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
//