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Database: UniProt
Entry: A0A923E914_CLOTT
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ID   A0A923E914_CLOTT        Unreviewed;       568 AA.
AC   A0A923E914;
DT   22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2023, sequence version 1.
DT   28-JAN-2026, entry version 15.
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:MBC2397341.1};
GN   ORFNames=HGG79_06060 {ECO:0000313|EMBL:MBC2397341.1};
OS   Clostridium tetanomorphum.
OC   Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1553 {ECO:0000313|EMBL:MBC2397341.1, ECO:0000313|Proteomes:UP000563151};
RN   [1] {ECO:0000313|EMBL:MBC2397341.1, ECO:0000313|Proteomes:UP000563151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DJ011 {ECO:0000313|EMBL:MBC2397341.1,
RC   ECO:0000313|Proteomes:UP000563151};
RA   Brown S.;
RT   "Genomic insights into acetone-butanol-ethanol (ABE) fermentation by
RT   sequencing solventogenic clostridia strains.";
RL   Submitted (APR-2020) to the EMBL/GenBank/DDBJ databases.
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:MBC2397341.1}.
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DR   EMBL; JAAZWO010000005; MBC2397341.1; -; Genomic_DNA.
DR   RefSeq; WP_035144377.1; NZ_JAAZWO010000005.1.
DR   AlphaFoldDB; A0A923E914; -.
DR   Proteomes; UP000563151; Unassembled WGS sequence.
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; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR   InterPro; IPR057335; Beta-barrel_SelB.
DR   InterPro; IPR050055; EF-Tu_GTPase.
DR   InterPro; IPR004161; EFTu-like_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; 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; 1.
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:MBC2397341.1};
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:UP000563151}.
FT   DOMAIN          1..172
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   568 AA;  65207 MW;  9BD5801D8C30D4F7 CRC64;
     MRHIVIGTAG HIDHGKTSLI KALTEQDTDR LKEEKKRGIS INLGFAYLDL PCGKRAGIID
     VPGHEKFIKN MLAGISSIDL VLMVIAADEG VMPQTREHLQ ILKLLDIKKG IVVLTKTDLV
     QKEWINIVKD EIKKEIQESF LQESKIYEVS CVTKKGIEEL IKALDDISEE LEEENIKEDF
     RMSVDRVFTV SGFGTVVTGT VLNGMVNQGE TIEIYPSKIN CKVRGIQVHE QKVNFAKIGQ
     RTALNLSNVK VKEIKRGDVI SSINAMESSI IIDCRLHYLK ENNKPLKNRQ RVRLHHGTSE
     ILCRVVILDK EDIRPGESVY VQLKLESPIA CKSEDRFIIR NYSPMYTIGG GIIIDPVSKK
     AKRFDKDYIN ELKIKENRNV EEILENVIKK FTEQVPDKNL IQKHLDIDDE VLKKEINKLK
     DKGKIIEICI DNNIRYIHNI YWKEKAKGLI EIYNEAGFSP PKYEEILEKE NNKKIFNIIY
     YSLIKNKDII IISEDIVLSC SNYYKAKRII IDTINKNGNI TLAEFRDILN TSRKYALAII
     EHFDSIKLTK RIGDKRILYS VDLKETFV
//
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