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Database: UniProt
Entry: F9UKL1_9MOLU
LinkDB: F9UKL1_9MOLU
Original site: F9UKL1_9MOLU 
ID   F9UKL1_9MOLU            Unreviewed;       397 AA.
AC   F9UKL1;
DT   19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT   19-OCT-2011, sequence version 1.
DT   24-JAN-2024, entry version 55.
DE   RecName: Full=Elongation factor Tu {ECO:0000256|ARBA:ARBA00029554, ECO:0000256|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu {ECO:0000256|HAMAP-Rule:MF_00118};
GN   Name=tuf {ECO:0000256|HAMAP-Rule:MF_00118};
GN   ORFNames=MCSF7_02121 {ECO:0000313|EMBL:EGV00216.1};
OS   Mycoplasmopsis columbina SF7.
OC   Bacteria; Mycoplasmatota; Mollicutes; Mycoplasmataceae; Mycoplasmopsis.
OX   NCBI_TaxID=1037410 {ECO:0000313|EMBL:EGV00216.1, ECO:0000313|Proteomes:UP000004978};
RN   [1] {ECO:0000313|EMBL:EGV00216.1, ECO:0000313|Proteomes:UP000004978}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SF7 {ECO:0000313|EMBL:EGV00216.1,
RC   ECO:0000313|Proteomes:UP000004978};
RX   PubMed=23599295;
RA   Guo Z., Xu X., Zheng Q., Li T., Kuang S., Zhang Z., Chen Y., Lu X.,
RA   Zhou R., Bi D., Jin H.;
RT   "Genome Sequence of Mycoplasma columbinum Strain SF7.";
RL   Genome Announc. 1:E00157-13(2013).
CC   -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC       tRNA to the A-site of ribosomes during protein biosynthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SUBUNIT: Monomer. {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00118}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. EF-Tu/EF-1A
CC       subfamily. {ECO:0000256|ARBA:ARBA00007249, ECO:0000256|HAMAP-
CC       Rule:MF_00118}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EGV00216.1}.
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DR   EMBL; AFXA01000011; EGV00216.1; -; Genomic_DNA.
DR   RefSeq; WP_006608829.1; NZ_AFXA01000011.1.
DR   AlphaFoldDB; F9UKL1; -.
DR   STRING; 1037410.MCSF7_02121; -.
DR   eggNOG; COG0050; Bacteria.
DR   Proteomes; UP000004978; Unassembled WGS sequence.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd01884; EF_Tu; 1.
DR   CDD; cd03697; EFTU_II; 1.
DR   CDD; cd03707; EFTU_III; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   HAMAP; MF_00118_B; EF_Tu_B; 1.
DR   InterPro; IPR041709; EF-Tu_GTP-bd.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR033720; EFTU_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR   InterPro; IPR004541; Transl_elong_EFTu/EF1A_bac/org.
DR   InterPro; IPR004160; Transl_elong_EFTu/EF1A_C.
DR   NCBIfam; TIGR00485; EF-Tu; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1.
DR   PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF03143; GTP_EFTU_D3; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   PROSITE; PS00301; G_TR_1; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00118};
KW   Elongation factor {ECO:0000256|ARBA:ARBA00022768, ECO:0000256|HAMAP-
KW   Rule:MF_00118};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00118}; Hydrolase {ECO:0000313|EMBL:EGV00216.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00118};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00118}; Reference proteome {ECO:0000313|Proteomes:UP000004978}.
FT   DOMAIN          10..207
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   COILED          178..205
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   BINDING         19..26
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT   BINDING         81..85
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT   BINDING         136..139
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
SQ   SEQUENCE   397 AA;  43716 MW;  32D25072B2ADDFBC CRC64;
     MAKLDFNRSK EHVNIGTIGH VDHGKTTLTA AIATVLAKKG LAEARDYASI DNAPEEKARG
     ITINTSHIEY ETEARHYAHV DCPGHADYIK NMITGAAQMD GAILVVAATD GPMPQTREHI
     LLSKQVGVPR MVVFLNKCDM LKSADDEEML ELVEMEIRDL LSKYGFDGDN TPIIRGSAKE
     ALEGKAEYED KIMELMNAVD TYIETPVKEF DKPFLMAVED VFTITGRGTV ATGRVERGKL
     SLNEEVEIVG LKPTKKTVVT GMEMFRKNLK EVQAGDNAGL LLRGVEKSQI ERGQVLAKPG
     SIIPHTEFKA AIYVLTKEEG GRHTPFFKNY KPQFYFRTTD VTGGVEFEAG REMVTPGENV
     DLTVKLIAPI AVEEGTKFSI REGGHTVGYG NVTQIIK
//
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