ID A0A366XVI9_9BACI Unreviewed; 634 AA.
AC A0A366XVI9;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 28-JAN-2026, entry version 28.
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:RBW69588.1};
GN ORFNames=DS031_10175 {ECO:0000313|EMBL:RBW69588.1};
OS Bacillus taeanensis.
OC Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=273032 {ECO:0000313|EMBL:RBW69588.1, ECO:0000313|Proteomes:UP000253314};
RN [1] {ECO:0000313|EMBL:RBW69588.1, ECO:0000313|Proteomes:UP000253314}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BH030017 {ECO:0000313|EMBL:RBW69588.1,
RC ECO:0000313|Proteomes:UP000253314};
RA Liu R., Huang Z.;
RT "Lottiidibacillus patelloidae gen. nov., sp. nov., isolated from the
RT intestinal tract of a marine limpet and the reclassification of B.
RT taeanensis BH030017T, B. algicola KMM 3737T and B. hwajinpoensis SW-72T as
RT genus Lottiidibacillus.";
RL Submitted (JUL-2018) 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:RBW69588.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QOCW01000009; RBW69588.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A366XVI9; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000253314; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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; 2.
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:RBW69588.1};
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:UP000253314}.
FT DOMAIN 3..174
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 634 AA; 73208 MW; 2282A39C4636702A CRC64;
MDTKYYTIGM AGHIDHGKTT LTKALTNVDT DRLKEEKERN ISIELGYAPL HMKDNMHVSV
VDVPGHERFI RQMIAGVAGI DLVLLVIAAD EGTMPQTKEH IEILEFLGIK RCIVVITKID
TVDEEFLEIV TLDIQEQLAS TVFHDASVVY ADSISKKGID ELKEKIFYEL NEIETRDSYG
SFRLPIDQVF TVQGQGTVVR GTIYEGLVRK GSPLIVLPQQ KKVKARQIQV HHQETDEARA
GQRTAINLGG ITKEEVQRGD VLVSSDHFLV TKVIDVSLKF VDEMNSPIKQ RSLVKIHVGT
SEVMGTIVFF DRNEVKQTSD EVLCQLRLHE EVVVRRGDRF ILRRPTPVET VGGGWVIDPK
GEKYRFGVET IEALMKKKEG TPEDRLKDVL FEYKLLDMQQ IMQYTSLNEH ELHDVLKKEV
ENNNIIEMTN DRFILSHQLI TLQDELVNAV KDYHEQYPMR IGINKAELVQ SYRDFYPKLY
VEFAVEKLVE KSKLKKSEQY IALQSFASHF PKKWEKRMNQ IIDHLKSDGI AVKRWEEYVK
ASQIPEKEIV DLQTFLLQSG EAYKLDEHLL VHKLSFEKAL SHLKQETEQS FDLKTAKEIL
ELPRKYLIPF LELLDELKLT SRLENERKWV KLKQ
//
