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Database: UniProt
Entry: A0A022KW46_9MICO
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ID   A0A022KW46_9MICO        Unreviewed;       626 AA.
AC   A0A022KW46;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 38.
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=D641_0103470 {ECO:0000313|EMBL:EYT50347.1};
OS   Brachybacterium muris UCD-AY4.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC   Brachybacterium.
OX   NCBI_TaxID=1249481 {ECO:0000313|EMBL:EYT50347.1, ECO:0000313|Proteomes:UP000019754};
RN   [1] {ECO:0000313|EMBL:EYT50347.1, ECO:0000313|Proteomes:UP000019754}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UCD-AY4 {ECO:0000313|EMBL:EYT50347.1,
RC   ECO:0000313|Proteomes:UP000019754};
RX   PubMed=23516213;
RA   Lo J.R., Lang J.M., Darling A.E., Eisen J.A., Coil D.A.;
RT   "Draft genome sequence of an Actinobacterium, Brachybacterium muris strain
RT   UCD-AY4.";
RL   Genome Announc. 1:E0008613-E0008613(2013).
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:EYT50347.1}.
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DR   EMBL; AORC01000004; EYT50347.1; -; Genomic_DNA.
DR   RefSeq; WP_017822410.1; NZ_AORC01000004.1.
DR   AlphaFoldDB; A0A022KW46; -.
DR   STRING; 1249481.D641_0103470; -.
DR   HOGENOM; CLU_009995_3_3_11; -.
DR   OrthoDB; 9801472at2; -.
DR   Proteomes; UP000019754; 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: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   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:UP000019754}.
FT   DOMAIN          23..204
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          1..20
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         35..40
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
FT   BINDING         151..154
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
SQ   SEQUENCE   626 AA;  68881 MW;  8FCB6B5461FE06BD CRC64;
     MPVTPRISAD EATDIQPAST PQERIRNFCI IAHIDHGKST LADRMLQMTG VVDERLMRAQ
     YLDRMDIERE RGITVKSQAV RMPWQVDGVN YALNMIDTPG HVDFTYEVSR SLAACEGAIL
     LVDAAQGIEA QTLANLYLAM ENDLTIIPVL NKIDLPAADP DKYAAEIGQL VGVDPSEVLR
     VSGKTGQGVQ ELLDHVVRTL PPPEGQVDAP CRAMIFDSVY DTYRGVITYI RVIDGYLKSR
     DRIDMMSTGA HHELLEIGVS SPEPSPTKGI GPGEVGYLIT GVKDVRQSKV GDTVTTSVRG
     ATEALPGYSD PKPMVYSGLF PIDGSDYPVL RDALDKLKLN DAALNYEPET STALGFGFRV
     GFLGLLHLEI VRERLEREFN LDLISTAPSV VYNVVMEDGT EVEVLNPSDF PEGKVKEISE
     PVAKATILVP SEFVGVVMEL CQSKRGSLGG MDYLSEDRVE LRYTVPLAEI VFDFFDQLKS
     RTRGYASLDY DVSGEQTADL VKVDMLLQGE PVDAFSAVVH RDKAYSYGVE MAGKLKNLIP
     RQQFEVPIQA AIGSRVIARE NIRAMRKDVL SKCYGGDISR KRKLLEKQKE GKKRMKNIGS
     VEVPQEAFIA ALSSDAADTG KDSKKK
//
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