ID A0A974XEB8_9FIRM Unreviewed; 639 AA.
AC A0A974XEB8;
DT 22-FEB-2023, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2023, sequence version 1.
DT 28-JAN-2026, entry version 15.
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:QSX08263.1};
GN ORFNames=J0B03_10790 {ECO:0000313|EMBL:QSX08263.1};
OS Alkalibacter rhizosphaerae.
OC Bacteria; Bacillati; Bacillota; Clostridia; Eubacteriales; Eubacteriaceae;
OC Alkalibacter.
OX NCBI_TaxID=2815577 {ECO:0000313|EMBL:QSX08263.1, ECO:0000313|Proteomes:UP000663499};
RN [1] {ECO:0000313|EMBL:QSX08263.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ES005 {ECO:0000313|EMBL:QSX08263.1};
RA Namirimu T., Yang J.-A., Yang S.-H., Kim Y.-J., Kwon K.K.;
RT "Alkalibacter marinus sp. nov., isolated from tidal flat sediment.";
RL Submitted (MAR-2021) 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}.
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DR EMBL; CP071444; QSX08263.1; -; Genomic_DNA.
DR RefSeq; WP_207299605.1; NZ_CP071444.1.
DR AlphaFoldDB; A0A974XEB8; -.
DR KEGG; alka:J0B03_10790; -.
DR Proteomes; UP000663499; 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:0035556; P:intracellular signal transduction; 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 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; IPR000591; DEP_dom.
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; PS50186; DEP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:QSX08263.1};
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:UP000663499}.
FT DOMAIN 1..177
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT DOMAIN 378..454
FT /note="DEP"
FT /evidence="ECO:0000259|PROSITE:PS50186"
SQ SEQUENCE 639 AA; 71578 MW; 3BEE056C9DAF1DE1 CRC64;
MKHITIGTAG HIDHGKTALV KRLTGTDTDR LAEEQDRGMT IELGFAFLQL ASGNQVSIVD
VPGHEKFVKT MVAGVTGIDI VLLIIAADEG IMPQTIEHLD ILSVLGLSKG VVALTKSDLV
DQKTLDQRIR EIRKYLKDTP LESLPVIPVS SKTGAGIDDL LIKIDELAIQ TREKSPTSLF
RLPVDRVFTM TGHGTIVTGT ISGGTVTKGD PVQILPEGLT TKVRNIQVRN QSVDQAYGGD
RCALNLASIE KKDLQRGSVV LESGNFRTTS LLDARVQMVP GSNGLVHNQR VHFHTGTTAV
LARVRLLGAD KIDAGEKGYV QLRLEEPVAA FRADRFILRS FSPVHTIGGG RLLLHHTRNR
KRFDSTSMKE LAFLDLGTDK EVIQWLIQSS SSLMDVESIY LETLIDRDRI KEMLEELVVE
GVIYAMGSTG KYYSLAWCDE MLKELEGVFH RFYNKNPYRY QISKEALRKK EFPFLSNKDF
DGMLEIMSAM SSLRLEEKFV HLHKEKRLDE ISDLVEVART RQLFETPDLP TLSPAQVAEE
TSLPIAVAEE ILHFFISIGY LVELEKGVFC SRRSLEMIYQ TVVDAIQKEK SITVARLRDL
LGTGRKTAIY FLEYFDAVRV TKRDGNDRIP GPRFRDFLH
//