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Protein

Methionyl-tRNA formyltransferase

Gene

fmt

Organism
Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Experimental evidence at protein leveli

Functioni

Modifies the free amino group of the aminoacyl moiety of methionyl-tRNA(fMet). The formyl group appears to play a dual role in the initiator identity of N-formylmethionyl-tRNA by: (I) promoting its recognition by IF2 and (II) impairing its binding to EFTu-GTP (By similarity).By similarity

Catalytic activityi

10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet).

GO - Molecular functioni

  • methionyl-tRNA formyltransferase activity Source: PseudoCAP

GO - Biological processi

  • regulation of transmembrane transporter activity Source: PseudoCAP

Keywordsi

Molecular functionTransferase
Biological processProtein biosynthesis

Names & Taxonomyi

Protein namesi
Recommended name:
Methionyl-tRNA formyltransferase (EC:2.1.2.9)
Gene namesi
Name:fmt
Ordered Locus Names:PA0018
OrganismiPseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
Taxonomic identifieri208964 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas
Proteomesi
  • UP000002438 Componenti: Chromosome

Organism-specific databases

PseudoCAPiPA0018.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000830171 – 314Methionyl-tRNA formyltransferaseAdd BLAST314

Proteomic databases

PaxDbiO85732.

Interactioni

Protein-protein interaction databases

STRINGi208964.PA0018.

Structurei

Secondary structure

1314
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 11Combined sources6
Helixi14 – 24Combined sources11
Beta strandi26 – 34Combined sources9
Beta strandi42 – 45Combined sources4
Helixi51 – 58Combined sources8
Beta strandi69 – 71Combined sources3
Helixi72 – 79Combined sources8
Beta strandi84 – 90Combined sources7
Helixi97 – 100Combined sources4
Beta strandi107 – 113Combined sources7
Turni115 – 118Combined sources4
Beta strandi119 – 121Combined sources3
Helixi123 – 129Combined sources7
Beta strandi133 – 141Combined sources9
Beta strandi151 – 158Combined sources8
Helixi165 – 188Combined sources24
Helixi199 – 201Combined sources3
Turni210 – 213Combined sources4
Helixi221 – 230Combined sources10
Turni231 – 235Combined sources5
Beta strandi237 – 241Combined sources5
Beta strandi244 – 254Combined sources11
Beta strandi262 – 267Combined sources6
Beta strandi270 – 274Combined sources5
Beta strandi276 – 286Combined sources11
Helixi295 – 299Combined sources5
Helixi304 – 306Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5UAIX-ray2.75A/B/C/D1-314[»]
ProteinModelPortaliO85732.
SMRiO85732.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni113 – 116Tetrahydrofolate (THF) bindingBy similarity4

Sequence similaritiesi

Belongs to the Fmt family.Curated

Phylogenomic databases

eggNOGiENOG4105CAE. Bacteria.
COG0223. LUCA.
HOGENOMiHOG000261177.
InParanoidiO85732.
KOiK00604.
OMAiLRIVFMG.
PhylomeDBiO85732.

Family and domain databases

Gene3Di3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
HAMAPiMF_00182. Formyl_trans. 1 hit.
InterProiView protein in InterPro
IPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
IPR001555. GART_AS.
PfamiView protein in Pfam
PF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
SUPFAMiSSF50486. SSF50486. 1 hit.
SSF53328. SSF53328. 1 hit.
TIGRFAMsiTIGR00460. fmt. 1 hit.
PROSITEiView protein in PROSITE
PS00373. GART. 1 hit.

Sequencei

Sequence statusi: Complete.

O85732-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSQALRIVFA GTPEFAAEHL KALLDTPHRI VAVYTQPDRP AGRGQKLMPS
60 70 80 90 100
AVKSLALEHG LPVMQPQSLR NAEAQAELAA LRADLMVVVA YGLILPQAVL
110 120 130 140 150
DIPRLGCINS HASLLPRWRG AAPIQRAVEA GDAESGVTVM QMEAGLDTGP
160 170 180 190 200
MLLKVSTPIS AADTGGSLHD RLAALGPKAV IEAIAGLAAG TLHGEIQDDA
210 220 230 240 250
LATYAHKLNK DEARLDWSRP AVELERQVRA FTPWPVCHTS LADAPLKVLG
260 270 280 290 300
ASLGQGSGAP GTILEASRDG LLVACGEGAL RLTRLQLPGG KPLAFADLYN
310
SRREQFAAGQ VLGQ
Length:314
Mass (Da):33,028
Last modified:November 1, 1998 - v1
Checksum:iEA1570CDCD61F269
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF073952 Genomic DNA. Translation: AAC26787.1.
AE004091 Genomic DNA. Translation: AAG03408.1.
PIRiG83643.
RefSeqiNP_248708.1. NC_002516.2.
WP_003114642.1. NC_002516.2.

Genome annotation databases

EnsemblBacteriaiAAG03408; AAG03408; PA0018.
GeneIDi879258.
KEGGipae:PA0018.
PATRICifig|208964.12.peg.17.

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

Entry informationi

Entry nameiFMT_PSEAE
AccessioniPrimary (citable) accession number: O85732
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1998
Last modified: June 7, 2017
This is version 112 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families