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Q81WH2 (FMT_BACAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 77. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Methionyl-tRNA formyltransferase
EC=2.1.2.9
Gene names
Name:fmt
Ordered Locus Names:BA_4004, GBAA_4004, BAS3717
OrganismBacillus anthracis [Reference proteome] [HAMAP]
Taxonomic identifier1392 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group

Protein attributes

Sequence length314 AA.
Sequence statusComplete.
Protein existenceEvidence 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 By similarity. HAMAP-Rule MF_00182

Catalytic activity

10-formyltetrahydrofolate + L-methionyl-tRNA(fMet) = tetrahydrofolate + N-formylmethionyl-tRNA(fMet). HAMAP-Rule MF_00182

Sequence similarities

Belongs to the fmt family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 314314Methionyl-tRNA formyltransferase HAMAP-Rule MF_00182
PRO_0000082910

Regions

Region110 – 1134Tetrahydrofolate (THF) binding By similarity

Secondary structure

1 ................................................ 314
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q81WH2 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 8E81D02492DABEE2

FASTA31434,736
        10         20         30         40         50         60 
MIKVVFMGTP DFSVPVLRRL IEDGYDVIGV VTQPDRPVGR KKVLTPTPVK VEAEKHGIPV 

        70         80         90        100        110        120 
LQPLRIREKD EYEKVLALEP DLIVTAAFGQ IVPNEILEAP KYGCINVHAS LLPELRGGAP 

       130        140        150        160        170        180 
IHYAIMEGKE KTGITIMYMV EKLDAGDILT QVEVEIEERE TTGSLFDKLS EAGAHLLSKT 

       190        200        210        220        230        240 
VPLLIQGKLE PIKQNEEEVT FAYNIKREQE KIDWTKTGEE VYNHIRGLNP WPVAYTTLAG 

       250        260        270        280        290        300 
QVVKVWWGEK VPVTKSAEAG TIVAIEEDGF VVATGNETGV KITELQPSGK KRMSCSQFLR 

       310 
GTKPEIGTKL GENA

« Hide

References

[1]"The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria."
Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T., Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R., Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M., Kolonay J.F., Beanan M.J., Dodson R.J. expand/collapse author list , Brinkac L.M., Gwinn M.L., DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C., Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y., Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M., Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E., White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M., Hanna P.C., Kolstoe A.-B., Fraser C.M.
Nature 423:81-86(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames / isolate Porton.
[2]"The complete genome sequence of Bacillus anthracis Ames 'Ancestor'."
Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D., Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.
J. Bacteriol. 191:445-446(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Ames ancestor.
[3]"Complete genome sequence of Bacillus anthracis Sterne."
Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K., Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R., Richardson P., Rubin E., Tice H.
Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sterne.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016879 Genomic DNA. Translation: AAP27732.1.
AE017334 Genomic DNA. Translation: AAT33120.1.
AE017225 Genomic DNA. Translation: AAT56019.1.
RefSeqNP_846246.1. NC_003997.3.
YP_020645.1. NC_007530.2.
YP_029968.1. NC_005945.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4IQFX-ray2.40A/B/C/D1-314[»]
ProteinModelPortalQ81WH2.
ModBaseSearch...

Protein-protein interaction databases

STRING198094.BA_4004.

Protocols and materials databases

DNASU1086742.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAP27732; AAP27732; BA_4004.
AAT33120; AAT33120; GBAA_4004.
AAT56019; AAT56019; BAS3717.
GeneID1086742.
2816238.
2852995.
KEGGban:BA_4004.
bar:GBAA_4004.
bat:BAS3717.

Phylogenomic databases

eggNOGCOG0223.
HOGENOMHOG000261177.
KOK00604.
OMAGITLMQM.
ProtClustDBPRK00005.

Enzyme and pathway databases

BioCycBANT260799:GJAJ-3775-MONOMER.
BANT261594:GJ7F-3892-MONOMER.

Family and domain databases

Gene3D3.10.25.10. 1 hit.
3.40.50.170. 1 hit.
HAMAPMF_00182. Formyl_trans.
InterProIPR005794. Fmt.
IPR005793. Formyl_trans_C.
IPR002376. Formyl_transf_N.
IPR011034. Formyl_transferase_C-like.
IPR001555. GART_AS.
IPR015518. Met_tRNA_Form_TA-like.
[Graphical view]
PANTHERPTHR11138. PTHR11138. 1 hit.
PfamPF02911. Formyl_trans_C. 1 hit.
PF00551. Formyl_trans_N. 1 hit.
[Graphical view]
SUPFAMSSF50486. FMT_C_like. 1 hit.
SSF53328. formyl_transf. 1 hit.
TIGRFAMsTIGR00460. fmt. 1 hit.
PROSITEPS00373. GART. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameFMT_BACAN
AccessionPrimary (citable) accession number: Q81WH2
Secondary accession number(s): Q6HUM0, Q6KNV4
Entry history
Integrated into UniProtKB/Swiss-Prot: August 4, 2003
Last sequence update: June 1, 2003
Last modified: May 1, 2013
This is version 77 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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