ID A0A7S7L5J7_9BACI Unreviewed; 642 AA.
AC A0A7S7L5J7;
DT 02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 1.
DT 28-JAN-2026, entry version 20.
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:QOY34785.1};
GN ORFNames=AWH56_018965 {ECO:0000313|EMBL:QOY34785.1};
OS Anaerobacillus isosaccharinicus.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC Anaerobacillus.
OX NCBI_TaxID=1532552 {ECO:0000313|EMBL:QOY34785.1, ECO:0000313|Proteomes:UP000180175};
RN [1] {ECO:0000313|EMBL:QOY34785.1, ECO:0000313|Proteomes:UP000180175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NB2006 {ECO:0000313|EMBL:QOY34785.1,
RC ECO:0000313|Proteomes:UP000180175};
RX PubMed=28104661;
RA Bassil N.M., Lloyd J.R.;
RT "Draft Genome Sequences of Four Alkaliphilic Bacteria Belonging to the
RT Anaerobacillus Genus.";
RL Genome Announc. 5:e01493-e01416(2017).
RN [2] {ECO:0000313|EMBL:QOY34785.1, ECO:0000313|Proteomes:UP000180175}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NB2006 {ECO:0000313|EMBL:QOY34785.1,
RC ECO:0000313|Proteomes:UP000180175};
RX PubMed=29580368;
RA Bassil N.M., Lloyd J.R.;
RT "Anaerobacillus isosaccharinicus sp. nov., an alkaliphilic bacterium which
RT degrades isosaccharinic acid.";
RL Int. J. Syst. Evol. Microbiol. 69:3666-3671(2019).
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; CP063356; QOY34785.1; -; Genomic_DNA.
DR RefSeq; WP_182081010.1; NZ_CP063356.2.
DR AlphaFoldDB; A0A7S7L5J7; -.
DR KEGG; aia:AWH56_018965; -.
DR Proteomes; UP000180175; 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 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:QOY34785.1};
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:UP000180175}.
FT DOMAIN 3..175
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 642 AA; 72913 MW; B08FE758CEB0403D CRC64;
MGDRFYTIGM AGHIDHGKTT LTKALTNIDT DRLKEEKERN ISIELGFAPL KLKSDIQVSV
IDVPGHERFI RQMIAGVAGI DLVMLIVSAD EGVMPQTKEH LDILSLLGIK KGIVVVTKID
RVDEELLELV QEDIAMEVEG TFLENAPFVF VDSLSGKGID HLKEVIEENL TDVPSRDAKG
AFRLPIDQVF TVHGQGTVVR GTIYEGSIQE GDILEILPQG VKVRARQLQV HHEKKEKGFA
GQRTAINLGG VTKEDVKRGD VLVSTQQYST TSTIDISLQA LKGLDHPLKQ RGHIKLHLGT
AEVYGKIIFF DRNELAGDEA ETILCQLRLD EPIVTRRGDR FILRRPTPVE TIGGGFVIDP
NGEKYKFGEQ TINLLERKKE GTPLERIIDT LKEEKFLSVG QLQKLADLAE DVVSAALEEL
RENEQMIETE QGEVVLTSIF EEIVELISRD LEEFHEETPL REGKSKAEVL HSLKQSYPIK
LLEFTLTKSE QDQQLSRRGQ FIALAQFEPH FPKKWAKRME QVVNELESQG MQVEAWEYVV
GRAGLPVNFQ EDLKHYLIRT RKVIALDEKH FVSATHLRGA IKNLRDKTND EFELQDAKEV
LQLSRKYLVP FMELLDQLKL TVRIETKRQW QKVEYDKWIQ GK
//
