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Database: UniProt
Entry: A0A2P7TC93_9SPHI
LinkDB: A0A2P7TC93_9SPHI
Original site: A0A2P7TC93_9SPHI 
ID   A0A2P7TC93_9SPHI        Unreviewed;       387 AA.
AC   A0A2P7TC93;
DT   23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT   23-MAY-2018, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Elongation factor Tu {ECO:0000256|ARBA:ARBA00029554, ECO:0000256|RuleBase:RU004061};
DE   Flags: Fragment;
GN   Name=tuf {ECO:0000313|EMBL:PSJ72282.1};
GN   ORFNames=C7N43_35000 {ECO:0000313|EMBL:PSJ72282.1};
OS   Sphingobacteriales bacterium UPWRP_1.
OC   Bacteria; Bacteroidota; Sphingobacteriia; Sphingobacteriales.
OX   NCBI_TaxID=2116516 {ECO:0000313|EMBL:PSJ72282.1, ECO:0000313|Proteomes:UP000240367};
RN   [1] {ECO:0000313|EMBL:PSJ72282.1, ECO:0000313|Proteomes:UP000240367}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UPWRP_1 {ECO:0000313|EMBL:PSJ72282.1,
RC   ECO:0000313|Proteomes:UP000240367};
RA   Tan S.M.;
RT   "Obtaining draft genomes of rare unknown microbial groups and defining 1
RT   their spatial structures from highly complex communities.";
RL   Submitted (MAR-2018) 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   -!- 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}.
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:PSJ72282.1}.
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DR   EMBL; PXYE01000251; PSJ72282.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2P7TC93; -.
DR   Proteomes; UP000240367; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
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   Elongation factor {ECO:0000256|ARBA:ARBA00022768,
KW   ECO:0000313|EMBL:PSJ72282.1}; GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000240367}.
FT   DOMAIN          1..193
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:PSJ72282.1"
SQ   SEQUENCE   387 AA;  42510 MW;  3FA0C3A26322472E CRC64;
     HVNIGTIGHV DHGKTTLTAA ITYVLAESGL AEKKSYDSID SAPEEKERGI TINTAHVEYE
     TKNRHYAHVD CPGHADYVKN MVTGAAQMDG AILVCAATDG PMPQTREHIL LARQVGVPRI
     VVFMNKVDLV DDPELIELVE MELRELLSFY NFPGDETPII KGSALLALNG DPEQKKIILE
     LMQAVDEYVP VPERAVDKPF LMPVEDVFSI TGRGTVATGR IERGVINSSE PVEIIGLRPV
     EEKPLTSVVT GVEMFRKILS RGEAGDNVGL LLRGIDKDAI KRGMVVCKPG SVKPHTKFTA
     EVYVLSKEEG GRHTPFFNKY RPQFYFRTTD VTGEITLPDG VEMCMPGDNL TITVNLIYPI
     AMEKGLRFAI REGGRTVGAG QVTEILQ
//
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