EFTU_CHLTR
ID EFTU_CHLTR Reviewed; 394 AA.
AC P0CD71; O84324; P26622;
DT 09-FEB-2010, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 65.
DE RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
GN Name=tuf {ECO:0000255|HAMAP-Rule:MF_00118}; Synonyms=tufA, tufB;
GN OrderedLocusNames=CT_322;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=F/IC-Cal-13;
RX PubMed=8106330; DOI=10.1128/jb.176.4.1184-1187.1994;
RA Zhang Y.X., Shi Y., Zhou M., Petsko G.A.;
RT "Cloning, sequencing, and expression in Escherichia coli of the gene
RT encoding a 45-kilodalton protein, elongation factor Tu, from Chlamydia
RT trachomatis serovar F.";
RL J. Bacteriol. 176:1184-1187(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
CC -!- FUNCTION: This protein promotes the GTP-dependent binding of aminoacyl-
CC tRNA to the A-site of ribosomes during protein biosynthesis.
CC {ECO:0000255|HAMAP-Rule:MF_00118}.
CC -!- SUBUNIT: Monomer. {ECO:0000255|HAMAP-Rule:MF_00118}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00118}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L22216; AAA19798.1; -; Genomic_DNA.
DR EMBL; AE001273; AAC67915.1; -; Genomic_DNA.
DR PIR; G71528; G71528.
DR PIR; JC1420; JC1420.
DR RefSeq; NP_219827.1; NC_000117.1.
DR RefSeq; WP_009871669.1; NC_000117.1.
DR AlphaFoldDB; P0CD71; -.
DR SMR; P0CD71; -.
DR STRING; 813.O172_01725; -.
DR EnsemblBacteria; AAC67915; AAC67915; CT_322.
DR GeneID; 884801; -.
DR KEGG; ctr:CT_322; -.
DR PATRIC; fig|272561.5.peg.344; -.
DR HOGENOM; CLU_007265_0_0_0; -.
DR InParanoid; P0CD71; -.
DR OMA; EGDKEWG; -.
DR Proteomes; UP000000431; Chromosome.
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; IBA:GO_Central.
DR GO; GO:0006414; P:translational elongation; IBA:GO_Central.
DR CDD; cd01884; EF_Tu; 1.
DR CDD; cd03697; EFTU_II; 1.
DR Gene3D; 3.40.50.300; -; 1.
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 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; SSF50447; SSF50447; 1.
DR SUPFAM; SSF50465; SSF50465; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00485; EF-Tu; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..394
FT /note="Elongation factor Tu"
FT /id="PRO_0000091308"
FT DOMAIN 10..204
FT /note="tr-type G"
FT REGION 19..26
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 60..64
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 81..84
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 136..139
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 174..176
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 19..26
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 81..85
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT BINDING 136..139
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT VARIANT 157
FT /note="V -> A (in strain: F/IC-Cal-13)"
FT VARIANT 348
FT /note="I -> V (in strain: F/IC-Cal-13)"
SQ SEQUENCE 394 AA; 43293 MW; 1540FF3292B72192 CRC64;
MSKETFQRNK PHINIGTIGH VDHGKTTLTA AITRALSGDG LADFRDYSSI DNTPEEKARG
ITINASHVEY ETANRHYAHV DCPGHADYVK NMITGAAQMD GAILVVSATD GAMPQTKEHI
LLARQVGVPY IVVFLNKIDM ISEEDAELVD LVEMELVELL EEKGYKGCPI IRGSALKALE
GDAAYIEKVR ELMQAVDDNI PTPEREIDKP FLMPIEDVFS ISGRGTVVTG RIERGIVKVS
DKVQLVGLRD TKETIVTGVE MFRKELPEGR AGENVGLLLR GIGKNDVERG MVVCLPNSVK
PHTQFKCAVY VLQKEEGGRH KPFFTGYRPQ FFFRTTDVTG VVTLPEGIEM VMPGDNVEFE
VQLISPVALE EGMRFAIREG GRTIGAGTIS KIIA
