ID A0A2N6SNB1_9LACT Unreviewed; 633 AA.
AC A0A2N6SNB1;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-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 Name=selB {ECO:0000313|EMBL:PMC58574.1};
GN ORFNames=CJ205_03475 {ECO:0000313|EMBL:PMC58574.1};
OS Dolosicoccus paucivorans.
OC Bacteria; Bacillati; Bacillota; Bacilli; Lactobacillales; Aerococcaceae;
OC Dolosicoccus.
OX NCBI_TaxID=84521 {ECO:0000313|EMBL:PMC58574.1, ECO:0000313|Proteomes:UP000235682};
RN [1] {ECO:0000313|EMBL:PMC58574.1, ECO:0000313|Proteomes:UP000235682}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UMB0852 {ECO:0000313|EMBL:PMC58574.1,
RC ECO:0000313|Proteomes:UP000235682};
RA Thomas-White K., Kumar N., Forster S., Putonti C., Lawley T., Wolfe A.J.;
RT "Bacterial strain isolated from the female urinary microbiota.";
RL Submitted (SEP-2017) 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:PMC58574.1}.
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DR EMBL; PNHE01000010; PMC58574.1; -; Genomic_DNA.
DR RefSeq; WP_102227627.1; NZ_PNFY01000011.1.
DR AlphaFoldDB; A0A2N6SNB1; -.
DR STRING; 84521.SAMN04487994_10705; -.
DR OrthoDB; 9804504at2; -.
DR Proteomes; UP000235682; 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; 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; 3.
DR PROSITE; PS51722; G_TR_2; 1.
PE 4: Predicted;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW Elongation factor {ECO:0000313|EMBL:PMC58574.1};
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:UP000235682}.
FT DOMAIN 2..176
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 633 AA; 71546 MW; 63322C0D1F7F8295 CRC64;
MQQPFIIATA GHIDHGKTTL IKALTTIQTD TAPEEKKRGL TINLGFAYLD LADGTRAGII
DVPGHERFVK NMLAGAIGVD LGLLVIDANE GVMPQTVEHI DILTLLGVKH FIIVLTKVDG
LDQDLLELVH LDVEEFIQNT PLEGSPIIET DALKDIGLNE LKETIENFST QIKRASTQLP
ARLNVDRSFH VKGIGTIVTG TLLDGQLSLE DEVYVYPADG QSTVRSIQIH EQQQTAAYPG
NRTALNLTHV KREEVPRGSV ISHVPLSKTY MLDVKLTALP TNDEPIRFWD RVHLYSGTTE
ILARVVPLEE DVLPGTSRFA QLRLEEPLYI RKGDRFIIRQ FSPLKTLGGG QVIDAHPVKH
ASADEELLTS FQIKESGSVD KQLMDLLNQP QQFFLTKEAI VDTLHVPVDS LEQSLKKALK
KKWVVSVGEY YIARQVYDEL QQQMIELLDA YHEEHPHHKG MPLETFRAQM DYLPLVGVNH
LIDHLVQKGR ALNKNNQLTS GNFVVILTKK QQKLHEAIVK KLEEDGINPP TIKEVFPKEK
DDQVVFEWMK DEGELYQLDR DTVVLTSAYQ QAKDQVVNYL MKQETIELAE CRDLLATNRK
AALRLLDELD RQKVTMRTEN GRTLHPNYQR ERD
//
