ID   EF1B_NITMS              Reviewed;          93 AA.
AC   A9A5W3;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   25-MAY-2022, entry version 64.
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=Nmar_1222;
OS   Nitrosopumilus maritimus (strain SCM1).
OC   Archaea; Thaumarchaeota; Nitrosopumilales; Nitrosopumilaceae;
OC   Nitrosopumilus.
OX   NCBI_TaxID=436308;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCM1;
RX   PubMed=20421470; DOI=10.1073/pnas.0913533107;
RA   Walker C.B., de la Torre J.R., Klotz M.G., Urakawa H., Pinel N., Arp D.J.,
RA   Brochier-Armanet C., Chain P.S., Chan P.P., Gollabgir A., Hemp J.,
RA   Hugler M., Karr E.A., Konneke M., Shin M., Lawton T.J., Lowe T.,
RA   Martens-Habbena W., Sayavedra-Soto L.A., Lang D., Sievert S.M.,
RA   Rosenzweig A.C., Manning G., Stahl D.A.;
RT   "Nitrosopumilus maritimus genome reveals unique mechanisms for
RT   nitrification and autotrophy in globally distributed marine crenarchaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:8818-8823(2010).
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}.
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DR   EMBL; CP000866; ABX13118.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9A5W3; -.
DR   SMR; A9A5W3; -.
DR   STRING; 436308.Nmar_1222; -.
DR   EnsemblBacteria; ABX13118; ABX13118; Nmar_1222.
DR   KEGG; nmr:Nmar_1222; -.
DR   eggNOG; arCOG01988; Archaea.
DR   HOGENOM; CLU_165896_1_0_2; -.
DR   OMA; YELEYFS; -.
DR   PhylomeDB; A9A5W3; -.
DR   Proteomes; UP000000792; 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..93
FT                   /note="Elongation factor 1-beta"
FT                   /id="PRO_0000366439"
SQ   SEQUENCE   93 AA;  10400 MW;  44689E2393C62EBE CRC64;
     MAQLLFITKI LPEGTDVDLD KLAETLKSTL PEGIQMKRHA KEPLAFGLEF LKAEFVLEDK
     EGQSDALENA VKNTEGVSEF EVLNMSRMSV DMK