EFTU_MYCPN
ID EFTU_MYCPN Reviewed; 394 AA.
AC P23568; P75126;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 139.
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}; OrderedLocusNames=MPN_665;
GN ORFNames=MP177;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2126326; DOI=10.1111/j.1365-2958.1990.tb00709.x;
RA Yogev D., Sela S., Bercovier H., Razin S.;
RT "Nucleotide sequence and codon usage of the elongation factor Tu(EF-Tu)
RT gene from Mycoplasma pneumoniae.";
RL Mol. Microbiol. 4:1303-1310(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
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 -!- INTERACTION:
CC P23568; P02751: FN1; Xeno; NbExp=2; IntAct=EBI-2259072, EBI-1220319;
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}.
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DR EMBL; X55768; CAA39292.1; -; Genomic_DNA.
DR EMBL; U00089; AAB95825.1; -; Genomic_DNA.
DR PIR; S73503; S73503.
DR RefSeq; NP_110354.1; NC_000912.1.
DR RefSeq; WP_010875022.1; NC_000912.1.
DR AlphaFoldDB; P23568; -.
DR SMR; P23568; -.
DR IntAct; P23568; 22.
DR STRING; 272634.MPN_665; -.
DR MoonProt; P23568; -.
DR EnsemblBacteria; AAB95825; AAB95825; MPN_665.
DR GeneID; 66608647; -.
DR KEGG; mpn:MPN_665; -.
DR PATRIC; fig|272634.6.peg.730; -.
DR HOGENOM; CLU_007265_0_1_14; -.
DR OMA; EGDKEWG; -.
DR BioCyc; MPNE272634:G1GJ3-1066-MON; -.
DR Proteomes; UP000000808; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:AgBase.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:CAFA.
DR GO; GO:0016020; C:membrane; IDA:AgBase.
DR GO; GO:0001968; F:fibronectin binding; IPI:CAFA.
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 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 1: Evidence at protein level;
KW Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..394
FT /note="Elongation factor Tu"
FT /id="PRO_0000091350"
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 CONFLICT 12..13
FT /note="HV -> QL (in Ref. 1; CAA39292)"
FT /evidence="ECO:0000305"
FT CONFLICT 65
FT /note="S -> I (in Ref. 1; CAA39292)"
FT /evidence="ECO:0000305"
FT CONFLICT 122
FT /note="L -> V (in Ref. 1; CAA39292)"
FT /evidence="ECO:0000305"
FT CONFLICT 136
FT /note="N -> F (in Ref. 1; CAA39292)"
FT /evidence="ECO:0000305"
FT CONFLICT 198..209
FT /note="EWIPTPEREVDK -> DGFQLLNVKWTN (in Ref. 1; CAA39292)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="E -> V (in Ref. 1; CAA39292)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="T -> S (in Ref. 1; CAA39292)"
FT /evidence="ECO:0000305"
FT CONFLICT 391..394
FT /note="EVLE -> KCLNSESRILSWLC (in Ref. 1; CAA39292)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 394 AA; 43149 MW; 32818DA027954BD8 CRC64;
MAREKFDRSK PHVNVGTIGH IDHGKTTLTA AICTVLAKEG KSAATRYDQI DKAPEEKARG
ITINSAHVEY SSDKRHYAHV DCPGHADYIK NMITGAAQMD GAILVVSATD SVMPQTREHI
LLARQVGVPR MVVFLNKCDI ATDEEVQELV AEEVRDLLTS YGFDGKNTPI IYGSALKALE
GDPKWEAKIH DLMNAVDEWI PTPEREVDKP FLLAIEDTMT ITGRGTVVTG RVERGELKVG
QEIEIVGLRP IRKAVVTGIE MFKKELDSAM AGDNAGVLLR GVDRKEVERG QVLAKPGSIK
PHKKFKAEIY ALKKEEGGRH TGFLNGYRPQ FYFRTTDVTG SISLPENTEM VLPGDNTSIT
VELIAPIACE KGSKFSIREG GRTVGAGSVT EVLE
