ID Q1MPY9_LAWIP Unreviewed; 641 AA.
AC Q1MPY9;
DT 30-MAY-2006, integrated into UniProtKB/TrEMBL.
DT 30-MAY-2006, sequence version 1.
DT 28-JAN-2026, entry version 115.
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:CAJ54938.1};
GN OrderedLocusNames=LI0884 {ECO:0000313|EMBL:CAJ54938.1};
OS Lawsonia intracellularis (strain PHE/MN1-00).
OC Bacteria; Pseudomonadati; Thermodesulfobacteriota; Desulfovibrionia;
OC Desulfovibrionales; Desulfovibrionaceae; Lawsonia.
OX NCBI_TaxID=363253 {ECO:0000313|EMBL:CAJ54938.1, ECO:0000313|Proteomes:UP000002430};
RN [1] {ECO:0000313|EMBL:CAJ54938.1, ECO:0000313|Proteomes:UP000002430}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PHE/MN1-00 {ECO:0000313|EMBL:CAJ54938.1,
RC ECO:0000313|Proteomes:UP000002430};
RA Kaur K., Zhang Q., Beckler D., Munir S., Li L., Kinsley K., Herron L.,
RA Peterson A., May B., Singh S., Gebhart C., Kapur V.;
RT "The complete genome sequence of Lawsonia intracellularis: the causative
RT agent of proliferative enteropathy.";
RL Submitted (NOV-2005) 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; AM180252; CAJ54938.1; -; Genomic_DNA.
DR RefSeq; WP_011526967.1; NC_008011.1.
DR AlphaFoldDB; Q1MPY9; -.
DR STRING; 363253.LI0884; -.
DR KEGG; lip:LI0884; -.
DR eggNOG; COG3276; Bacteria.
DR HOGENOM; CLU_023030_3_0_7; -.
DR OrthoDB; 9803139at2; -.
DR Proteomes; UP000002430; 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: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; 3.40.50.300:FF:001064; Selenocysteine-specific translation elongation factor; 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; 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; IPR031157; G_TR_CS.
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; 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:CAJ54938.1};
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:UP000002430}.
FT DOMAIN 1..171
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
SQ SEQUENCE 641 AA; 71622 MW; 1FF14DCD8DC015A8 CRC64;
MSIVIGTAGH IDHGKTSLVQ ILTGINCDKL SEEKRRGITI DLGFAYYVSP TGEKLSIIDV
PGHEKFIKNM VAGASGIDVV MLVIAADEGV MPQTKEHIEI CSLLGIKHGF IVLTKTDIVD
KEWLEVIKED IKLFLKNTFL HNTPILQVSS TTGEGIKNLK THLNHYLSIP HSKQKTDIFR
LPIDRVFTIK GHGTVVTGTI ASGSIATGEA ITILPSNKKT KVKQIQYHGN IVETAYAGQR
TAINLHGINT SEVKRGDILA HPDTLVLSTR WLISLTCLPS SPRPLKHCSE VHLHHGTQEI
LAQLYFFNKN SLAPGETILC EIRLKKPLVG IFGDHVVIRT FSPLQTVAGG SIVNPIASPI
SRHTITDHTI DTLLSLPSAT EEELVKKQIE FLDATGIYLT TLSIVTNIEH NRLLSILTSF
IERGIIICFD KENYGYLSVN TMKTLVEQCL VAITNFHKKN PIKQGIEQGT FFTNYKIWGK
ILPHKLIGFI INQLIQKGNL TSEGNYIYLP SHTISLSFEQ QHLYDNILKL YIEAGYTPPK
LSNILTTLNS TIKQATPIIT LLLERKALTH ITEDMYYSTQ AIKKLKSILQ NWFNSHKELD
IATFKELSGG LPRKYSIPLL EYFDKEKLTI RIGDKRQLRN P
//
