ID A0A2Z5G675_9BACT Unreviewed; 633 AA.
AC A0A2Z5G675;
DT 10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT 10-OCT-2018, sequence version 1.
DT 28-JAN-2026, entry version 29.
DE RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN ORFNames=ACPOL_4790 {ECO:0000313|EMBL:AXC14056.1};
OS Acidisarcina polymorpha.
OC Bacteria; Pseudomonadati; Acidobacteriota; Terriglobia; Terriglobales;
OC Acidobacteriaceae; Acidisarcina.
OX NCBI_TaxID=2211140 {ECO:0000313|EMBL:AXC14056.1, ECO:0000313|Proteomes:UP000253606};
RN [1] {ECO:0000313|EMBL:AXC14056.1, ECO:0000313|Proteomes:UP000253606}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SBC82 {ECO:0000313|EMBL:AXC14056.1,
RC ECO:0000313|Proteomes:UP000253606};
RX PubMed=30510549; DOI=10.3389/fmicb.2018.02775;
RA Belova S.E., Ravin N.V., Pankratov T.A., Rakitin A.L., Ivanova A.A.,
RA Beletsky A.V., Mardanov A.V., Sinninghe Damste J.S., Dedysh S.N.;
RT "Hydrolytic Capabilities as a Key to Environmental Success: Chitinolytic
RT and Cellulolytic Acidobacteria From Acidic Sub-arctic Soils and Boreal
RT Peatlands.";
RL Front. Microbiol. 9:2775-2775(2018).
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; CP030840; AXC14056.1; -; Genomic_DNA.
DR RefSeq; WP_114208916.1; NZ_CP030840.1.
DR AlphaFoldDB; A0A2Z5G675; -.
DR KEGG; abas:ACPOL_4790; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000253606; Chromosome.
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; IPR031157; G_TR_CS.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR015191; SelB_WHD4.
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 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; 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; PS00301; G_TR_1; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:AXC14056.1};
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:UP000253606}.
FT DOMAIN 5..187
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 633 AA; 69040 MW; 6F382EB2A24D5D38 CRC64;
MTPPLKSIVI GTAGHIDHGK TALIHALTGV DADRLPEEKR RGITIDLGFA SLDETAPDGT
PLRISFVDVP GHALFIRNML AGAGGVDAVL LVIAANEGVK PQTREHLAIC GLLGVRRGIT
TISKVDAVSP ERLDQVLTAV RAFLRGTFLD ASESRILPVS AKNGEGLAEL RHELRALAVD
TKVRQPDHVS RLPIDRAFMM KGFGTVVTGT LLSGTVFAGE SLALEPGGRT VRVRGLQTHG
HSEARVSAGS RVALNLTGIE VSKISRGQTF VEPEMLTATS TIDAEVMLLP GVAALKHRER
LHFHAFTTET LASVSLYGYN SVEPGAKRIV RLKLNDPVLL LPGDRFVLRQ LSPAATIGGG
RVLDAQPIEK LKKAECLAWL ESMGNASLEE QVKLRIGRRK TRGVSLRELV RETGLTPEAM
IRHLNILVSR NNLGRFAGDL FLTKDAVEAA AEAVLLRLEM KSNQKGIKLS ELKSQIGLSG
EVFEYLVEGL FAEQKLCRQG EMVFSRGAAP QPSGEDDPIQ SKIEGIYKNA GLASPSTNEV
ATVLGITDDQ MRRSMTMLLR DKTMVRMGTD PVYIHRQALD ELRAQFKGFR GQTIDVARFK
QITGLSRKYA IPLLEYLDRE RVTRKEGDRR LVL
//
