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Database: UniProt
Entry: A0A135L2H7_9BACI
LinkDB: A0A135L2H7_9BACI
Original site: A0A135L2H7_9BACI 
ID   A0A135L2H7_9BACI        Unreviewed;       640 AA.
AC   A0A135L2H7;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   28-JAN-2026, entry version 40.
DE   RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE   AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN   ORFNames=U473_03705 {ECO:0000313|EMBL:KXG43218.1};
OS   Tepidibacillus decaturensis.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC   Tepidibacillus.
OX   NCBI_TaxID=1413211 {ECO:0000313|EMBL:KXG43218.1, ECO:0000313|Proteomes:UP000070352};
RN   [1] {ECO:0000313|EMBL:KXG43218.1, ECO:0000313|Proteomes:UP000070352}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Z9 {ECO:0000313|EMBL:KXG43218.1,
RC   ECO:0000313|Proteomes:UP000070352};
RA   Dong Y., Chang J.Y., Sanford R., Fouke B.W.;
RT   "Draft Genome for Tepidibacillus decaturensis nov. sp. Strain Z9, an
RT   Anaerobic, Moderately Thermophilic and Heterotrophic Bacterium from Deep
RT   Subsurface of the Illinois Basin, USA.";
RL   Submitted (FEB-2016) 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:KXG43218.1}.
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DR   EMBL; LSKU01000001; KXG43218.1; -; Genomic_DNA.
DR   RefSeq; WP_068723448.1; NZ_LSKU01000001.1.
DR   AlphaFoldDB; A0A135L2H7; -.
DR   STRING; 1413211.U473_03705; -.
DR   OrthoDB; 9804504at2; -.
DR   Proteomes; UP000070352; 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:InterPro.
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   FunFam; 2.40.30.10:FF:000020; Translation elongation factor EF-1; 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; ELONGATION FACTOR TU-RELATED; 1.
DR   PANTHER; PTHR43721:SF11; SELENOCYSTEINE-SPECIFIC ELONGATION FACTOR; 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; 3.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
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:UP000070352}.
FT   DOMAIN          2..174
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   640 AA;  72990 MW;  1C0D04DEA0054530 CRC64;
     MQKHYIVGTA GHIDHGKTTL SKALTGKDTD RLKEEKERNI SIELGFAPFL LPNGDQVSLI
     DVPGHEKFIR HMVAGVGGID LVLLVIAADE GIMPQTKEHM QIIELLGIEH GVIVLTKKDL
     IDDEFLQLVV EEVKETIEDT ILKDAPIICV SSTTNEGIEE LKQMIQNQLQ LIPERTYTGF
     FRMPIDRVFT LKGIGTVVTG TVYSGNVEVG QELEILPSNH KVRVRSLQVH SESVDQAFAG
     QRVAINLTGI EIEDLKRGDS VVTPKQWEPS ERVDIQLHIL KDIDFSIKQN TEVKFHVGTS
     EVLGTLLLYD RKEALPGDTV YCQIKLEEPI ISSRKERFII RRPSPAATIG GGMIIEPNAE
     KHKYRQETVE LLKQKSKGTL EDLLLHQFLT LPQIFLSLTD LSNLFVLPDT EILVGVNKLI
     QNHKVSPFNQ SSVPFYASSD RLAELENKIT SFLEGYHTTY SIRKGQAKSE LIKQFLPKIK
     PKMAQEILQY WQDKTLLKVK DDYISLFTFS PHLPEELRKK AELLEKKLIQ QEFNPDTWDD
     LTKEFGINDK EKNELFSFLI NQGRIYKLTD KMVIHAQSFD KLKKLVTDFL MKEKQITIQQ
     AKDLLNVSRK YLVPLLELLD QEKVTVLRQG QNYRELRSLN
//
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