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Database: UniProt
Entry: A0A0C2BRF9_9BURK
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ID   A0A0C2BRF9_9BURK        Unreviewed;       597 AA.
AC   A0A0C2BRF9;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=Elongation factor 4 {ECO:0000256|HAMAP-Rule:MF_00071};
DE            Short=EF-4 {ECO:0000256|HAMAP-Rule:MF_00071};
DE            EC=3.6.5.n1 {ECO:0000256|HAMAP-Rule:MF_00071};
DE   AltName: Full=Ribosomal back-translocase LepA {ECO:0000256|HAMAP-Rule:MF_00071};
GN   Name=lepA {ECO:0000256|HAMAP-Rule:MF_00071};
GN   ORFNames=TSA66_20490 {ECO:0000313|EMBL:KIF82664.1};
OS   Noviherbaspirillum autotrophicum.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Noviherbaspirillum.
OX   NCBI_TaxID=709839 {ECO:0000313|EMBL:KIF82664.1, ECO:0000313|Proteomes:UP000031572};
RN   [1] {ECO:0000313|EMBL:KIF82664.1, ECO:0000313|Proteomes:UP000031572}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TSA66 {ECO:0000313|EMBL:KIF82664.1,
RC   ECO:0000313|Proteomes:UP000031572};
RA   Ishii S., Ashida N., Ohno H., Otsuka S., Yokota A., Senoo K.;
RT   "Denitrispirillum autotrophicum gen. nov., sp. nov., Denitrifying,
RT   Facultatively Autotrophic Bacteria Isolated from Rice Paddy Soil.";
RL   Submitted (DEC-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Required for accurate and efficient protein synthesis under
CC       certain stress conditions. May act as a fidelity factor of the
CC       translation reaction, by catalyzing a one-codon backward translocation
CC       of tRNAs on improperly translocated ribosomes. Back-translocation
CC       proceeds from a post-translocation (POST) complex to a pre-
CC       translocation (PRE) complex, thus giving elongation factor G a second
CC       chance to translocate the tRNAs correctly. Binds to ribosomes in a GTP-
CC       dependent manner. {ECO:0000256|HAMAP-Rule:MF_00071}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + H2O = GDP + H(+) + phosphate; Xref=Rhea:RHEA:19669,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:37565,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58189; EC=3.6.5.n1;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00071};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00071};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00071};
CC       Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_00071}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. LepA subfamily.
CC       {ECO:0000256|ARBA:ARBA00005454, ECO:0000256|HAMAP-Rule:MF_00071}.
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:KIF82664.1}.
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DR   EMBL; JWJG01000028; KIF82664.1; -; Genomic_DNA.
DR   RefSeq; WP_040041343.1; NZ_JWJG01000028.1.
DR   AlphaFoldDB; A0A0C2BRF9; -.
DR   STRING; 709839.TSA66_20490; -.
DR   OrthoDB; 9801472at2; -.
DR   Proteomes; UP000031572; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005525; F:GTP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003924; F:GTPase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
DR   GO; GO:0043022; F:ribosome binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0045727; P:positive regulation of translation; IEA:UniProtKB-UniRule.
DR   CDD; cd03699; EF4_II; 1.
DR   CDD; cd16260; EF4_III; 1.
DR   CDD; cd01890; LepA; 1.
DR   CDD; cd03709; lepA_C; 1.
DR   Gene3D; 3.30.70.240; -; 1.
DR   Gene3D; 3.30.70.2570; Elongation factor 4, C-terminal domain; 1.
DR   Gene3D; 3.30.70.870; Elongation Factor G (Translational Gtpase), domain 3; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 1.
DR   HAMAP; MF_00071; LepA; 1.
DR   InterPro; IPR006297; EF-4.
DR   InterPro; IPR035647; EFG_III/V.
DR   InterPro; IPR000640; EFG_V-like.
DR   InterPro; IPR004161; EFTu-like_2.
DR   InterPro; IPR031157; G_TR_CS.
DR   InterPro; IPR038363; LepA_C_sf.
DR   InterPro; IPR013842; LepA_CTD.
DR   InterPro; IPR035654; LepA_IV.
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   NCBIfam; TIGR01393; lepA; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43512:SF4; TRANSLATION FACTOR GUF1 HOMOLOG, CHLOROPLASTIC; 1.
DR   PANTHER; PTHR43512; TRANSLATION FACTOR GUF1-RELATED; 1.
DR   Pfam; PF00679; EFG_C; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF06421; LepA_C; 1.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SMART; SM00838; EFG_C; 1.
DR   SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
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   Cell membrane {ECO:0000256|HAMAP-Rule:MF_00071};
KW   Elongation factor {ECO:0000313|EMBL:KIF82664.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00071};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|HAMAP-Rule:MF_00071};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00071};
KW   Nucleotide-binding {ECO:0000256|HAMAP-Rule:MF_00071};
KW   Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00071};
KW   Reference proteome {ECO:0000313|Proteomes:UP000031572}.
FT   DOMAIN          2..184
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         14..19
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
FT   BINDING         131..134
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
SQ   SEQUENCE   597 AA;  65591 MW;  FD65477E364213EF CRC64;
     MDNIRNFSII AHIDHGKSTL ADRIIQLCGG LSDREMEAQV LDSMDLERER GITIKAQTAA
     LSYKARDGKV YNLNLIDTPG HVDFSYEVSR SLSACEGALL VVDASQGVEA QTVANCYTAL
     DLNVEVVPVL NKIDLPSANP DNAIAEIEDV IGIEASDAVR CSAKTGLGVE DVLEALIAKV
     PPPKGNPDAL LQALIIDSWF DNYVGVVMLV RVVNGTLRPK DKISLMATGA QYLTESVGVF
     TPKSQARESL SAGQVGFVIA GIKELKAARV GDTITLAGKP AAQPLPGFKE VQPQVFAGLF
     PVEANQYDAL RESLEKLKLN DAALQYEPEV SQALGFGFRC GFLGLLHMEI VQERLEREFD
     MDLITTAPTV IYEVALRDGT ILMVDNPSKM PDPSKIEEIR EPIVTVNLYM PQEYVGSVIT
     LCTQKRGVQI NMAYHGKQVM LTYEMPMAEI VLDFFDKLKS TSRGYASMDY EFKEYRAADV
     VKVDMLINGD KVDALAIIVH RSSSQYRGRA VAAKMRELIP RQMFDVAIQA AIGSNIIARE
     NVKAMRKNVL AKCYGGDISR KRKLLEKQKA GKKRMKQVGS VEVPQEAFLA ILQVEDK
//
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