ID B5EJ40_CITBB Unreviewed; 636 AA.
AC B5EJ40;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 28-JAN-2026, entry version 96.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN Name=selB {ECO:0000313|EMBL:ACH37066.1};
GN OrderedLocusNames=Gbem_0035 {ECO:0000313|EMBL:ACH37066.1};
OS Citrifermentans bemidjiense (strain ATCC BAA-1014 / DSM 16622 / JCM 12645 /
OS Bem) (Geobacter bemidjiensis).
OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfuromonadia;
OC Geobacterales; Geobacteraceae; Citrifermentans.
OX NCBI_TaxID=404380 {ECO:0000313|EMBL:ACH37066.1, ECO:0000313|Proteomes:UP000008825};
RN [1] {ECO:0000313|EMBL:ACH37066.1, ECO:0000313|Proteomes:UP000008825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1014 / DSM 16622 / JCM 12645 / Bem
RC {ECO:0000313|Proteomes:UP000008825};
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Kiss H., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Lovley D., Richardson P.;
RT "Complete sequence of Geobacter bemidjiensis BEM.";
RL Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACH37066.1, ECO:0000313|Proteomes:UP000008825}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1014 / DSM 16622 / JCM 12645 / Bem
RC {ECO:0000313|Proteomes:UP000008825};
RX PubMed=20828392; DOI=10.1186/1471-2164-11-490;
RA Aklujkar M., Young N.D., Holmes D., Chavan M., Risso C., Kiss H.E.,
RA Han C.S., Land M.L., Lovley D.R.;
RT "The genome of Geobacter bemidjiensis, exemplar for the subsurface clade of
RT Geobacter species that predominate in Fe(III)-reducing subsurface
RT environments.";
RL BMC Genomics 11:490-490(2010).
CC -!- FUNCTION: Translation factor necessary for the incorporation of
CC selenocysteine into proteins. It probably replaces EF-Tu for the
CC insertion of selenocysteine directed by the UGA codon. SelB binds GTP
CC and GDP. {ECO:0000256|ARBA:ARBA00025526}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496}.
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DR EMBL; CP001124; ACH37066.1; -; Genomic_DNA.
DR RefSeq; WP_012528476.1; NC_011146.1.
DR AlphaFoldDB; B5EJ40; -.
DR STRING; 404380.Gbem_0035; -.
DR KEGG; gbm:Gbem_0035; -.
DR eggNOG; COG3276; Bacteria.
DR HOGENOM; CLU_023030_3_0_7; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000008825; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0003746; F:translation elongation factor activity; IEA:UniProtKB-KW.
DR GO; GO:0001514; P:selenocysteine incorporation; IEA:InterPro.
DR CDD; cd04171; SelB; 1.
DR CDD; cd03696; SelB_II; 1.
DR CDD; cd15491; selB_III; 1.
DR FunFam; 3.40.50.300:FF:001064; Selenocysteine-specific translation elongation factor; 1.
DR Gene3D; 1.10.10.2770; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 1.
DR Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
DR InterPro; IPR057335; Beta-barrel_SelB.
DR InterPro; IPR050055; EF-Tu_GTPase.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR015190; Elong_fac_SelB-wing-hlx_typ-2.
DR InterPro; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015191; SelB_WHD4.
DR InterPro; IPR005225; Small_GTP-bd.
DR InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR InterPro; IPR009000; Transl_B-barrel_sf.
DR InterPro; IPR009001; Transl_elong_EF1A/Init_IF2_C.
DR InterPro; IPR004535; Transl_elong_SelB.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR NCBIfam; TIGR00475; selB; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43721:SF22; ELONGATION FACTOR TU, MITOCHONDRIAL; 1.
DR PANTHER; PTHR43721; ELONGATION FACTOR TU-RELATED; 1.
DR Pfam; PF25461; Beta-barrel_SelB; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF09106; WHD_2nd_SelB; 1.
DR Pfam; PF09107; WHD_3rd_SelB; 1.
DR PRINTS; PR00315; ELONGATNFCT.
DR SUPFAM; SSF50465; EF-Tu/eEF-1alpha/eIF2-gamma C-terminal domain; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR SUPFAM; SSF46785; Winged helix' DNA-binding domain; 3.
DR PROSITE; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:ACH37066.1};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW Reference proteome {ECO:0000313|Proteomes:UP000008825}.
FT DOMAIN 1..174
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 636 AA; 69227 MW; 89214218DF2BB0A5 CRC64;
MKHLILGTAG HIDHGKTSLV KALTGVDTDR LKEEKARGIT IELGFAHLEL PGDLRFGIVD
VPGHERFVRT MVAGVGGMDL VLLVIAADEG IMPQTREHLE ICQLLGVKRG IVVLSKKDTV
EPDWLDLVTE EVREYLAESF LAGAPIVAVS SRTGDGIEAL KAELTRMAGE IEQKRVDSPF
RLPVDRVFTV TGFGTVVTGT LLSGAVSVGD EVEILPSGIA CRVRGVQSFG SKVEKGGAGE
RLAVNLQGVD HTDVERGDVV VPKGLYQPTS AVDVRLNYLA SAGKELKHRA TVRLHSATYE
VPAKIILFDR GALQPGESAY VQLRLSRPVL LLPGDPFVLR TYSPQATLGG GTVLDPAPPR
RRRRSVEALE LLAAAESGAD QERIRLLVES SLLSGISVQE MVNRSGMSAK RIEAALAPLL
SSGAAIQVVK EPRIFLGKDA FAQLKQKLSG ELHDYLEENP MQEGIGKEEL KSRIPKRSDP
RFFGPLLASM EKDGQALSDR DLVKLPGRKA GVTQDQASVQ AALEEALKKG WCEPPTLKEL
CDMLGCSEKQ VLDHANLLTR EGRVAKIKGD IFYAPGAVAE LREKLVARLK EKGEITPPEF
REVTGLSRKF MIPLLEYFDS EKLTIRMGDK RILRKG
//
