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Database: UniProt
Entry: W4VEI3_9BACI
LinkDB: W4VEI3_9BACI
Original site: W4VEI3_9BACI 
ID   W4VEI3_9BACI            Unreviewed;       456 AA.
AC   W4VEI3;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   SubName: Full=Translation initiation factor 2 {ECO:0000313|EMBL:GAE91576.1};
GN   ORFNames=JCM21714_529 {ECO:0000313|EMBL:GAE91576.1};
OS   Gracilibacillus boraciitolerans JCM 21714.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Gracilibacillus.
OX   NCBI_TaxID=1298598 {ECO:0000313|EMBL:GAE91576.1, ECO:0000313|Proteomes:UP000019102};
RN   [1] {ECO:0000313|EMBL:GAE91576.1, ECO:0000313|Proteomes:UP000019102}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 21714 {ECO:0000313|EMBL:GAE91576.1,
RC   ECO:0000313|Proteomes:UP000019102};
RA   Ahmed I., Oshima K., Suda W., Kitamura K., Iida T., Ohmori Y., Fujiwara T.,
RA   Hattori M., Ohkuma M.;
RT   "Draft Genome Sequence of the Boron-Tolerant and Moderately Halotolerant
RT   Bacterium Gracilibacillus boraciitolerans JCM 21714T.";
RL   Genome Announc. 2:e00097-14(2014).
CC   -!- FUNCTION: One of the essential components for the initiation of protein
CC       synthesis. Protects formylmethionyl-tRNA from spontaneous hydrolysis
CC       and promotes its binding to the 30S ribosomal subunits. Also involved
CC       in the hydrolysis of GTP during the formation of the 70S ribosomal
CC       complex. {ECO:0000256|ARBA:ARBA00025162}.
CC   -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC       superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC       {ECO:0000256|ARBA:ARBA00007733}.
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:GAE91576.1}.
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DR   EMBL; BAVS01000001; GAE91576.1; -; Genomic_DNA.
DR   AlphaFoldDB; W4VEI3; -.
DR   STRING; 1298598.JCM21714_529; -.
DR   eggNOG; COG0532; Bacteria.
DR   Proteomes; UP000019102; Unassembled WGS sequence.
DR   GO; GO:0005525; F:GTP binding; IEA:InterPro.
DR   GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR   CDD; cd01887; IF2_eIF5B; 1.
DR   Gene3D; 1.10.10.2480; -; 1.
DR   Gene3D; 3.30.1330.30; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR006847; IF2_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR029064; Ribosomal_eL30-like_sf.
DR   InterPro; IPR004038; Ribosomal_eL8/eL30/eS12/Gad45.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR015760; TIF_IF2.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF04760; IF2_N; 2.
DR   Pfam; PF01248; Ribosomal_L7Ae; 1.
DR   SUPFAM; SSF55315; L30e-like; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW   ECO:0000313|EMBL:GAE91576.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019102}.
FT   DOMAIN          307..456
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          160..218
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        160..208
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   456 AA;  51029 MW;  BC568D7F1AF4BA8B CRC64;
     MENKKSYLNI LGLATRAGKC TFGEELIVKE IQSNRARIVL IASDIGDQTR KKLTDKCKFY
     KVPFFFVDER DILSQAVGKS GRVAVSIDEQ GFAMKLMALL DENNRGGERM SKIRVYEYAK
     QVNKSSKDII NKLKEIELPV SNHMSTISTE MKTKLDQIFQ PKSKEQSSKN QNSNNQQSKP
     KHNTNQQNNQ KQTKNNQQNN QQIKSEQPTQ EVEKQEQEQL KQADKIVYSG SLTVSELAQK
     LNKQTNEIIK KLISLGVMAT KNQALDHDAL ESICGEYGVE VEREVEVDKA DLANYIDEED
     PEKLKERPAV VTIMGGHVDH GKTTLLDAIR HTKVTEGEAG GITQHIGAYQ VRENDKRVTF
     LDTPGHAAFT SMRARGAQVT DIAILVVAAD DGVMPQTIEA INHAKAAEVP IIVAVNKIDV
     EGANPDRVMQ ELTEYQLVPE AWGGRDDFRA IVSLKR
//
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