LEPA_MYCPN
ID LEPA_MYCPN Reviewed; 598 AA.
AC P75498;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 05-MAR-2002, sequence version 2.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Elongation factor 4 {ECO:0000255|HAMAP-Rule:MF_00071};
DE Short=EF-4 {ECO:0000255|HAMAP-Rule:MF_00071};
DE EC=3.6.5.n1 {ECO:0000255|HAMAP-Rule:MF_00071};
DE AltName: Full=Ribosomal back-translocase LepA {ECO:0000255|HAMAP-Rule:MF_00071};
GN Name=lepA {ECO:0000255|HAMAP-Rule:MF_00071}; OrderedLocusNames=MPN_279;
GN ORFNames=MP556;
OS Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
RX PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT pneumoniae.";
RL Nucleic Acids Res. 24:4420-4449(1996).
RN [2]
RP IDENTIFICATION OF PROBABLE FRAMESHIFT.
RA Sinan C.;
RL Unpublished observations (FEB-2002).
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:0000255|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:0000255|HAMAP-Rule:MF_00071};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00071};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00071};
CC Cytoplasmic side {ECO:0000255|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:0000255|HAMAP-Rule:MF_00071}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB96204.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U00089; AAB96204.1; ALT_FRAME; Genomic_DNA.
DR PIR; S73882; S73882.
DR RefSeq; NP_109967.1; NC_000912.1.
DR RefSeq; WP_015344898.1; NZ_OU342337.1.
DR AlphaFoldDB; P75498; -.
DR SMR; P75498; -.
DR STRING; 272634.MPN_279; -.
DR PRIDE; P75498; -.
DR EnsemblBacteria; AAB96204; AAB96204; MPN_279.
DR KEGG; mpn:MPN_279; -.
DR PATRIC; fig|272634.6.peg.299; -.
DR HOGENOM; CLU_009995_3_3_14; -.
DR OMA; MVQIAIQ; -.
DR Proteomes; UP000000808; Chromosome.
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; cd03709; lepA_C; 1.
DR Gene3D; 3.30.70.2570; -; 1.
DR Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR43512; PTHR43512; 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; SSF50447; SSF50447; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF54980; SSF54980; 2.
DR TIGRFAMs; TIGR01393; lepA; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW Cell membrane; GTP-binding; Hydrolase; Membrane; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..598
FT /note="Elongation factor 4"
FT /id="PRO_0000176305"
FT DOMAIN 4..185
FT /note="tr-type G"
FT BINDING 16..21
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
FT BINDING 132..135
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
SQ SEQUENCE 598 AA; 68025 MW; 4E5A1A230763B57C CRC64;
MEQQKIRNFS IIAHIDHGKS TLSDRLIERS IGFEKRLLQA QMLDTMAIER ERGITIKLNA
VQLKMAQGNQ QYLFHLVDTP GHVDFTYEVS RSLAACEGVL LLVDATQGIQ AQTISNTYLA
LENNLEIIPV INKVDMESAD VEKTKQAFHQ LLGVDPNTIP LVSAKTGLGI DQLITTIIEK
VPPPKGDESK PLKALLFDSY YDPYKGVVCF IRIFEGSLKL NDKIRFARSN SVYQIVELGI
KNPFFEKQDV LKAGEIGWFS AGIKKLRDVT VGDTIVHAED TTTPPLPGYK KVLPMIYCGL
YPIDNNDYQN LKMAMEKIIL SDVALEYEYE TSQALGFGVR CGFLGLLHMD VIKERLEREY
NLKLISAPPS VRYKVLLTNG EELELDNPSL LPERSRIKSI SEPFVRVYID LPDHYLGTVI
DLCQNFRGQY EKLEEIDIDR KRLVYLMPLG EIIYSFFDKL KSITKGYASL NYEFDQYQVS
QLAKVEIMLN KQKVDALSFI AHHDFAFQRA KKFCVKLKEL IPKHLFEIPI QATIGSKVIA
RETIKAVRKD VTAKLYGGDV TRKKKLLEKQ KEGKKRLKAI GSVELPQELF SHLLKDED
