GCW_01315

Uniprot: A0A0F6CKA9
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:0000256|HAMAP-Rule:MF_00118}.
Pathway:
Active site:
Binding site:
Calcium binding:
DNA binding:
Metal binding:
Nucleotide binding: NP_BIND 19 26 GTP. {ECO:0000256|HAMAP-Rule:MF_00118}.; NP_BIND 81 85 GTP. {ECO:0000256|HAMAP-Rule:MF_00118}.; NP_BIND 136 139 GTP. {ECO:0000256|HAMAP-Rule:MF_00118}.
Site:
Gene names (primary): tuf
Gene names (synonym):
Mass: 43,099
Subunit structure [CC]: SUBUNIT: Monomer. {ECO:0000256|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:
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:0000256|HAMAP-Rule:MF_00118}.
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 (guanine nucleotide-binding). {ECO:0000259|PROSITE:PS51722}.
Motif:
Region:
EMBL: CP006916
ProteinModelPortal: A0A0F6CKA9
MEROPS:
EnsemblBacteria KO: AHB99531
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
308766-309951(+)

>nucleotide sequence
ATGGCAAAAGAAAGGTTCGATCGTAGTAAACCTCACGTTAATATTGGAACAATCGGTCAT
ATTGACCACGGTAAAACTACATTAACCGCAGCAATTTGTACCGTGTTATCAAAAGCTGGT
ACATCTGAAGCTAAAAAATATGATGAAATTGATGCTGCACCAGAAGAAAAAGCTCGTGGG
ATTACAATTAACACTGCACACGTAGAATACGCAACTCAAAATCGTCACTATGCACACGTT
GACTGTCCTGGTCACGCCGACTACGTTAAAAACATGATTACAGGTGCTGCTCAAATGGAC
GGTGGTATCTTAGTTGTGTCTGCAACTGATGGTCCAATGCCTCAAACTCGTGAACACATC
CTATTAGCTCGCCAAGTTGGTGTTCCTAAGATGGTTGTATTCTTAAACAAATGTGATGTA
GCTGATGATCCAGAAATGCAAGAATTAGTTGAAATGGAAGTTAGAGACCTTCTTAAATCT
TACGGATTCGATGGTGATAACACTCCAGTAATCAGAGGCTCTGCTTTAGGTGCTCTTAAT
GGCGAACCTGCATGAGAAGAAAAAATTCATGAACTAATGAAAGCAGTTGATGAATACATC
CCAACTCCTGACCGTGAAGTTGATAAACCATTCTTATTACCAATCGAAGATACTATGACA
ATTACTGGTCGTGGTACTGTAGTAACTGGTAGAGTTGAACGTGGTCAACTTAAAGTTGGT
GAAGAAGTTGAAATCGTTGGTATTACTGACACTAGAAAAGTAGTAGTAACTGGTATTGAA
ATGTTCAGAAAAGAACTAGATGCTGCTATGGCTGGTGACAACGCTGGGATCTTACTTCGT
GGTGTAGACCGTAAAGATGTACAACGTGGTCAAGTTTTAGCTAAACCTGGTTCAATTACT
CCACACAAGAAATTCAGAGCTGAAATTTATGCGCTTAAGAAGGATGAAGGTGGTCGTCAC
ACAGCTTTCTTAAATGGTTACAGACCTCAATTCTACTTCAGAACAACTGACGTAACTGGT
TCAATCCAATTAAAAGAAGGAACTGAAATGGTTATGCCTGGTGATAACACAGAAATTATC
GTTGAATTAATTTCTTCAATTGCTTGTGAAAAAGGTTCTAAGTTCTCTATCCGTGAAGGT
GGTAGAACTGTAGGTGCTGGTACAGTTGTAGAAGTACTTGAATAG

>protein sequence
MAKERFDRSKPHVNIGTIGHIDHGKTTLTAAICTVLSKAGTSEAKKYDEIDAAPEEKARG
ITINTAHVEYATQNRHYAHVDCPGHADYVKNMITGAAQMDGGILVVSATDGPMPQTREHI
LLARQVGVPKMVVFLNKCDVADDPEMQELVEMEVRDLLKSYGFDGDNTPVIRGSALGALN
GEPAWEEKIHELMKAVDEYIPTPDREVDKPFLLPIEDTMTITGRGTVVTGRVERGQLKVG
EEVEIVGITDTRKVVVTGIEMFRKELDAAMAGDNAGILLRGVDRKDVQRGQVLAKPGSIT
PHKKFRAEIYALKKDEGGRHTAFLNGYRPQFYFRTTDVTGSIQLKEGTEMVMPGDNTEII
VELISSIACEKGSKFSIREGGRTVGAGTVVEVLE