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Database: UniProt
Entry: A0A126RS59_9SPHN
LinkDB: A0A126RS59_9SPHN
Original site: A0A126RS59_9SPHN 
ID   A0A126RS59_9SPHN        Unreviewed;       601 AA.
AC   A0A126RS59;
DT   11-MAY-2016, integrated into UniProtKB/TrEMBL.
DT   11-MAY-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
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=K426_19585 {ECO:0000313|EMBL:AMK24846.1};
OS   Sphingobium sp. TKS.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC   Sphingomonadaceae; Sphingobium.
OX   NCBI_TaxID=1315974 {ECO:0000313|EMBL:AMK24846.1, ECO:0000313|Proteomes:UP000060779};
RN   [1] {ECO:0000313|Proteomes:UP000060779}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TKS {ECO:0000313|Proteomes:UP000060779};
RA   Tabata M.;
RT   "Whole genome sequence of gamma-HCH degrading bacterium Sphingobium sp.
RT   TKS.";
RL   Submitted (APR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AMK24846.1, ECO:0000313|Proteomes:UP000060779}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TKS {ECO:0000313|EMBL:AMK24846.1,
RC   ECO:0000313|Proteomes:UP000060779};
RX   PubMed=27056231;
RA   Tabata M., Ohhata S., Kawasumi T., Nikawadori Y., Kishida K., Sato T.,
RA   Ohtsubo Y., Tsuda M., Nagata Y.;
RT   "Complete Genome Sequence of a gamma-Hexachlorocyclohexane Degrader,
RT   Sphingobium sp. Strain TKS, Isolated from a gamma-Hexachlorocyclohexane-
RT   Degrading Microbial Community.";
RL   Genome Announc. 4:0-0(2016).
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}.
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DR   EMBL; CP005083; AMK24846.1; -; Genomic_DNA.
DR   RefSeq; WP_066560489.1; NZ_CP005083.1.
DR   AlphaFoldDB; A0A126RS59; -.
DR   STRING; 1315974.K426_19585; -.
DR   KEGG; spht:K426_19585; -.
DR   PATRIC; fig|1315974.3.peg.4112; -.
DR   OrthoDB; 9802948at2; -.
DR   Proteomes; UP000060779; Chromosome 1.
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   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   SUPFAM; SSF54980; EF-G C-terminal domain-like; 2.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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   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:UP000060779}.
FT   DOMAIN          5..187
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   BINDING         17..22
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
FT   BINDING         134..137
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
SQ   SEQUENCE   601 AA;  66733 MW;  E652D224E0FE9D91 CRC64;
     MTDLSHIRNF SIIAHIDHGK STLADRLIQR TGGLTDREMS AQVLDNMDIE KERGITIKAQ
     TVRLDYVAKN GETYELNLMD TPGHVDFAYE VSRSLAACEG ALLVVDAAQG VEAQTLANVY
     QSIEHDHEIV PVINKIDLPA AEPEKVKAEI EEVIGLDASE AVLASAKSGI GIDDILEAVV
     AKIPAPKGDR EAPLEAMLVD SWYDPYLGVV ILVRVMNGVI KKGQNIKFMI GGTEHLIDRV
     GCFRPKIEQL AELGPGEIGF ITAQIKDISQ TRVGDTITTV KNPAKVPLPG FKEVQPVVFC
     GLFPVDANDF EKLRDSISKL RLNDASFSFE METSAALGFG FRCGFLGLLH LEIIQERLTR
     EYDLDLITTA PSVVYEIHMN DGTTRHLHNP ADMPDANHID FIEEPWIEAV IYCPDEYLGS
     ILKLCQDRRG IQKNLTYVGG RAQVTYELPL NEVVFDFYDR LKSISRGYAS FDYHQIGTRE
     GDLVKMGILV NNEPVDALSM IVHRGTAESR GRGMCERLKD LIPRHLFKIP IQAAIGGKVI
     ARETIAAMRK DVTAKCYGGD ITRKKKLLEK QKEGKKRMRE YGSVQIPQEA FIAALRMGDE
     S
//
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