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Database: UniProt
Entry: A0A0F4M068_9LACO
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ID   A0A0F4M068_9LACO        Unreviewed;       632 AA.
AC   A0A0F4M068;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   28-JAN-2026, entry version 39.
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:KJY63236.1};
GN   ORFNames=JG30_01470 {ECO:0000313|EMBL:KJY63236.1};
OS   Bombilactobacillus mellifer.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Bombilactobacillus.
OX   NCBI_TaxID=1218492 {ECO:0000313|EMBL:KJY63236.1, ECO:0000313|Proteomes:UP000033558};
RN   [1] {ECO:0000313|EMBL:KJY63236.1, ECO:0000313|Proteomes:UP000033558}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Bin4 {ECO:0000313|EMBL:KJY63236.1,
RC   ECO:0000313|Proteomes:UP000033558};
RA   Ellegaard K.M., Tamarit D., Javelind E., Olofsson T., Andersson S.G.,
RA   Vasquez A.;
RT   "Comparative genomics of the lactic acid bacteria isolated from the honey
RT   bee gut.";
RL   Submitted (JAN-2015) 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:KJY63236.1}.
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DR   EMBL; JXJQ01000002; KJY63236.1; -; Genomic_DNA.
DR   RefSeq; WP_046315319.1; NZ_JBHSZT010000003.1.
DR   AlphaFoldDB; A0A0F4M068; -.
DR   STRING; 1218492.JG30_01470; -.
DR   PATRIC; fig|1218492.5.peg.260; -.
DR   HOGENOM; CLU_023030_3_0_9; -.
DR   Proteomes; UP000033558; 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; 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   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; 2.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Elongation factor {ECO:0000313|EMBL:KJY63236.1};
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:UP000033558}.
FT   DOMAIN          1..175
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   632 AA;  70083 MW;  49BCE96B4D671CE9 CRC64;
     MDQVVIATAG HVDHGKTTLI KSLTGVDTDT TKEEKQRGLT INLGFTFFQL PNHQRVGIVD
     VPGHEKFLKN MLSGLSGIDL VLLVVDVNEG VMPQTREHAQ ILRLLGITNF IIVLTKVQTV
     DADMVELAVE DIRTTFAADP VLAAAPMVQT DAVSNYGMEH LVQVIQQLVN HIPPRKNTGQ
     ARMNIDRSFT MKGFGTVVTG TLLEGPIHTG DNICLYPTQK TTQVKNIRTY DYATDIALPG
     QRTALNLTLP HDEIRRGDVL ATADSVQVTK EFNAQLTTLA LPQSVLKLNT RVRVYVGSME
     VMGRLYPLGS EQIPAHATAN VQIRLEKPVT IKYGDYFIIR SYSPITTLGG GQILDGAPPT
     RKRYDAAMLN TLKIRSQGQL PAILLDYCLG QSLYWFDPAA GAIAFNESST EIQKAVQQLV
     QTKDLIALAG ELLVAQNVAQ AGQQIQTQLN HYHQQFPLRW GIPVSILTSR WTKDVGAKAT
     HLIFQYLKQQ QALAVTKGCY HLVNFQPQIN SQDQQVQATI QAKLKAAGSK PPAIAELIAH
     QPNGQEVLNA MIGDSVVLLD NTTVMDQAVY QQLVAQVVDF LQRHHTMSLA DYRDLTHSSR
     KYAMLVLERM DKDQITERWQ NKRILKKSVI NK
//
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