EF1B_METTH
ID EF1B_METTH Reviewed; 89 AA.
AC O27734;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 25-MAY-2022, entry version 131.
DE RecName: Full=Elongation factor 1-beta;
DE Short=EF-1-beta;
DE AltName: Full=aEF-1beta;
GN Name=ef1b; OrderedLocusNames=MTH_1699;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
RN [2]
RP STRUCTURE BY NMR.
RX PubMed=10959626; DOI=10.1023/a:1008363304977;
RA Kozlov G., Ekiel I., Beglova N., Yee A., Dharamsi A., Engel A.,
RA Siddiqui N., Nong A., Gehring K.;
RT "Rapid fold and structure determination of the archaeal translation
RT elongation factor 1beta from Methanobacterium thermoautotrophicum.";
RL J. Biomol. NMR 17:187-194(2000).
CC -!- FUNCTION: Promotes the exchange of GDP for GTP in EF-1-alpha/GDP, thus
CC allowing the regeneration of EF-1-alpha/GTP that could then be used to
CC form the ternary complex EF-1-alpha/GTP/AAtRNA.
CC -!- MISCELLANEOUS: Binds calcium.
CC -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family. {ECO:0000305}.
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DR EMBL; AE000666; AAB86171.1; -; Genomic_DNA.
DR PIR; B69094; B69094.
DR RefSeq; WP_010877307.1; NC_000916.1.
DR PDB; 1GH8; NMR; -; A=1-89.
DR PDBsum; 1GH8; -.
DR AlphaFoldDB; O27734; -.
DR BMRB; O27734; -.
DR SMR; O27734; -.
DR STRING; 187420.MTH_1699; -.
DR EnsemblBacteria; AAB86171; AAB86171; MTH_1699.
DR GeneID; 24854799; -.
DR KEGG; mth:MTH_1699; -.
DR PATRIC; fig|187420.15.peg.1660; -.
DR HOGENOM; CLU_165896_0_0_2; -.
DR OMA; VMPNSPE; -.
DR EvolutionaryTrace; O27734; -.
DR Proteomes; UP000005223; Chromosome.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd00292; EF1B; 1.
DR Gene3D; 3.30.70.60; -; 1.
DR HAMAP; MF_00043; EF1_beta; 1.
DR InterPro; IPR036219; eEF-1beta-like_sf.
DR InterPro; IPR014038; EF1B_bsu/dsu_GNE.
DR InterPro; IPR014717; Transl_elong_EF1B/ribosomal_S6.
DR InterPro; IPR004542; Transl_elong_EF1B_B_arc.
DR PANTHER; PTHR39647; PTHR39647; 1.
DR Pfam; PF00736; EF1_GNE; 1.
DR PIRSF; PIRSF006521; Transl_elong_EF1B_B_arc; 1.
DR SMART; SM00888; EF1_GNE; 1.
DR SUPFAM; SSF54984; SSF54984; 1.
DR TIGRFAMs; TIGR00489; aEF-1_beta; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Elongation factor; Protein biosynthesis;
KW Reference proteome.
FT CHAIN 1..89
FT /note="Elongation factor 1-beta"
FT /id="PRO_0000155060"
FT STRAND 4..15
FT /evidence="ECO:0007829|PDB:1GH8"
FT HELIX 19..29
FT /evidence="ECO:0007829|PDB:1GH8"
FT STRAND 34..36
FT /evidence="ECO:0007829|PDB:1GH8"
FT STRAND 41..43
FT /evidence="ECO:0007829|PDB:1GH8"
FT STRAND 45..47
FT /evidence="ECO:0007829|PDB:1GH8"
FT STRAND 49..60
FT /evidence="ECO:0007829|PDB:1GH8"
FT HELIX 62..65
FT /evidence="ECO:0007829|PDB:1GH8"
FT HELIX 66..71
FT /evidence="ECO:0007829|PDB:1GH8"
FT STRAND 76..87
FT /evidence="ECO:0007829|PDB:1GH8"
SQ SEQUENCE 89 AA; 9532 MW; 17CC49327D3B773D CRC64;
MGDVVATIKV MPESPDVDLE ALKKEIQERI PEGTELHKID EEPIAFGLVA LNVMVVVGDA
EGGTEAAEES LSGIEGVSNI EVTDVRRLM