ID F4KUH0_HALH1 Unreviewed; 398 AA.
AC F4KUH0;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 64.
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 OrderedLocusNames=Halhy_4567 {ECO:0000313|EMBL:AEE52406.1};
OS Haliscomenobacter hydrossis (strain ATCC 27775 / DSM 1100 / LMG 10767 / O).
OC Bacteria; Bacteroidota; Saprospiria; Saprospirales; Haliscomenobacteraceae;
OC Haliscomenobacter.
OX NCBI_TaxID=760192 {ECO:0000313|EMBL:AEE52406.1, ECO:0000313|Proteomes:UP000008461};
RN [1] {ECO:0000313|EMBL:AEE52406.1, ECO:0000313|Proteomes:UP000008461}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 27775 / DSM 1100 / LMG 10767 / O
RC {ECO:0000313|Proteomes:UP000008461};
RX PubMed=21886862; DOI=10.4056/sigs.1964579;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Daligault H., Lapidus A., Zeytun A., Nolan M., Lucas S., Del Rio T.G.,
RA Tice H., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S., Liolios K.,
RA Pagani I., Ivanova N., Huntemann M., Mavromatis K., Mikhailova N., Pati A.,
RA Chen A., Palaniappan K., Land M., Hauser L., Brambilla E.M., Rohde M.,
RA Verbarg S., Goker M., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P., Woyke T.;
RT "Complete genome sequence of Haliscomenobacter hydrossis type strain (O).";
RL Stand. Genomic Sci. 4:352-360(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DSM 1100;
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Han J., Lapidus A., Bruce D., Goodwin L., Pitluck S., Peters L.,
RA Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G., Pagani I.,
RA Daligault H., Detter J.C., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Verbarg S., Frueling A.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "Complete sequence of chromosome of Haliscomenobacter hydrossis DSM 1100.";
RL Submitted (APR-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Abolishes the inhibitory effect of tetracyclin on protein
CC synthesis by a non-covalent modification of the ribosomes.
CC {ECO:0000256|ARBA:ARBA00003987}.
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}.
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DR EMBL; CP002691; AEE52406.1; -; Genomic_DNA.
DR RefSeq; WP_013766944.1; NC_015510.1.
DR AlphaFoldDB; F4KUH0; -.
DR STRING; 760192.Halhy_4567; -.
DR GeneID; 78194273; -.
DR KEGG; hhy:Halhy_4567; -.
DR eggNOG; COG0050; Bacteria.
DR HOGENOM; CLU_007265_0_0_10; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000008461; 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; 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 Cytoplasm {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};
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:UP000008461}.
FT DOMAIN 10..204
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
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 398 AA; 43574 MW; 935A8845B2B29B1C CRC64;
MAKGTFERNK PHVNIGTIGH VDHGKTTLTA AITTVLASKG LAEKKDYDSI DAAPEEKERG
ITINTAHVEY ETEKRHYAHV DCPGHADYVK NMVTGAAQMD GAILVCAATD GPMPQTREHI
LLARQVGVPA IVVFMNKVDL VDDPEMLELV EMEVRELLDT YQFDGDNAAV IQGSALKALE
GDPVYVQRIM DLMDAVDAQI PEPIRLTDKP FLMPIEDVFS ITGRGTVATG RIERGIIKVG
ESVEIIGMQK EGEKPLVSTV TGVEMFRKIL DRGEAGDNAG ILLRGIDKEA IRRGMVICAP
NSVKPHLEFK CEVYVLSKEE GGRHTPFFKG YRPQFYFRTT DVTGDCTLPD GVEMVMPGDN
VTLNVKLLSP IAMEKGLRFA IREGGRTVGA GQVTEIIK
//
