EFTS_CLAM3
ID EFTS_CLAM3 Reviewed; 275 AA.
AC A5CQS1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-JUN-2007, sequence version 1.
DT 25-MAY-2022, entry version 77.
DE RecName: Full=Elongation factor Ts {ECO:0000255|HAMAP-Rule:MF_00050};
DE Short=EF-Ts {ECO:0000255|HAMAP-Rule:MF_00050};
GN Name=tsf {ECO:0000255|HAMAP-Rule:MF_00050}; OrderedLocusNames=CMM_1384;
OS Clavibacter michiganensis subsp. michiganensis (strain NCPPB 382).
OC Bacteria; Actinobacteria; Micrococcales; Microbacteriaceae; Clavibacter.
OX NCBI_TaxID=443906;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCPPB 382;
RX PubMed=18192381; DOI=10.1128/jb.01595-07;
RA Gartemann K.-H., Abt B., Bekel T., Burger A., Engemann J., Fluegel M.,
RA Gaigalat L., Goesmann A., Graefen I., Kalinowski J., Kaup O., Kirchner O.,
RA Krause L., Linke B., McHardy A., Meyer F., Pohle S., Rueckert C.,
RA Schneiker S., Zellermann E.-M., Puehler A., Eichenlaub R., Kaiser O.,
RA Bartels D.;
RT "The genome sequence of the tomato-pathogenic actinomycete Clavibacter
RT michiganensis subsp. michiganensis NCPPB382 reveals a large island involved
RT in pathogenicity.";
RL J. Bacteriol. 190:2138-2149(2008).
CC -!- FUNCTION: Associates with the EF-Tu.GDP complex and induces the
CC exchange of GDP to GTP. It remains bound to the aminoacyl-tRNA.EF-
CC Tu.GTP complex up to the GTP hydrolysis stage on the ribosome.
CC {ECO:0000255|HAMAP-Rule:MF_00050}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00050}.
CC -!- SIMILARITY: Belongs to the EF-Ts family. {ECO:0000255|HAMAP-
CC Rule:MF_00050}.
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DR EMBL; AM711867; CAN01429.1; -; Genomic_DNA.
DR RefSeq; WP_012038070.1; NC_009480.1.
DR AlphaFoldDB; A5CQS1; -.
DR SMR; A5CQS1; -.
DR STRING; 443906.CMM_1384; -.
DR EnsemblBacteria; CAN01429; CAN01429; CMM_1384.
DR GeneID; 56885696; -.
DR KEGG; cmi:CMM_1384; -.
DR eggNOG; COG0264; Bacteria.
DR HOGENOM; CLU_047155_0_0_11; -.
DR OMA; DAGMMDC; -.
DR OrthoDB; 1405357at2; -.
DR Proteomes; UP000001564; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR Gene3D; 3.30.479.20; -; 2.
DR HAMAP; MF_00050; EF_Ts; 1.
DR InterPro; IPR036402; EF-Ts_dimer_sf.
DR InterPro; IPR001816; Transl_elong_EFTs/EF1B.
DR InterPro; IPR014039; Transl_elong_EFTs/EF1B_dimer.
DR InterPro; IPR009060; UBA-like_sf.
DR PANTHER; PTHR11741; PTHR11741; 1.
DR Pfam; PF00889; EF_TS; 1.
DR SUPFAM; SSF46934; SSF46934; 1.
DR SUPFAM; SSF54713; SSF54713; 1.
DR TIGRFAMs; TIGR00116; tsf; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Elongation factor; Protein biosynthesis.
FT CHAIN 1..275
FT /note="Elongation factor Ts"
FT /id="PRO_1000006075"
FT REGION 80..83
FT /note="Involved in Mg(2+) ion dislocation from EF-Tu"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00050"
SQ SEQUENCE 275 AA; 29287 MW; D3468EDB249B6BFD CRC64;
MANFTAADVK ELRDRLGAGM MDSKNALVEA DGDIEKAIEI LRLKGQKGNA KRGDRSTAEG
LVAASTQDGA ATLIELACET DFVAKNDKFI ALSESVLAAV VAAGASTVEE ALQAPAGEQT
VDQLISDQAA ILGEKIALRR VARLAGEHQE VYLHRTSKDL PPQVGVVVDY SGTDAETARS
IAQHIAFANP EYLAREDVPA DKVEAERAIV TEISRNEGKP EAALPKIIEG RLTGFFKQVA
LLEQDYAKDN KQSVKKVVEA AGLTVTGFAR FKVGA