ID F3NFF4_9ACTN Unreviewed; 1020 AA.
AC F3NFF4;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=SGM_1853 {ECO:0000313|EMBL:EGG47767.1};
OS Streptomyces griseoaurantiacus M045.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX NCBI_TaxID=996637 {ECO:0000313|EMBL:EGG47767.1, ECO:0000313|Proteomes:UP000003022};
RN [1] {ECO:0000313|EMBL:EGG47767.1, ECO:0000313|Proteomes:UP000003022}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M045 {ECO:0000313|EMBL:EGG47767.1,
RC ECO:0000313|Proteomes:UP000003022};
RX PubMed=21551298; DOI=10.1128/JB.05053-11;
RA Li F., Jiang P., Zheng H., Wang S., Zhao G., Qin S., Liu Z.;
RT "Draft genome sequence of the marine bacterium Streptomyces
RT griseoaurantiacus M045, which produces novel manumycin-type antibiotics
RT with a pABA core component.";
RL J. Bacteriol. 193:3417-3418(2011).
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:EGG47767.1}.
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DR EMBL; AEYX01000029; EGG47767.1; -; Genomic_DNA.
DR AlphaFoldDB; F3NFF4; -.
DR STRING; 996637.SGM_1853; -.
DR eggNOG; COG0532; Bacteria.
DR Proteomes; UP000003022; 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.
DR PROSITE; PS01176; IF2; 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}; Reference proteome {ECO:0000313|Proteomes:UP000003022}.
FT DOMAIN 513..685
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 49..420
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 90..106
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 115..171
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..245
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..295
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 522..529
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 572..576
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 626..629
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1020 AA; 104572 MW; A68EA527105FD235 CRC64;
MAKVRVYELA KEFGVESKVV MAKLQELGEF VRSASSTIEA PVVRKLTDAF QQGGGNGKSG
ARPAPRKAAP RPAAPSPAQA GSTSPGPRPT GERPAAPKPG APRPAAAERP AAPAASAPTP
GPRPAPAPKP APAPAPRPAP AAPAAPEFQA PPSAPTGPRP GARPAPKPGS RPAAPGQGQG
QGQGRPAGQG QRPGGAAPRP GGRAAGPRPG NNPFTSGGST GMGRPAPRPQ GGPRPGGPGA
PGAGPRPQAP GGQGGPRPQS PGGSRPTPGG MPRPQGGAPR PGGPRPNPGM MPQRPAAGPR
PGGGGGGRGP GGGGRPGGGG GRPGGGGFAG RPGGGGGGGF AGRPGGPGGG GGGFAGRPGG
GGGRPGFGGR PGGPGGRGGT QGAFGRPGGP ARRGRKSKRQ RRQEYEAMQA PSVGGVMLPR
GNGQTVRLSR GASLTDFAEK INANPASLVA VMMNLGEMVT ATQSVSDETL QLLADEMNYV
VEIVSPEEED RELLESFDIE FGEDEGGEEA LVARPPVVTV MGHVDHGKTR LLDTIRKTNV
VAGEAGGITQ HIGAYQVTTQ VNEEERRITF IDTPGHEAFT AMRARGAKST DIAILVVAAN
DGVMPQTVEA LNHAKAADVP IVVAVNKIDV EGADPTKVRG QLTEYGLVAE EYGGDTMFVD
ISAKQGLNIE SLLEAVVLTA DASLDLRANP EQDAQGIAIE SHLDRGRGAV ATVLVQRGTL
RVGDTMVVGD AYGRVRAMLD DKGENVEEAG PSTPVLVLGL TNVPGAGDNF LVVDEDRTAR
QIAEKRAARE RNANFARRGV RFSLENLDEA LKAGLVQELN LIIKGDASGS VEALESSLLQ
LDVGEEVDIR VLHRGVGAVT ESDIDLATGS DAIVIGFNVR AAGRAAQMAE REGVDVRYYS
VIYQAIEEVE AALKGMLKPE YEEVELGTAE IREVFKSSKL GNIAGVLVRS GEVKRNTKAR
LLRDGKVIAE NLNISGLRRF KDDVTEIREG FEGGINLGNY NDIKVDDVIA TYEMREKPRA
//
