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MNMA_STAAE
ID   MNMA_STAAE              Reviewed;         372 AA.
AC   A6QHG3;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=tRNA-specific 2-thiouridylase MnmA {ECO:0000255|HAMAP-Rule:MF_00144};
DE            EC=2.8.1.13 {ECO:0000255|HAMAP-Rule:MF_00144};
GN   Name=mnmA {ECO:0000255|HAMAP-Rule:MF_00144}; Synonyms=trmU;
GN   OrderedLocusNames=NWMN_1523;
OS   Staphylococcus aureus (strain Newman).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=426430;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Newman;
RX   PubMed=17951380; DOI=10.1128/jb.01000-07;
RA   Baba T., Bae T., Schneewind O., Takeuchi F., Hiramatsu K.;
RT   "Genome sequence of Staphylococcus aureus strain Newman and comparative
RT   analysis of staphylococcal genomes: polymorphism and evolution of two major
RT   pathogenicity islands.";
RL   J. Bacteriol. 190:300-310(2008).
CC   -!- FUNCTION: Catalyzes the 2-thiolation of uridine at the wobble position
CC       (U34) of tRNA, leading to the formation of s(2)U34. {ECO:0000255|HAMAP-
CC       Rule:MF_00144}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AH2 + ATP + S-sulfanyl-L-cysteinyl-[protein] + uridine(34) in
CC         tRNA = 2-thiouridine(34) in tRNA + A + AMP + diphosphate + H(+) + L-
CC         cysteinyl-[protein]; Xref=Rhea:RHEA:47032, Rhea:RHEA-COMP:10131,
CC         Rhea:RHEA-COMP:11726, Rhea:RHEA-COMP:11727, Rhea:RHEA-COMP:11728,
CC         ChEBI:CHEBI:13193, ChEBI:CHEBI:15378, ChEBI:CHEBI:17499,
CC         ChEBI:CHEBI:29950, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:61963, ChEBI:CHEBI:65315, ChEBI:CHEBI:87170,
CC         ChEBI:CHEBI:456215; EC=2.8.1.13; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00144};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00144}.
CC   -!- SIMILARITY: Belongs to the MnmA/TRMU family. {ECO:0000255|HAMAP-
CC       Rule:MF_00144}.
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DR   EMBL; AP009351; BAF67795.1; -; Genomic_DNA.
DR   RefSeq; WP_000066097.1; NZ_CP023390.1.
DR   AlphaFoldDB; A6QHG3; -.
DR   SMR; A6QHG3; -.
DR   EnsemblBacteria; BAF67795; BAF67795; NWMN_1523.
DR   KEGG; sae:NWMN_1523; -.
DR   HOGENOM; CLU_035188_1_0_9; -.
DR   OMA; AVCTGHY; -.
DR   Proteomes; UP000006386; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016783; F:sulfurtransferase activity; IEA:InterPro.
DR   GO; GO:0000049; F:tRNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0006400; P:tRNA modification; IEA:UniProtKB-UniRule.
DR   CDD; cd01998; tRNA_Me_trans; 1.
DR   Gene3D; 2.30.30.280; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   HAMAP; MF_00144; tRNA_thiouridyl_MnmA; 1.
DR   InterPro; IPR023382; Adenine_a_hdrlase_dom.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR004506; tRNA-specific_2-thiouridylase.
DR   TIGRFAMs; TIGR00420; trmU; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cytoplasm; Disulfide bond; Nucleotide-binding; RNA-binding;
KW   Transferase; tRNA processing; tRNA-binding.
FT   CHAIN           1..372
FT                   /note="tRNA-specific 2-thiouridylase MnmA"
FT                   /id="PRO_1000071468"
FT   REGION          97..99
FT                   /note="Interaction with target base in tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   REGION          149..151
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   REGION          309..310
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   ACT_SITE        102
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   ACT_SITE        199
FT                   /note="Cysteine persulfide intermediate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   BINDING         11..18
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   BINDING         37
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   BINDING         126
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   SITE            127
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   SITE            342
FT                   /note="Interaction with tRNA"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
FT   DISULFID        102..199
FT                   /note="Alternate"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00144"
SQ   SEQUENCE   372 AA;  42150 MW;  5E8973274B2585D0 CRC64;
     MSNKDIRVVV GMSGGVDSSV TAHVLKEQGY DVIGIFMKNW DDTDENGVCT ATEDYNDVIE
     VCNQIGIPYY AVNFEKEYWD KVFTYFLDEY KKGRTPNPDV MCNKEIKFKA FLDHAMNLGA
     DYVATGHYAR IHRHEDGHVE MLRGVDNNKD QTYFLNQLSQ QQLSKVMFPI GDIEKSEVRR
     IAEEQGLVTA KKKDSTGICF IGEKNFKTFL SQYLPAQPGD MITLDGKKMG KHSGLMYYTI
     GQRHGLGIGG DGDPWFVVGK NLKDNVLYVE QGFHHDALYS DYLIASDYSF VNPEDNDLDQ
     GFECTAKFRY RQKDTKVFVK RENDHALRVT FAEPVRAITP GQAVVFYQGD VCLGGATIDD
     VFKNEGQLNY VV
 
 
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