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Database: UniProt
Entry: A0A0P0A4I7_9RHOB
LinkDB: A0A0P0A4I7_9RHOB
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ID   A0A0P0A4I7_9RHOB        Unreviewed;       391 AA.
AC   A0A0P0A4I7;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   27-MAR-2024, entry version 33.
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   ORFNames=IMCC12053_1481 {ECO:0000313|EMBL:ALI55428.1}, IMCC12053_1498
GN   {ECO:0000313|EMBL:ALI55445.1}, SAMN05444421_10232
GN   {ECO:0000313|EMBL:SFK18740.1}, SAMN05444421_10251
GN   {ECO:0000313|EMBL:SFK19289.1};
OS   Celeribacter marinus.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Celeribacter.
OX   NCBI_TaxID=1397108 {ECO:0000313|EMBL:ALI55428.1, ECO:0000313|Proteomes:UP000064920};
RN   [1] {ECO:0000313|EMBL:ALI55428.1, ECO:0000313|Proteomes:UP000064920}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IMCC 12053 {ECO:0000313|EMBL:ALI55428.1,
RC   ECO:0000313|Proteomes:UP000064920};
RA   Wang D.B., Wang M.;
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SFK18740.1, ECO:0000313|Proteomes:UP000181863}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100036 {ECO:0000313|EMBL:SFK18740.1,
RC   ECO:0000313|Proteomes:UP000181863};
RA   Varghese N., Submissions S.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; CP012023; ALI55428.1; -; Genomic_DNA.
DR   EMBL; CP012023; ALI55445.1; -; Genomic_DNA.
DR   EMBL; FOSM01000002; SFK18740.1; -; Genomic_DNA.
DR   EMBL; FOSM01000002; SFK19289.1; -; Genomic_DNA.
DR   RefSeq; WP_062217321.1; NZ_FOSM01000002.1.
DR   STRING; 1397108.IMCC12053_1481; -.
DR   KEGG; cmar:IMCC12053_1481; -.
DR   KEGG; cmar:IMCC12053_1498; -.
DR   PATRIC; fig|1397108.4.peg.1515; -.
DR   OrthoDB; 9803139at2; -.
DR   Proteomes; UP000064920; Chromosome.
DR   Proteomes; UP000181863; Unassembled WGS sequence.
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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
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:UP000064920}.
FT   DOMAIN          10..201
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         76..80
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
FT   BINDING         131..134
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00118"
SQ   SEQUENCE   391 AA;  42739 MW;  B8196C39C59033C3 CRC64;
     MAKGKFERNK PHVNIGTIGH VDHGKTTLTA AITKYFGDFK AYDQIDGAPE EKARGITIST
     AHVEYETEAR HYAHVDCPGH ADYVKNMITG AAQMDGAILV VNAADGPMPQ TREHILLGRQ
     VGIPHMVVYM NKVDQVDDEE LLELVEMEIR ELLSSYDYPG DDIPVIPGSA LAAMEGRDPE
     IGEESIRKLM AAVDSYIPTP ARAVDKPFLM PIEDVFSISG RGTVVTGRVE RGVVNVGDEL
     EIVGIKDTTK TICTGVEMFR KLLDRGEAGD NIGALLRGVD RDAVERGQVL VKPGSVKPHT
     KFEAEVYILT KEEGGRHTPF FANYRPQFYF RTTDVTGTCV LPEGTEMVMP GDNLKLSAEL
     IAPIAMEEGL RFAIREGGRT VGSGVVSKII E
//
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