ACL_RS00920

Uniprot: A9NEN4
Description: elongation factor Tu
EC number:
Annotation score: 2 out of 5
Miscellaneous [CC]:
Protein existence: Inferred from homology
Catalytic activity:
Cofactor:
Enzyme regulation:
Function [CC]: FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-tRNA to the A-site of ribosomes during protein biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00118}.
Pathway:
Active site:
Binding site:
Calcium binding:
DNA binding:
Metal binding:
Nucleotide binding: NP_BIND 19 26 GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.; NP_BIND 81 85 GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.; NP_BIND 136 139 GTP. {ECO:0000255|HAMAP-Rule:MF_00118}.
Site:
Gene names (primary): tuf
Gene names (synonym):
Mass: 42,851
Subunit structure [CC]: SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00118}.
Gene ontology (GO): cytoplasm [GO:0005737]; GTP binding [GO:0005525]; GTPase activity [GO:0003924]; translation elongation factor activity [GO:0003746]
Gene ontology IDs: GO:0003746; GO:0003924; GO:0005525; GO:0005737
Chain: CHAIN 1 395 Elongation factor Tu. /FTId=PRO_1000076092.
Signal peptide:
Domain [CC]:
Sequence similarities: SIMILARITY: Belongs to the TRAFAC class translation factor GTPase superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A subfamily. {ECO:0000255|HAMAP-Rule:MF_00118}.; SIMILARITY: Contains 1 tr-type G (guanine nucleotide-binding) domain. {ECO:0000305}.
Protein families: TRAFAC class translation factor GTPase superfamily, Classic translation factor GTPase family, EF-Tu/EF-1A subfamily
Coiled coil:
Domain [FT]: DOMAIN 10 204 tr-type G.
Motif:
Region: REGION 19 26 G1. {ECO:0000250}.; REGION 60 64 G2. {ECO:0000250}.; REGION 81 84 G3. {ECO:0000250}.; REGION 136 139 G4. {ECO:0000250}.; REGION 174 176 G5. {ECO:0000250}.
EMBL: CP000896
ProteinModelPortal: A9NEN4
MEROPS:
EnsemblBacteria KO: ABX80814
UniPathway: K02358
CDD:
Gene3D: cd03697
HAMAP: 3.40.50.300
InterPro: MF_00118_B
PANTHER: IPR004161;IPR033720;IPR031157;IPR027417;IPR005225;IPR000795;IPR009000;IPR009001;IPR004541;IPR004160
PIRSF:
PRINTS:
PROSITE: PR00315
Pfam: PS00301;PS51722
ProDom: PF03144;PF03143
SMART:
SUPFAM:
TIGRFAMs: SSF50447;SSF50465;SSF52540

181290-182478(+)

>nucleotide sequence
ATGGCAAAACAAAAATTCGAAAGAACAAAACCACACGTTAACGTTGGAACAATCGGACAC
GTTGACCATGGTAAAACTACATTAACTGCTGCAATTACATCAGTACTTGCAGGAAAAGGT
TTAGCTACAAAAAGAGATTATAACCAAATCGATGGTGCACCAGAAGAAAAAGCTCGTGGT
ATAACTATTAACGCATCTCACGTTGAGTATGAAACTGTAAACAGACACTACGCTCACGTA
GACTGCCCAGGTCACGCTGACTATGTTAAAAACATGATTACAGGTGCTGCTCAAATGGAC
GGTGCTATCTTAGTTGTTTCTGCAGCGGATGGTCCAATGCCACAAACTCGTGAACATATT
CTTTTATCACGCCAAGTTGGGGTACCTAAATTAGTAGTATTCTTAAACAAAGCTGACTTA
GTTGATGACGAAGAGTTATTAGACTTAGTTGAAATGGAAGTTAGAGAATTATTATCAGAA
TATGATTTCCCAGGAGATGATATTCCAGTAATTAAAGGATCTGCTTTAGGCGCTTTAGAA
GGTAAACCAGAATGGGTTGCTAAAGTTGAAGAATTAATGGATGCAGTTGATGCATACATC
GATACTCCATTACGTGCTACTGACAAACCATTTATGATGCCAGTTGAAGACGTATTCACA
ATTACAGGTCGTGGTACAGTTGCTACAGGACGTGTTGATCGTGGTATCGTTAAAGTTGGT
GACCAAGTTGAAATCGTTGGTATTACTGATACTAAAACTACAACTGTTACAGGTGTAGAA
ATGTTTAGAAAATTATTAGACCAAGCTGAAGCTGGAGACAACATCGGTGCTTTATTAAGA
GGTGTTGATCGTGAAGGTGTAGAACGTGGTCAAGTATTATCAAAACCAGGTACAGTTAAA
CCTCATGCTAAATTCACTGCTCAAATTTATGTATTAAGTAAAGAAGAAGGTGGACGCCAT
ACAGCGTTCTTCTCAAACTATCGTCCTCAATTCTACTTCAGAACTACAGACATCACAGGT
ATCATCACTTTAGGTGAAGGTACTGAAATGGTTATGCCAGGTGATAACGCTGAAGTTACA
GTAGAACTTATTCACCCAATCGCGCTTGAAGAAGGTACAAAATTCTCAATCCGCGAAGGT
GGTAGAACAGTTGCTTCTGGATCAGTAGTTAAAATTCTTGCTGACTAA

>protein sequence
MAKQKFERTKPHVNVGTIGHVDHGKTTLTAAITSVLAGKGLATKRDYNQIDGAPEEKARG
ITINASHVEYETVNRHYAHVDCPGHADYVKNMITGAAQMDGAILVVSAADGPMPQTREHI
LLSRQVGVPKLVVFLNKADLVDDEELLDLVEMEVRELLSEYDFPGDDIPVIKGSALGALE
GKPEWVAKVEELMDAVDAYIDTPLRATDKPFMMPVEDVFTITGRGTVATGRVDRGIVKVG
DQVEIVGITDTKTTTVTGVEMFRKLLDQAEAGDNIGALLRGVDREGVERGQVLSKPGTVK
PHAKFTAQIYVLSKEEGGRHTAFFSNYRPQFYFRTTDITGIITLGEGTEMVMPGDNAEVT
VELIHPIALEEGTKFSIREGGRTVASGSVVKILAD