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Database: UniProt
Entry: K6DQU3_9BACI
LinkDB: K6DQU3_9BACI
Original site: K6DQU3_9BACI 
ID   K6DQU3_9BACI            Unreviewed;       626 AA.
AC   K6DQU3;
DT   09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT   09-JAN-2013, sequence version 1.
DT   28-JAN-2026, entry version 54.
DE   RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE   AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN   ORFNames=BABA_04739 {ECO:0000313|EMBL:EKN70719.1};
OS   Neobacillus bataviensis LMG 21833.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC   Neobacillus.
OX   NCBI_TaxID=1117379 {ECO:0000313|EMBL:EKN70719.1, ECO:0000313|Proteomes:UP000006316};
RN   [1] {ECO:0000313|EMBL:EKN70719.1, ECO:0000313|Proteomes:UP000006316}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21833T {ECO:0000313|Proteomes:UP000006316};
RX   PubMed=23087684;
RA   Heylen K., Keltjens J.;
RT   "Redundancy and modularity in membrane-associated dissimilatory nitrate
RT   reduction in Bacillus.";
RL   Front. Microbiol. 3:371-371(2012).
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:EKN70719.1}.
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DR   EMBL; AJLS01000036; EKN70719.1; -; Genomic_DNA.
DR   RefSeq; WP_007083981.1; NZ_AJLS01000036.1.
DR   AlphaFoldDB; K6DQU3; -.
DR   STRING; 1117379.BABA_04739; -.
DR   PATRIC; fig|1117379.3.peg.983; -.
DR   eggNOG; COG3276; Bacteria.
DR   OrthoDB; 9804504at2; -.
DR   Proteomes; UP000006316; 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; 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:EKN70719.1};
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:UP000006316}.
FT   DOMAIN          3..174
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   626 AA;  71469 MW;  919CEC6CD4822F2B CRC64;
     MEKRYFTIGM AGHIDHGKTS LTKALTNVDT DRLKEEKERQ ISIELGFAPL YEDDEIQISV
     IDVPGHERFI RQMIAGVAGI DLVVLVVAAD EGVMPQTREH LDILKFLGIK NGVIAITKID
     RVDEEFIELV KDDILEELTN TVFEGAPFML VDSLSKKGIG ETKDLIIKTL MEQEMRDAKG
     AFRLPIDQVF TVKGQGTVVR GTVYEGTVEE GQALKIMPNG LEVRARQIQV HHKQAQKAYA
     GQRTAINLSN VSKEDLERGD VLVSSEHFIV TRTVDVAIRV VEDLEHLVKQ RMPIKLHIGT
     AEVMGRIVFF DRNEIKEENG EILCQLRLEE EILTKRGDRF ILRRPSPQET IGGGWVIDPL
     GNKYRFGNQT VEDLEKKKVG TPKERIMAAL VEGKSLQLNE LITRTALDDE ALTEQLSDND
     FVLYNDKEYT LHSIINSIEE DIFDRLQEFH LTHSMKAGVN KAELLHVLQK KFPKSLLDFV
     VENGIANEIF KRKEQYVSLK AFVPHVPKSW EKRTENLLME LKKDGLKVRY LKDYFSSAGI
     PETLEFDLKK FLEDQQLIVQ LDEKFAYHGE VFRGAVDKLR SQTGSEFEVG EAKEVLDLSR
     KYMIPFLERL DANGLTKRVE NKRVWK
//
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