(data stored in SCRATCH zone)

SWISSPROT: LEPA_BACSU

ID   LEPA_BACSU              Reviewed;         612 AA.
AC   P37949;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-1996, sequence version 2.
DT   11-DEC-2019, entry version 137.
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}; Synonyms=yqeQ, yqxB;
GN   OrderedLocusNames=BSU25510;
OS   Bacillus subtilis (strain 168).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=224308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=8757728; DOI=10.1099/13500872-142-7-1641;
RA   Homuth G., Heinemann M., Zuber U., Schumann W.;
RT   "The genes of lepA and hemN form a bicistronic operon in Bacillus
RT   subtilis.";
RL   Microbiology 142:1641-1649(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=168 / JH642;
RX   PubMed=8969508; DOI=10.1099/13500872-142-11-3103;
RA   Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M.,
RA   Kobayashi Y.;
RT   "Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the
RT   Bacillus subtilis genome containing the skin element and many sporulation
RT   genes.";
RL   Microbiology 142:3103-3111(1996).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=168;
RX   PubMed=9384377; DOI=10.1038/36786;
RA   Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA   Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA   Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA   Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA   Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA   Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA   Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA   Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA   Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA   Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA   Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA   Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA   Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA   Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA   Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA   Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA   Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA   Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA   Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA   Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA   Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA   Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA   Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA   Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA   Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA   Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA   Yoshikawa H., Danchin A.;
RT   "The complete genome sequence of the Gram-positive bacterium Bacillus
RT   subtilis.";
RL   Nature 390:249-256(1997).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-327.
RC   STRAIN=168;
RA   Takemaru K., Sato T., Kobayashi Y.;
RL   Submitted (SEP-1993) 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: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}.
DR   EMBL; X91655; CAA62842.1; -; Genomic_DNA.
DR   EMBL; D84432; BAA12460.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB14493.1; -; Genomic_DNA.
DR   EMBL; D17650; BAA04544.1; -; Genomic_DNA.
DR   PIR; G69649; G69649.
DR   RefSeq; NP_390429.1; NC_000964.3.
DR   RefSeq; WP_003229999.1; NZ_JNCM01000036.1.
DR   SMR; P37949; -.
DR   IntAct; P37949; 1.
DR   STRING; 224308.BSU25510; -.
DR   jPOST; P37949; -.
DR   PaxDb; P37949; -.
DR   PRIDE; P37949; -.
DR   EnsemblBacteria; CAB14493; CAB14493; BSU25510.
DR   GeneID; 937840; -.
DR   KEGG; bsu:BSU25510; -.
DR   PATRIC; fig|224308.179.peg.2772; -.
DR   eggNOG; ENOG4105C4S; Bacteria.
DR   eggNOG; COG0481; LUCA.
DR   HOGENOM; HOG000020624; -.
DR   InParanoid; P37949; -.
DR   KO; K03596; -.
DR   OMA; KPMVFCG; -.
DR   PhylomeDB; P37949; -.
DR   BioCyc; BSUB:BSU25510-MONOMER; -.
DR   Proteomes; UP000001570; 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   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; TF_GTP-bd_dom.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
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; 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;
DR   PRODOM; P37949.
DR   SWISS-2DPAGE; P37949.
KW   Cell membrane; GTP-binding; Hydrolase; Membrane; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..612
FT                   /note="Elongation factor 4"
FT                   /id="PRO_0000176232"
FT   DOMAIN          12..194
FT                   /note="tr-type G"
FT   NP_BIND         24..29
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
FT   NP_BIND         141..144
FT                   /note="GTP"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00071"
SQ   SEQUENCE   612 AA;  68587 MW;  B1C7D65173A73B4C CRC64;
     MTDKEKRLER QSRIRNFSII AHIDHGKSTL ADRILEKTSA ITQREMKEQL LDSMDLERER
     GITIKLNSVQ LKYKAKDGEE YIFHLIDTPG HVDFTYEVSR SLAACEGAIL VVDAAQGIEA
     QTLANVYLAL DNDLEILPVI NKIDLPSAEP ERVRQEVEDV IGLDASEAVL ASAKAGIGIE
     EILEQIVEKV PAPTGDPEAP LKALIFDSLY DAYRGVVAYI RVVEGTVKPG QKIKMMATGK
     EFEVTEVGVF TPKATPTNEL TVGDVGFLTA SIKNVGDTRV GDTITSAANP AEEALPGYRK
     LNPMVYCGLY PIDTAKYNDL REALEKLELN DSSLQYEAET SQALGFGFRC GFLGMLHMEI
     IQERIEREFN IDLITTAPSV IYDVYMTDGE KVVVDNPSNM PDPQKIERVE EPYVKATMMV
     PNDYVGAVME LCQGKRGNFI DMQYLDANRV SIIYDMPLAE IVYEFFDQLK SSTKGYASFD
     YELIGYKPSK LVKMDIMLNG EKIDALSFIV HRDYAYERGK VIVEKLKELI PRQQFEVPVQ
     AAIGQKIVAR STIKAMRKNV LAKCYGGDIS RKRKLLEKQK EGKRRMKQVG SVEVPQEAFM
     AVLKMDDSPK KQ
//

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