ID X8DPF3_9MYCO Unreviewed; 602 AA.
AC X8DPF3;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
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 ECO:0000313|EMBL:EUA70507.1};
GN ORFNames=I540_3626 {ECO:0000313|EMBL:EUA70507.1};
OS Mycobacteroides abscessus subsp. bolletii 1513.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacteroides; Mycobacteroides abscessus.
OX NCBI_TaxID=1299321 {ECO:0000313|EMBL:EUA70507.1, ECO:0000313|Proteomes:UP000023351};
RN [1] {ECO:0000313|EMBL:EUA70507.1, ECO:0000313|Proteomes:UP000023351}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1513 {ECO:0000313|EMBL:EUA70507.1,
RC ECO:0000313|Proteomes:UP000023351};
RA Zelazny A., Olivier K., Holland S., Lenaerts A., Ordway D., DeGroote M.A.,
RA Parker T., Sizemore C., Tallon L.J., Sadzewicz L.K., Sengamalay N.,
RA Fraser C.M., Hine E., Shefchek K.A., Das S.P., Tettelin H.;
RL Submitted (DEC-2013) 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:EUA70507.1}.
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DR EMBL; JAOJ01000002; EUA70507.1; -; Genomic_DNA.
DR AlphaFoldDB; X8DPF3; -.
DR PATRIC; fig|1299321.3.peg.3485; -.
DR Proteomes; UP000023351; 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; 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; 1.
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 98..269
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT BINDING 107..114
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 157..161
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 211..214
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 602 AA; 65226 MW; B26664C1610A9546 CRC64;
MRLPHGNGEV IRLARGASLS DFAEKIDANP ASLVQALFNL GEMVTATQSV GDETLELLGG
EMNYVVQVVS PEDEDRELLE SFDLTYGEDE GGEEDLRTRP PVVTVMGHVD HGKTRLLDTI
RKANVREGEA GGITQHIGAY QVAVEHDGTE RPITFIDTPG HEAFTAMRAR GAKATDIAIL
VVAADDGVMP QTVEAINHAQ AADVPIVVAV NKIDKEGADP AKIRAQLTEY NLVAEDFGGD
TMFVDISARQ GTNIEQLLEA VLLTADAALD LRANPDMEAQ GVAIEAHLDR GRGPVATVLI
QRGTLRVGDS IVAGDAYGRV RRMVDEHGED VEEALPSRPV QVIGFTSVPG AGDNLLVVDE
DRIARQIADR RSARKRNALA ARSRKRISLD DLDAALKETS QLNLILKGDN AGTVEALEEA
LLGIAIDDEV QLRVIDRGVG GVTETNVNLA SASDAIIIGF NVRAEGKATE LANREGVDIR
YYSVIYQAID EIESALKGML KPVYEEVELG RAEIRAMFRS SKVGNIAGCL VTSGIIRRNA
KARLLRDNIV VAETVTISSL RREKDDVVEV RDGYECGLTL TYNDIKEGDV IEAYELREKE
RV
//
