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Database: UniProt
Entry: A0A7X0LWN6_9BACI
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ID   A0A7X0LWN6_9BACI        Unreviewed;       627 AA.
AC   A0A7X0LWN6;
DT   02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT   02-JUN-2021, sequence version 1.
DT   28-JAN-2026, entry version 21.
DE   RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE   AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN   ORFNames=HNR53_002193 {ECO:0000313|EMBL:MBB6445574.1};
OS   Bacillus benzoevorans.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1456 {ECO:0000313|EMBL:MBB6445574.1, ECO:0000313|Proteomes:UP000531594};
RN   [1] {ECO:0000313|EMBL:MBB6445574.1, ECO:0000313|Proteomes:UP000531594}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 5391 {ECO:0000313|EMBL:MBB6445574.1,
RC   ECO:0000313|Proteomes:UP000531594};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (AUG-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:MBB6445574.1}.
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DR   EMBL; JACHGK010000006; MBB6445574.1; -; Genomic_DNA.
DR   RefSeq; WP_184525724.1; NZ_JACHGK010000006.1.
DR   AlphaFoldDB; A0A7X0LWN6; -.
DR   Proteomes; UP000531594; 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   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; 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   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; 2.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Elongation factor {ECO:0000313|EMBL:MBB6445574.1};
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:UP000531594}.
FT   DOMAIN          1..172
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   627 AA;  71112 MW;  BDBB2DBB3298F9B6 CRC64;
     MDHFVIGTAG HVDHGKTTLI KAMTGMETDT TAEEKTRGLS INLGFAYMDL PSGKRAGIVD
     VPGHEKFIKN MMAGLSGIQL ILLVIDAGEG IMPQTKEHMD ILQILGIKNY IIVLTKANTV
     DQELVELVEE DIKEQLHGTL LEDAPIYKVD SLSGMGINEL IAEIDHVSQT IERASSLVPP
     RMHIDRVFSL KGFGTIVTGT LIEGALRIND ELVIYPKELR TKIRNIQVHE QNVDEAVAGM
     RVALNLANVH VNDVSRGDTL AVPESVQRTW MIDVQAHLLP HAEEPLKLWN RLRLHIGTRE
     ILCRTVPIGV KIVEPGEEAF LQLRLEEEIV AKRGDKFIIR SYSPMHVIGG GSILDTTPTK
     HRRFNEEIIQ TLETRAKGST NEMIDDFVVR KEELLTSKEE VVSYLGISQT EINETMADMV
     SSKQLLPVNQ QYMHPLKYEQ FKKEMAAILE HFHKTYSLRT GIIKEELRSR IAPDLKGKDF
     DRLLQMLAEE KLIKNHHDTI SLSEFTVTYN RAQLQEKEEI EQSLKQSGFT PPSEAELIGE
     HKERKEIIDS LVGKTIIRLD PETVIYKDYY DTAVEKVTEF IKGNGKMTLA EFRDMIGSNR
     KYSLIILEYL DKNKITRRVE DYRVLHS
//
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