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PTH_VIBCH
ID   PTH_VIBCH               Reviewed;         196 AA.
AC   Q9KQ21;
DT   01-JUN-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 121.
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=VC_2184;
OS   Vibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=243277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 39315 / El Tor Inaba N16961;
RX   PubMed=10952301; DOI=10.1038/35020000;
RA   Heidelberg J.F., Eisen J.A., Nelson W.C., Clayton R.A., Gwinn M.L.,
RA   Dodson R.J., Haft D.H., Hickey E.K., Peterson J.D., Umayam L.A., Gill S.R.,
RA   Nelson K.E., Read T.D., Tettelin H., Richardson D.L., Ermolaeva M.D.,
RA   Vamathevan J.J., Bass S., Qin H., Dragoi I., Sellers P., McDonald L.A.,
RA   Utterback T.R., Fleischmann R.D., Nierman W.C., White O., Salzberg S.L.,
RA   Smith H.O., Colwell R.R., Mekalanos J.J., Venter J.C., Fraser C.M.;
RT   "DNA sequence of both chromosomes of the cholera pathogen Vibrio
RT   cholerae.";
RL   Nature 406:477-483(2000).
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; AE003852; AAF95329.1; -; Genomic_DNA.
DR   PIR; C82107; C82107.
DR   RefSeq; NP_231815.1; NC_002505.1.
DR   RefSeq; WP_000081944.1; NZ_LT906614.1.
DR   PDB; 4Z86; X-ray; 1.63 A; A/B=2-196.
DR   PDB; 4ZXP; X-ray; 1.63 A; A/B=2-196.
DR   PDB; 5B6J; X-ray; 2.43 A; A/B=2-196.
DR   PDB; 5EKT; X-ray; 1.63 A; A/B=2-196.
DR   PDB; 5IKE; X-ray; 2.09 A; A/B=2-196.
DR   PDB; 5IMB; X-ray; 2.40 A; A/B=2-196.
DR   PDB; 5IVP; X-ray; 2.01 A; A/B=2-196.
DR   PDB; 5ZK0; X-ray; 2.55 A; A/B=2-196.
DR   PDBsum; 4Z86; -.
DR   PDBsum; 4ZXP; -.
DR   PDBsum; 5B6J; -.
DR   PDBsum; 5EKT; -.
DR   PDBsum; 5IKE; -.
DR   PDBsum; 5IMB; -.
DR   PDBsum; 5IVP; -.
DR   PDBsum; 5ZK0; -.
DR   AlphaFoldDB; Q9KQ21; -.
DR   BMRB; Q9KQ21; -.
DR   SMR; Q9KQ21; -.
DR   STRING; 243277.VC_2184; -.
DR   DNASU; 2613320; -.
DR   EnsemblBacteria; AAF95329; AAF95329; VC_2184.
DR   KEGG; vch:VC_2184; -.
DR   PATRIC; fig|243277.26.peg.2082; -.
DR   eggNOG; COG0193; Bacteria.
DR   HOGENOM; CLU_062456_3_1_6; -.
DR   OMA; HVLSKFH; -.
DR   BioCyc; VCHO:VC2184-MON; -.
DR   BRENDA; 3.1.1.29; 15862.
DR   Proteomes; UP000000584; Chromosome 1.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0004045; F:aminoacyl-tRNA hydrolase activity; IBA:GO_Central.
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   1: Evidence at protein level;
KW   3D-structure; Cytoplasm; Hydrolase; Reference proteome.
FT   CHAIN           1..196
FT                   /note="Peptidyl-tRNA hydrolase"
FT                   /id="PRO_0000187850"
FT   STRAND          6..10
FT                   /evidence="ECO:0007829|PDB:4Z86"
FT   TURN            16..20
FT                   /evidence="ECO:0007829|PDB:4Z86"
FT   HELIX           22..24
FT                   /evidence="ECO:0007829|PDB:4Z86"
FT   HELIX           25..36
FT                   /evidence="ECO:0007829|PDB:4Z86"
FT   STRAND          42..44
FT                   /evidence="ECO:0007829|PDB:4Z86"
FT   HELIX           45..47
FT                   /evidence="ECO:0007829|PDB:4Z86"
FT   STRAND          49..56
FT                   /evidence="ECO:0007829|PDB:4Z86"
FT   STRAND          59..66
FT                   /evidence="ECO:0007829|PDB:4Z86"
FT   HELIX           70..72
FT                   /evidence="ECO:0007829|PDB:4Z86"
FT   HELIX           73..83
FT                   /evidence="ECO:0007829|PDB:4Z86"
FT   HELIX           88..90
FT                   /evidence="ECO:0007829|PDB:4Z86"
FT   STRAND          91..97
FT                   /evidence="ECO:0007829|PDB:4Z86"
FT   STRAND          105..109
FT                   /evidence="ECO:0007829|PDB:4Z86"
FT   HELIX           117..125
FT                   /evidence="ECO:0007829|PDB:4Z86"
FT   TURN            126..128
FT                   /evidence="ECO:0007829|PDB:4Z86"
FT   STRAND          132..138
FT                   /evidence="ECO:0007829|PDB:4Z86"
FT   HELIX           145..147
FT                   /evidence="ECO:0007829|PDB:4Z86"
FT   HELIX           148..152
FT                   /evidence="ECO:0007829|PDB:4Z86"
FT   HELIX           158..181
FT                   /evidence="ECO:0007829|PDB:4Z86"
FT   HELIX           183..190
FT                   /evidence="ECO:0007829|PDB:4Z86"
FT   TURN            193..195
FT                   /evidence="ECO:0007829|PDB:5ZK0"
SQ   SEQUENCE   196 AA;  21483 MW;  6D5F7C3D6E4F6304 CRC64;
     MSQPIKLLVG LANPGPEYAK TRHNAGAWVV EELARIHNVT LKNEPKFFGL TGRLLINSQE
     LRVLIPTTFM NLSGKAIAAL ANFYQIKPEE IMVAHDELDL PPGVAKFKQG GGHGGHNGLK
     DTISKLGNNK EFYRLRLGIG HPGHKDKVAG YVLGKAPAKE QECLDAAVDE SVRCLEILMK
     DGLTKAQNRL HTFKAE
 
 
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