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Database: UniProt
Entry: K9B0S6_9MICO
LinkDB: K9B0S6_9MICO
Original site: K9B0S6_9MICO 
ID   K9B0S6_9MICO            Unreviewed;       615 AA.
AC   K9B0S6;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   28-JAN-2026, entry version 53.
DE   RecName: Full=Selenocysteine-specific elongation factor {ECO:0000256|ARBA:ARBA00015953};
DE   AltName: Full=SelB translation factor {ECO:0000256|ARBA:ARBA00031615};
GN   ORFNames=C272_05744 {ECO:0000313|EMBL:EKU48387.1};
OS   Brevibacterium casei S18.
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC   Brevibacteriaceae; Brevibacterium.
OX   NCBI_TaxID=1229781 {ECO:0000313|EMBL:EKU48387.1, ECO:0000313|Proteomes:UP000009879};
RN   [1] {ECO:0000313|EMBL:EKU48387.1, ECO:0000313|Proteomes:UP000009879}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S18 {ECO:0000313|EMBL:EKU48387.1,
RC   ECO:0000313|Proteomes:UP000009879};
RA   Sharma R., Singh A., Jangir P.K.;
RT   "Genome Sequence of Brevibacterium casei S18.";
RL   Submitted (SEP-2012) 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:EKU48387.1}.
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DR   EMBL; AMSP01000003; EKU48387.1; -; Genomic_DNA.
DR   RefSeq; WP_009376752.1; NZ_AMSP01000003.1.
DR   AlphaFoldDB; K9B0S6; -.
DR   PATRIC; fig|1229781.4.peg.1154; -.
DR   eggNOG; COG3276; Bacteria.
DR   OrthoDB; 9803139at2; -.
DR   Proteomes; UP000009879; 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   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; 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; 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   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 1.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   4: Predicted;
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Elongation factor {ECO:0000313|EMBL:EKU48387.1};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009879}.
FT   DOMAIN          1..170
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
SQ   SEQUENCE   615 AA;  64960 MW;  378CCF2DCEB78C8B CRC64;
     MFVVATAGHV DHGKSTLVKA LTGMEPDRWE EERRRGLTID LGFAWTTLPS GRELAFVDVP
     GHERFLANML AGVGPAPIVC FVIAADKGWQ AQSSDHRDAI AALGIDRGLV VVTRADLAPD
     TVTETEAQVR AELRGTTLAD APIVTVSATT GQGMDELIAR LDEVTAAAPA PDADARVRLW
     IDRAFSITGA GTVVTGTLTA GTLRAGDRVR VVGESVDLVT GIRGMQSRES SAEVVTPAAR
     VAVNVRDVPV DDIHRGDALI TPDAWPIVEV LDVRRTMGEA LDDGVHELML HIGTAAVPVR
     LRPFDAEHAR LTLERPLPLQ LGDRMVLRNP GSRNVFAGVV VLDVDPPELG RRGDGARRAA
     ALASRPVTGD VLAEVARRGA VERVVLVRFG LTVPEALPSG VEALGAWLVH APTLQAWVTA
     AKEVVAKQLA AQPMAPGVPV KAVVEALRRV DPPLPSAGAQ PAASPGSGTG IGALVAEVIR
     RAGLEAADGV VRPPGHRADL GPAEAGVAKV EQRLKANPFD APEADDLRAL CLGARELAVA
     EKAGRVLRLG DGVVVSPRTP AQAMRLLAGL DQPFTTSQAR RALGTTRRVV IPLLEHLDSR
     GWTRRLDGSH REVVR
//
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