Reviewed, UniProtKB/Swiss-Prot P23882 (FMT_ECOLI)

Names and origin

Protein names

Recommended name:
    Methionyl-tRNA formyltransferase
    EC=2.1.2.9

Gene names

Name:	fmt
Synonyms:	yhdD
Ordered Locus Names:	b3288, JW3249

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	315 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	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. HAMAP MF_00182
Catalytic activity	10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) + H2O = tetrahydrofolate + N-formylmethionyl-tRNA(fMet). HAMAP MF_00182
Subunit structure	Monomer. HAMAP MF_00182
Domain	Composed of an N- and a C-terminal domain. The N-terminal domain carries the tetrahydrofolate (THF)-binding site and the C-terminal domain is presumably involved in positioning the Met-tRNA substrate for the formylation reaction. HAMAP MF_00182
Sequence similarities	Belongs to the fmt family.

Ontologies

Keywords
Biological process	Protein biosynthesis
Molecular function	Methyltransferase Transferase
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	translation Inferred from electronic annotation. Source: HAMAP
Molecular function	methionyl-tRNA formyltransferase activity Inferred from electronic annotation. Source: HAMAP
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed HAMAP MF_00182

Chain

2 – 315

314

Methionyl-tRNA formyltransferase HAMAP MF_00182

PRO_0000082959

Regions

Region

2 – 189

188

N-terminal domain HAMAP MF_00182

Region

113 – 116

4

Tetrahydrofolate (THF) binding HAMAP MF_00182

Region

210 – 315

106

C-terminal domain HAMAP MF_00182

Secondary structure

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315

Helix Strand Turn

Details...

Beta strand

6 – 11

6

Helix

14 – 25

12

Beta strand

29 – 34

6

Helix

51 – 58

8

Helix

72 – 80

9

Beta strand

84 – 90

7

Helix

97 – 101

5

Beta strand

107 – 114

8

Turn

115 – 118

4

Beta strand

119 – 121

3

Helix

123 – 130

8

Beta strand

133 – 141

9

Beta strand

144 – 147

4

Beta strand

151 – 158

8

Helix

165 – 189

25

Helix

199 – 201

3

Helix

210 – 213

4

Helix

221 – 230

10

Turn

231 – 235

5

Beta strand

237 – 241

5

Beta strand

244 – 254

11

Beta strand

264 – 269

6

Beta strand

272 – 276

5

Beta strand

278 – 289

12

Helix

297 – 303

7

Helix

305 – 307

3

Sequences

	Sequence		Length	Mass (Da)
	P23882-1 [UniParc]. Last modified January 23, 2007. Version 4. Checksum: 1AE14C808F04A126	FASTA	315	34,168
	10 20 30 40 50 60 MSESLRIIFA GTPDFAARHL DALLSSGHNV VGVFTQPDRP AGRGKKLMPS PVKVLAEEKG 70 80 90 100 110 120 LPVFQPVSLR PQENQQLVAE LQADVMVVVA YGLILPKAVL EMPRLGCINV HGSLLPRWRG 130 140 150 160 170 180 AAPIQRSLWA GDAETGVTIM QMDVGLDTGD MLYKLSCPIT AEDTSGTLYD KLAELGPQGL 190 200 210 220 230 240 ITTLKQLADG TAKPEVQDET LVTYAEKLSK EEARIDWSLS AAQLERCIRA FNPWPMSWLE 250 260 270 280 290 300 IEGQPVKVWK ASVIDTATNA APGTILEANK QGIQVATGDG ILNLLSLQPA GKKAMSAQDL 310 LNSRREWFVP GNRLV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Disruption of the gene for Met-tRNA(fMet) formyltransferase severely impairs growth of Escherichia coli." Guillon J.-M., Mechulam Y., Schmitter J.-M., Blanquet S., Fayat G. J. Bacteriol. 174:4294-4301(1992) [PubMed: 1624424] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: K12 / K37.
[2]	"The Escherichia coli fmt gene, encoding methionyl-tRNA(fMet) formyltransferase, escapes metabolic control." Meinnel T., Guillon J.-M., Mechulam Y., Blanquet S. J. Bacteriol. 175:993-1000(1993) [PubMed: 8432722] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: K12 / K37.
[3]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[4]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[5]	"Genetic characterization of polypeptide deformylase, a distinctive enzyme of eubacterial translation." Mazel D., Pochet S., Marliere P. EMBO J. 13:914-923(1994) [PubMed: 8112305] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-82.
[6]	"Nucleotide sequence of the rpoA-rplQ DNA of Escherichia coli: a second regulatory binding site for protein S4?" Meek D.W., Hayward R.S. Nucleic Acids Res. 12:5813-5821(1984) [PubMed: 6379605] [Abstract] Cited for: PRELIMINARY NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 82-162.
[7]	"A survey of polypeptide deformylase function throughout the eubacterial lineage." Mazel D., Coic E., Blanchard S., Saurin W., Marliere P. J. Mol. Biol. 266:939-949(1997) [PubMed: 9086272] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 161-315. Strain: K12 / MG1655 / ATCC 47076.
[8]	"Structure of crystalline Escherichia coli methionyl-tRNA(f)Met formyltransferase: comparison with glycinamide ribonucleotide formyltransferase." Schmitt E., Blanquet S., Mechulam Y. EMBO J. 15:4749-4758(1996) [PubMed: 8887566] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[9]	"Crystal structure of methionyl-tRNAfMet transformylase complexed with the initiator formyl-methionyl-tRNAfMet." Schmitt E., Panvert M., Blanquet S., Mechulam Y. EMBO J. 17:6819-6826(1998) [PubMed: 9843487] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).

Cross-references

Sequence databases

EMBLGenBankDDBJ

X63666 Genomic DNA. Translation: CAA45207.1.
X77091 Genomic DNA. Translation: CAA54368.1.
U18997 Genomic DNA. Translation: AAA58085.1.
U00096 Genomic DNA. Translation: AAC76313.1.
AP009048 Genomic DNA. Translation: BAE78004.1.
X00767 Genomic DNA. Translation: CAA25339.1. Sequence problems.
Y10307 Genomic DNA. Translation: CAA71358.1.

PIR

S23108.

RefSeq

AP_004503.1.
NP_417746.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1FMT	X-ray	2.00	A/B	2-315	[»]
2FMT	X-ray	2.80	A/B	2-315	[»]

ModBase

Search...

2-D gel databases

SWISS-2DPAGE

P23882.

ECO2DBASE

F033.6. 6TH EDITION.

Genome annotation databases

GeneID

947779.

GenomeReviews

Gene locus JW3249 in contig AP009048_GR.
Gene locus b3288 in contig U00096_GR.

KEGG

ecj:JW3249.
eco:b3288.

Organism-specific databases

EchoBASE

EB1247.

EcoGene

EG11268. fmt.

CMR

Search...

Phylogenomic databases

HOGENOM

P23882.

OMA

P23882. PIQRALW.

Enzyme and pathway databases

BioCyc

EcoCyc:EG11268-MON.

Family and domain databases

HAMAP

MF_00182.
[Tree]

InterPro

IPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR001555. GART_AS.
IPR015518. Met_tRNA_Form_TA-like.
[Graphical view]

Gene3D

G3DSA:3.10.25.10. Formyl_trans_C. 1 hit.
G3DSA:3.40.50.170. Formyl_transf_N. 1 hit.

PANTHER

PTHR11138. Met_tRNA_Form_TA-like. 1 hit.

Pfam

PF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
[Graphical view]

TIGRFAMs

TIGR00460. fmt. 1 hit.

PROSITE

PS00373. GART. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

FMT_ECOLI

Accession

Primary (citable) accession number: P23882
Secondary accession number(s): P77040, Q2M6V2

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1991
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 91 of the entry and version 4 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)