ID   EF1B_SULAC              Reviewed;          90 AA.
AC   Q4JAN4;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 2.
DT   25-MAY-2022, entry version 73.
DE   RecName: Full=Elongation factor 1-beta {ECO:0000255|HAMAP-Rule:MF_00043};
DE            Short=EF-1-beta {ECO:0000255|HAMAP-Rule:MF_00043};
DE   AltName: Full=aEF-1beta {ECO:0000255|HAMAP-Rule:MF_00043};
GN   Name=ef1b {ECO:0000255|HAMAP-Rule:MF_00043}; OrderedLocusNames=Saci_0772;
OS   Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC
OS   15157 / NCIMB 11770).
OC   Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC   Sulfolobus.
OX   NCBI_TaxID=330779;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770;
RX   PubMed=15995215; DOI=10.1128/jb.187.14.4992-4999.2005;
RA   Chen L., Bruegger K., Skovgaard M., Redder P., She Q., Torarinsson E.,
RA   Greve B., Awayez M., Zibat A., Klenk H.-P., Garrett R.A.;
RT   "The genome of Sulfolobus acidocaldarius, a model organism of the
RT   Crenarchaeota.";
RL   J. Bacteriol. 187:4992-4999(2005).
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. {ECO:0000255|HAMAP-
CC       Rule:MF_00043}.
CC   -!- SIMILARITY: Belongs to the EF-1-beta/EF-1-delta family.
CC       {ECO:0000255|HAMAP-Rule:MF_00043}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAY80145.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; CP000077; AAY80145.1; ALT_INIT; Genomic_DNA.
DR   AlphaFoldDB; Q4JAN4; -.
DR   SMR; Q4JAN4; -.
DR   STRING; 330779.Saci_0772; -.
DR   EnsemblBacteria; AAY80145; AAY80145; Saci_0772.
DR   KEGG; sai:Saci_0772; -.
DR   PATRIC; fig|330779.12.peg.738; -.
DR   eggNOG; arCOG01988; Archaea.
DR   HOGENOM; CLU_165896_1_0_2; -.
DR   Proteomes; UP000001018; 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   3: Inferred from homology;
KW   Elongation factor; Protein biosynthesis; Reference proteome.
FT   CHAIN           1..90
FT                   /note="Elongation factor 1-beta"
FT                   /id="PRO_0000155067"
SQ   SEQUENCE   90 AA;  10058 MW;  D7D5577F96F51794 CRC64;
     MDVLVILKVF PESDEINLTQ LSEEIKKRLP EGYRLVKNET EPIAYGLKAL IAYIQMPENT
     EGGTDKLEEL VNGIEGVSHA EVVNVTRLGF