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Protein

tRNA(Met) cytidine acetyltransferase TmcA

Gene

tmcA

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the formation of N4-acetylcytidine (ac4C) at the wobble position of tRNA(Met), by using acetyl-CoA as an acetyl donor and ATP (or GTP). It recognizes the wobble base of tRNA(Met), thus distinguishing between tRNA(Met) and the structurally similar tRNA(Ile2).UniRule annotation2 Publications

Miscellaneous

Could use an RNA helicase motor driven by ATP hydrolysis to deliver the wobble base of tRNA(Met) to the acetyltransferase domain of TmcA.1 Publication

Catalytic activityi

(Elongator tRNA(Met))-cytidine(34) + ATP + acetyl-CoA + H2O = (elongator tRNA(Met))-N4-acetylcytidine(34) + ADP + phosphate + CoA.UniRule annotation2 Publications

Enzyme regulationi

ATP/GTP hydrolysis is stimulated by the addition of acetyl-CoA and tRNA(Met). Binding of acetyl-CoA to TmcA activates both ATPase and tRNA-binding activities.2 Publications

Kineticsi

  1. KM=2.93 µM for ATP (in the absence of both acetyl-CoA and tRNA(Met))1 Publication
  2. KM=4.16 µM for ATP (in the presence of both acetyl-CoA and tRNA(Met))1 Publication
  3. KM=117 µM for GTP (in the absence of both acetyl-CoA and tRNA(Met))1 Publication
  4. KM=66.6 µM for GTP (in the presence of both acetyl-CoA and tRNA(Met))1 Publication

    Sites

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Binding sitei180ATPUniRule annotation1 Publication1
    Binding sitei319ATPUniRule annotation1 Publication1
    Binding sitei499Acetyl-CoAUniRule annotation1 Publication1
    Binding sitei506Acetyl-CoAUniRule annotation1 Publication1

    Regions

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Nucleotide bindingi202 – 211ATPUniRule annotation1 Publication10

    GO - Molecular functioni

    • ATP binding Source: UniProtKB-KW
    • rRNA cytidine N-acetyltransferase activity Source: GO_Central
    • tRNA binding Source: EcoCyc
    • tRNA N-acetyltransferase activity Source: EcoCyc

    GO - Biological processi

    • rRNA acetylation involved in maturation of SSU-rRNA Source: GO_Central
    • tRNA acetylation Source: EcoCyc
    • tRNA wobble cytosine modification Source: EcoCyc

    Keywordsi

    Molecular functionAcyltransferase, RNA-binding, Transferase, tRNA-binding
    Biological processtRNA processing
    LigandATP-binding, Nucleotide-binding

    Enzyme and pathway databases

    BioCyciEcoCyc:G7297-MONOMER
    MetaCyc:G7297-MONOMER
    BRENDAi2.3.1.193 2026

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    tRNA(Met) cytidine acetyltransferase TmcAUniRule annotation (EC:2.3.1.193UniRule annotation)
    Gene namesi
    Name:tmcAUniRule annotation
    Synonyms:ypfI
    Ordered Locus Names:b2474, JW2459
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
    Proteomesi

    Organism-specific databases

    EcoGeneiEG14196 tmcA

    Subcellular locationi

    • Cytoplasm UniRule annotation

    GO - Cellular componenti

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Disruption phenotypei

    Mutants lack the ac4C modification, but do not show any growth defects.1 Publication

    Mutagenesis

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Mutagenesisi287T → A: Loss of ATPase activity, but no change in tRNA-binding. 1 Publication1
    Mutagenesisi291Y → A: Loss of ATPase activity, but no change in tRNA-binding. 1 Publication1
    Mutagenesisi292E → A: Loss of ATPase activity, but no change in tRNA-binding. 1 Publication1
    Mutagenesisi296R → A: Decrease in ATPase activity and loss of tRNA-binding. 1 Publication1
    Mutagenesisi301K → A: Decrease in ATPase activity and loss of tRNA-binding. 1 Publication1
    Mutagenesisi319R → A: Loss of ATPase activity, but no change in tRNA-binding. 1 Publication1
    Mutagenesisi327E → A: Loss of ATPase activity, but no change in tRNA-binding. 1 Publication1
    Mutagenesisi377H → A: Decrease in ATPase activity and loss of tRNA-binding. 1 Publication1
    Mutagenesisi387R → A: Abolishes the tRNA-binding capacity, but no loss of activity. 1 Publication1
    Mutagenesisi460R → A: Loss of tRNA-binding. 1 Publication1

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001692391 – 671tRNA(Met) cytidine acetyltransferase TmcAAdd BLAST671

    Proteomic databases

    PaxDbiP76562
    PRIDEiP76562

    Interactioni

    Protein-protein interaction databases

    BioGridi4259195, 20 interactors
    DIPiDIP-12825N
    IntActiP76562, 8 interactors
    STRINGi316385.ECDH10B_2640

    Structurei

    Secondary structure

    1671
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Helixi3 – 17Combined sources15
    Beta strandi21 – 27Combined sources7
    Helixi29 – 42Combined sources14
    Beta strandi48 – 50Combined sources3
    Turni68 – 70Combined sources3
    Beta strandi73 – 79Combined sources7
    Helixi86 – 93Combined sources8
    Beta strandi101 – 107Combined sources7
    Helixi109 – 111Combined sources3
    Turni112 – 114Combined sources3
    Helixi118 – 120Combined sources3
    Helixi121 – 124Combined sources4
    Helixi133 – 143Combined sources11
    Beta strandi145 – 153Combined sources9
    Helixi178 – 187Combined sources10
    Beta strandi192 – 199Combined sources8
    Helixi205 – 215Combined sources11
    Beta strandi216 – 218Combined sources3
    Beta strandi220 – 223Combined sources4
    Helixi231 – 237Combined sources7
    Helixi238 – 240Combined sources3
    Helixi246 – 251Combined sources6
    Beta strandi257 – 262Combined sources6
    Helixi264 – 266Combined sources3
    Helixi269 – 276Combined sources8
    Beta strandi279 – 290Combined sources12
    Helixi296 – 304Combined sources9
    Beta strandi310 – 313Combined sources4
    Beta strandi318 – 320Combined sources3
    Helixi325 – 333Combined sources9
    Helixi339 – 342Combined sources4
    Beta strandi350 – 355Combined sources6
    Helixi358 – 361Combined sources4
    Helixi364 – 376Combined sources13
    Beta strandi377 – 380Combined sources4
    Helixi382 – 390Combined sources9
    Beta strandi394 – 400Combined sources7
    Beta strandi402 – 415Combined sources14
    Helixi419 – 426Combined sources8
    Helixi436 – 444Combined sources9
    Helixi450 – 452Combined sources3
    Beta strandi453 – 463Combined sources11
    Beta strandi469 – 471Combined sources3
    Helixi472 – 482Combined sources11
    Beta strandi488 – 495Combined sources8
    Helixi498 – 506Combined sources9
    Beta strandi510 – 514Combined sources5
    Turni520 – 522Combined sources3
    Beta strandi526 – 532Combined sources7
    Helixi535 – 559Combined sources25
    Helixi575 – 586Combined sources12
    Turni591 – 594Combined sources4
    Helixi595 – 604Combined sources10
    Helixi610 – 617Combined sources8
    Helixi622 – 628Combined sources7
    Helixi634 – 650Combined sources17
    Helixi654 – 666Combined sources13

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2ZPAX-ray2.35A/B1-671[»]
    ProteinModelPortaliP76562
    SMRiP76562
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP76562

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Domaini356 – 531N-acetyltransferaseUniRule annotationAdd BLAST176

    Region

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Regioni461 – 463Acetyl-CoA bindingUniRule annotation1 Publication3
    Regioni468 – 474Acetyl-CoA bindingUniRule annotation1 Publication7

    Sequence similaritiesi

    Belongs to the RNA cytidine acetyltransferase family. TmcA subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiENOG4105E0I Bacteria
    COG1444 LUCA
    HOGENOMiHOG000283762
    InParanoidiP76562
    KOiK06957
    OMAiMRIAVHP

    Family and domain databases

    Gene3Di1.20.120.890, 1 hit
    HAMAPiMF_01886 tRNA_acetyltr_TmcA, 1 hit
    InterProiView protein in InterPro
    IPR016181 Acyl_CoA_acyltransferase
    IPR000182 GNAT_dom
    IPR007807 Helicase_dom
    IPR027417 P-loop_NTPase
    IPR032672 TmcA/NAT10/Kre33
    IPR038321 TmcA_C_sf
    IPR013562 TmcA_N
    IPR033442 TmcA_tRNA_bind
    IPR024914 tRNA_acetyltr_TmcA
    PANTHERiPTHR10925 PTHR10925, 1 hit
    PTHR10925:SF6 PTHR10925:SF6, 1 hit
    PfamiView protein in Pfam
    PF08351 DUF1726, 1 hit
    PF13718 GNAT_acetyltr_2, 1 hit
    PF05127 Helicase_RecD, 1 hit
    PF17176 tRNA_bind_3, 1 hit
    SUPFAMiSSF52540 SSF52540, 1 hit
    SSF55729 SSF55729, 2 hits
    PROSITEiView protein in PROSITE
    PS51186 GNAT, 1 hit

    Sequencei

    Sequence statusi: Complete.

    P76562-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MAELTALHTL TAQMKREGIR RLLVLSGEEG WCFEHTLKLR DALPGDWLWI
    60 70 80 90 100
    SPRPDAENHC SPSALQTLLG REFRHAVFDA RHGFDAAAFA ALSGTLKAGS
    110 120 130 140 150
    WLVLLLPVWE EWENQPDADS LRWSDCPDPI ATPHFVQHLK RVLTADNEAI
    160 170 180 190 200
    LWRQNQPFSL AHFTPRTDWY PATGAPQPEQ QQLLKQLMTM PPGVAAVTAA
    210 220 230 240 250
    RGRGKSALAG QLISRIAGRA IVTAPAKAST DVLAQFAGEK FRFIAPDALL
    260 270 280 290 300
    ASDEQADWLV VDEAAAIPAP LLHQLVSRFP RTLLTTTVQG YEGTGRGFLL
    310 320 330 340 350
    KFCARFPHLH RFELQQPIRW AQGCPLEKMV SEALVFDDEN FTHTPQGNIV
    360 370 380 390 400
    ISAFEQTLWQ SDPETPLKVY QLLSGAHYRT SPLDLRRMMD APGQHFLQAA
    410 420 430 440 450
    GENEIAGALW LVDEGGLSQQ LSQAVWAGFR RPRGNLVAQS LAAHGNNPLA
    460 470 480 490 500
    ATLRGRRVSR IAVHPARQRE GTGRQLIAGA LQYTQDLDYL SVSFGYTGEL
    510 520 530 540 550
    WRFWQRCGFV LVRMGNHREA SSGCYTAMAL LPMSDAGKQL AEREHYRLRR
    560 570 580 590 600
    DAQALAQWNG ETLPVDPLND AVLSDDDWLE LAGFAFAHRP LLTSLGCLLR
    610 620 630 640 650
    LLQTSELALP ALRGRLQKNA SDAQLCTTLK LSGRKMLLVR QREEAAQALF
    660 670
    ALNDVRTERL RDRITQWQLF H
    Length:671
    Mass (Da):74,893
    Last modified:February 1, 1997 - v1
    Checksum:i07C5A019570CDA5D
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    U00096 Genomic DNA Translation: AAC75527.1
    AP009048 Genomic DNA Translation: BAA16352.2
    PIRiA65023
    RefSeqiNP_416969.1, NC_000913.3
    WP_000829360.1, NZ_LN832404.1

    Genome annotation databases

    EnsemblBacteriaiAAC75527; AAC75527; b2474
    BAA16352; BAA16352; BAA16352
    GeneIDi946053
    KEGGiecj:JW2459
    eco:b2474
    PATRICifig|1411691.4.peg.4265

    Entry informationi

    Entry nameiTMCA_ECOLI
    AccessioniPrimary (citable) accession number: P76562
    Secondary accession number(s): P76972
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: February 1, 1997
    Last modified: March 28, 2018
    This is version 128 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

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