ID I4LVZ1_GARVA Unreviewed; 626 AA.
AC I4LVZ1;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 46.
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=CGSMWGv55152_01659 {ECO:0000313|EMBL:EIK81131.1};
OS Gardnerella vaginalis 55152.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Gardnerella.
OX NCBI_TaxID=698955 {ECO:0000313|EMBL:EIK81131.1, ECO:0000313|Proteomes:UP000005936};
RN [1] {ECO:0000313|EMBL:EIK81131.1, ECO:0000313|Proteomes:UP000005936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=55152 {ECO:0000313|EMBL:EIK81131.1,
RC ECO:0000313|Proteomes:UP000005936};
RX PubMed=22609915; DOI=10.1128/JB.00056-12;
RA Ahmed A., Earl J., Retchless A., Hillier S., Rabe L., Cherpes T.,
RA Powell E., Janto B., Eutsey R., Hiller N.L., Boissy R., Dahlgreen M.,
RA Hall B., Costerton J., Post J.C., Hu F., Ehrlich G.;
RT "Comparative Genomic Analyses of 17 Clinical Isolates of Gardnerella
RT vaginalis Provide Evidence of Multiple Genetically Isolated Clades
RT Consistent with Subspeciation into Genovars.";
RL J. Bacteriol. 194:3922-3937(2012).
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:EIK81131.1}.
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DR EMBL; ADEQ01000003; EIK81131.1; -; Genomic_DNA.
DR RefSeq; WP_004120758.1; NZ_ADEQ01000003.1.
DR AlphaFoldDB; I4LVZ1; -.
DR PATRIC; fig|698955.3.peg.323; -.
DR Proteomes; UP000005936; 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|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00071}; Protein biosynthesis {ECO:0000256|HAMAP-Rule:MF_00071}.
FT DOMAIN 14..195
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 26..31
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
FT BINDING 142..145
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00071"
SQ SEQUENCE 626 AA; 69040 MW; 16D690514C47202F CRC64;
MITPHNQPGF TDQSLIRNFC IIAHIDHGKS TVADRILQLS GIVPEREMRD RFLDRMDIEQ
ERGITIKSQA VRVPWVFDGK EYSLGMIDTP GHVDFTYEVS RALAACEGAV LLVDATQGIE
AQTLSNLYMA IEHDLTIIPV LNKIDLPSAE PDKHAEEIAG LIGCKPNEVL RVSGKTGEGV
KDLLDQIVLE VPAPSGNPNG AARALIFDSV YDSYRGIVTY IRMVDGELKS REKLHMMGIG
MTHDPIEIGV ISPDMTPTKA LGAGEVGYVI TGAKDVSQSK VGDTITSAVN PASEPLEGYR
DPKPMVYAGL FPIDNAQFPE LRDALDKLKL NDAALIYEPE TSVALGFGFR CGFLGLLHME
IVSERLSREF GLDLISTAPN VTYDVTSEDG TEHHVTNPSE FPEGKIKRII EPMVAADIIA
PKDFIGAIMD LCQDHRGEMG TMEYISADRV EMHYRIPLAE IVFDFFDQLK SRTKGYASLD
YHEDGEQAAD LVKVDILIQG DKVDAFSAIV HRDKAYSYGV MMTKKLRGLI PRQQFEIPIQ
AAIGSRIIAR ETISALRKDV LAKCYGGDIT RKRKLLEKQK AGKKRMKMLG HVEVPQEAFV
AALATDDGAN DRDTKDKIRA AQKSEG
//
