(data stored in ACNUC29543 zone)

SWISSPROT: EFTU_ACIBT

ID   EFTU_ACIBT              Reviewed;         396 AA.
AC   A3M1F6;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-MAY-2008, sequence version 2.
DT   11-DEC-2019, entry version 85.
DE   RecName: Full=Elongation factor Tu {ECO:0000255|HAMAP-Rule:MF_00118};
DE            Short=EF-Tu {ECO:0000255|HAMAP-Rule:MF_00118};
GN   Name=tuf1 {ECO:0000255|HAMAP-Rule:MF_00118}; OrderedLocusNames=A1S_0279;
GN   and
GN   Name=tuf2 {ECO:0000255|HAMAP-Rule:MF_00118}; OrderedLocusNames=A1S_0869;
OS   Acinetobacter baumannii (strain ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC
OS   KC755 / 5377).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Moraxellaceae; Acinetobacter;
OC   Acinetobacter calcoaceticus/baumannii complex.
OX   NCBI_TaxID=400667;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 17978 / CIP 53.77 / LMG 1025 / NCDC KC755 / 5377;
RX   PubMed=17344419; DOI=10.1101/gad.1510307;
RA   Smith M.G., Gianoulis T.A., Pukatzki S., Mekalanos J.J., Ornston L.N.,
RA   Gerstein M., Snyder M.;
RT   "New insights into Acinetobacter baumannii pathogenesis revealed by high-
RT   density pyrosequencing and transposon mutagenesis.";
RL   Genes Dev. 21:601-614(2007).
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   -!- SEQUENCE CAUTION:
CC       Sequence=ABO11301.2; Type=Miscellaneous discrepancy; Note=This prediction is not full-length and may not be functional.; Evidence={ECO:0000305};
DR   EMBL; CP000521; ABO10750.2; -; Genomic_DNA.
DR   EMBL; CP000521; ABO11301.2; ALT_SEQ; Genomic_DNA.
DR   RefSeq; WP_001029610.1; NZ_CP039028.2.
DR   SMR; A3M1F6; -.
DR   PRIDE; A3M1F6; -.
DR   EnsemblBacteria; ABO10750; ABO10750; A1S_0279.
DR   EnsemblBacteria; ABO11301; ABO11301; A1S_0869.
DR   GeneID; 31350097; -.
DR   KEGG; acb:A1S_0279; -.
DR   KEGG; acb:A1S_0869; -.
DR   HOGENOM; HOG000229290; -.
DR   KO; K02358; -.
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   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; TF_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;
DR   PRODOM; A3M1F6.
DR   SWISS-2DPAGE; A3M1F6.
KW   Cytoplasm; Elongation factor; GTP-binding; Nucleotide-binding;
KW   Protein biosynthesis.
FT   CHAIN           1..396
FT                   /note="Elongation factor Tu"
FT                   /id="PRO_0000337301"
FT   DOMAIN          10..206
FT                   /note="tr-type G"
FT   NP_BIND         19..26
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   NP_BIND         81..85
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
FT   NP_BIND         136..139
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00118"
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"
SQ   SEQUENCE   396 AA;  42892 MW;  56B9D9300174DF8A CRC64;
     MAKAKFERNK PHVNVGTIGH VDHGKTTLTA AIATICAKTY GGEAKDYSQI DSAPEEKARG
     ITINTSHVEY DSPTRHYAHV DCPGHADYVK NMITGAAQMD GAILVCAATD GPMPQTREHI
     LLSRQVGVPY IIVFLNKCDL VDDEELLELV EMEVRELLST YDFPGDDTPV IRGSALAALN
     GEAGPYGEES VLALVAALDS YIPEPERAID KAFLMPIEDV FSISGRGTVV TGRVEAGIIK
     VGEEVEIVGI KDTVKTTVTG VEMFRKLLDE GRAGENCGIL LRGTKREEVQ RGQVLAKPGT
     IKPHTKFDAE VYVLSKEEGG RHTPFLNGYR PQFYFRTTDV TGAIQLKEGV EMVMPGDNVE
     MSVELIHPIA MDPGLRFAIR EGGRTVGAGV VAKVTA
//

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