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Database: UniProt
Entry: A0A1X0JJX2_9MYCO
LinkDB: A0A1X0JJX2_9MYCO
Original site: A0A1X0JJX2_9MYCO 
ID   A0A1X0JJX2_9MYCO        Unreviewed;       914 AA.
AC   A0A1X0JJX2;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000256|HAMAP-Rule:MF_00100};
GN   ORFNames=BST47_20815 {ECO:0000313|EMBL:ORB63164.1};
OS   Mycolicibacterium tusciae.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycolicibacterium.
OX   NCBI_TaxID=75922 {ECO:0000313|EMBL:ORB63164.1, ECO:0000313|Proteomes:UP000192411};
RN   [1] {ECO:0000313|EMBL:ORB63164.1, ECO:0000313|Proteomes:UP000192411}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44153 {ECO:0000313|Proteomes:UP000192411};
RA   Tortoli E., Trovato A., Cirillo D.M.;
RT   "The new phylogeny of genus Mycobacterium.";
RL   Submitted (FEB-2017) to the EMBL/GenBank/DDBJ databases.
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|HAMAP-Rule:MF_00100,
CC       ECO:0000256|RuleBase:RU000644}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00100}.
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, ECO:0000256|HAMAP-Rule:MF_00100,
CC       ECO:0000256|RuleBase:RU000644}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_00100}.
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:ORB63164.1}.
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DR   EMBL; MVIM01000012; ORB63164.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X0JJX2; -.
DR   STRING; 75922.BST47_20815; -.
DR   eggNOG; COG0481; Bacteria.
DR   OrthoDB; 9811804at2; -.
DR   Proteomes; UP000192411; 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:UniProtKB-UniRule.
DR   GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR   CDD; cd01887; IF2_eIF5B; 1.
DR   CDD; cd03702; IF2_mtIF2_II; 1.
DR   CDD; cd03692; mtIF2_IVc; 1.
DR   Gene3D; 1.10.10.2480; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR   HAMAP; MF_00100_B; IF_2_B; 1.
DR   InterPro; IPR044145; IF2_II.
DR   InterPro; IPR006847; IF2_N.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR005225; Small_GTP-bd_dom.
DR   InterPro; IPR000795; T_Tr_GTP-bd_dom.
DR   InterPro; IPR000178; TF_IF2_bacterial-like.
DR   InterPro; IPR015760; TIF_IF2.
DR   InterPro; IPR023115; TIF_IF2_dom3.
DR   InterPro; IPR036925; TIF_IF2_dom3_sf.
DR   InterPro; IPR009000; Transl_B-barrel_sf.
DR   NCBIfam; TIGR00487; IF-2; 1.
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; PF11987; IF-2; 1.
DR   Pfam; PF04760; IF2_N; 2.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 2.
DR   PROSITE; PS51722; G_TR_2; 1.
PE   3: Inferred from homology;
KW   Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00100};
KW   GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW   Rule:MF_00100};
KW   Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW   Rule:MF_00100};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW   Rule:MF_00100};
KW   Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW   Rule:MF_00100}.
FT   DOMAIN          410..581
FT                   /note="Tr-type G"
FT                   /evidence="ECO:0000259|PROSITE:PS51722"
FT   REGION          26..300
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        86..145
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        165..199
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         419..426
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT   BINDING         469..473
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT   BINDING         523..526
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   914 AA;  94211 MW;  3016032F971CD9AE CRC64;
     MAGKARVHEL AKELGVTSKE VLARLSDQGE FVKSASSTVE APVARRLRES FGGGKPAAEK
     APASGNGSSA GAPAKPAATT AKPGAPKPAA PAPPPAPAAP AEPAAPPAAA ATPQPAAPPA
     APPAQPGPTP GATPGPRPGP APKPAARAPR VGNNPFSSQT PVERPAPRPQ APRPGAPRPG
     APRPGMSPGN MPPRPAGPRP GVGAGGGRPG GPRPGPGGRG PGGGAGGGRP GGPGGGGGGG
     NYRGGGAGGG GGAPAGGGGG FRGRPGGGGR PGQRGGAAGA FGRPGGAPKR GRKSKRAKRA
     EYENMQAPVV GGVRLPHGNG ETIRLARGAS LVDFAEKIDA NPAALVQALF NLGEMVTATQ
     SVGDETLELL GGEMNYVVQV VSPEDEDREL LESFDLTYGE DEGGEDDLEQ RPPVVTVMGH
     VDHGKTRLLD TIRNASVREG EAGGITQHIG AYQVAVEHDG SERPITFIDT PGHEAFTAMR
     ARGAKATDIA ILVVAADDGV MPQTVEAINH AQAADVPIVV AVNKIDKEGA DPSKIRAQLT
     EYNLVAEDFG GDTMFVDISA KQGTNIQALL EAVLLTADAA LDLRANPDME AQGVAIEAHL
     DRGRGPVATV LIQRGTLRVG DSIVAGDAYG RVRRMVDEHG ADVEEALPSR PVQVVGFTSV
     PGAGDNLLVV DEDRIARQIA DRRSARKRNA LAARTRKRIS LDDLDAALKE TSQLNLILKG
     DNSGTVEALE EALLGIEIDD EVELRVIDRG VGGVTETNVN LASASDAIII GFNVRAEGKA
     TELANREGVD IRYYSVIYQA IDEIQSALKG MLKPVYEEKE LGRAEIRAIF RSSKVGNIAG
     CLVTSGLIRR NAKARLLRDN VVVAETVTIS SLRREKDDVT EVRDGYECGL TLTYSDIKEG
     DVIEAYELVE KERT
//
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