RT   into virulence evolution in Neisseria meningitidis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:3473-3478(2008).
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; AM889136; CBA04985.1; -; Genomic_DNA.
DR   RefSeq; WP_002221185.1; NC_013016.1.
DR   AlphaFoldDB; C6S660; -.
DR   SMR; C6S660; -.
DR   KEGG; nmi:NMO_0683; -.
DR   HOGENOM; CLU_062456_3_1_4; -.
DR   Proteomes; UP000002054; 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;  21474 MW;  11ED239E968CFCA7 CRC64;
     MSNTIKMVVG LGNPGKEYEQ TRHNAGFWFL DELAWKWKAS FKEEKKFFGE VARAALPDGD
     VWLLKPATFM NRSGQAVAAL AQFYKIKPEE ILVVHDELDI PCGRIKFKLG GGNGGHNGLK
     DIQAKLGTAD YYRLRLGIGH PGDRNLVVGY VLNKPSTEHR RQIDDAVAKS LQAIPDILAG
     KWEEATRFLH SK
//
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