ID IF2_SACEN Reviewed; 1027 AA.
AC A4FM34;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 101.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=SACE_5926;
OS Saccharopolyspora erythraea (strain ATCC 11635 / DSM 40517 / JCM 4748 /
OS NBRC 13426 / NCIMB 8594 / NRRL 2338).
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Saccharopolyspora.
OX NCBI_TaxID=405948;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 11635 / DSM 40517 / JCM 4748 / NBRC 13426 / NCIMB 8594 / NRRL
RC 2338;
RX PubMed=17369815; DOI=10.1038/nbt1297;
RA Oliynyk M., Samborskyy M., Lester J.B., Mironenko T., Scott N., Dickens S.,
RA Haydock S.F., Leadlay P.F.;
RT "Complete genome sequence of the erythromycin-producing bacterium
RT Saccharopolyspora erythraea NRRL23338.";
RL Nat. Biotechnol. 25:447-453(2007).
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:0000255|HAMAP-Rule:MF_00100}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00100}.
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DR EMBL; AM420293; CAM05109.1; -; Genomic_DNA.
DR RefSeq; WP_011874889.1; NZ_PDBV01000001.1.
DR AlphaFoldDB; A4FM34; -.
DR SMR; A4FM34; -.
DR STRING; 405948.SACE_5926; -.
DR KEGG; sen:SACE_5926; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_4_11; -.
DR Proteomes; UP000006728; Chromosome.
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; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..1027
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335508"
FT DOMAIN 523..695
FT /note="tr-type G"
FT REGION 31..433
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..539
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 557..561
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 582..585
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 636..639
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 672..674
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 90..129
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 172..188
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 532..539
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 582..586
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 636..639
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1027 AA; 106677 MW; 546A2848701A9B87 CRC64;
MAGKARVHEL AKELGVTSKE VLNKLAEQGE YVKSASSTVE APVARRLRDA FPKSGGKKGG
GDSNGRAGGA KPAPPRPPES SGRTEAQAPK PGPKPGPRTE TPSGERPKPG PKPGPKPGPK
APAPETKPFE EAPAPAAKAD APAQPRSEQP RSEQPRSEQP RSEQPRSERS GPKPGGPKPG
PKPGPKPGPR GGGDADAGVV PPKPQSPKPG PRSPRVGNNP FGVGSGAPAQ RPPRPGPGGG
QRQGGQGPGR GGPQGGRPDR QGGGGQGAGT APAGGDRAPR GEGGGGGNRP NPGMMPPRPN
PGMMPSRPAR SGGGPGGGRG GGRGGPGGGG GGRPGGGGGG GRPGGGGGGF RGGGGPGAGA
GTGAPAGGGF RGRPGGGGRP GGPGGRGGAA GAFGRPGGPA RRGRKSKRQK RQEYMDNMQA
PSVGGVRLPR GNGESVRLRR GASLTDFAEK INANPASLVQ AMFHLGEMVT ATQSVSDEIL
ELLGSEMNYK VEMVSPEDED RELLESFDIS FGDPGSSDEE LMSRPPVVTV MGHVDHGKTR
LLDTIRKANV QAGEAGGITQ HIGAYQVITE LEGNERPITF IDTPGHEAFT AMRARGAKST
DIAVLVVAAD DGVMPQTVEA LNHAQAAGVP IVVAVNKIDV EGANPAKVRQ QLTEYNLVAE
EYGGETMFVD ISARQGTNIE SLLEAILLTA DATLDLRANP SMEAQGVAIE AHLDRGRGPV
ATVLVQRGTL RVGDSVVAGN AFGRVRRMIN EHDEDVTEAL PSRPVQVIGF TSVPGAGDTF
LVVDEDRVAR QIADRRGARI REAQNAAKRK RVSLEDLDKV LKETNQLNLI IKGDNSGTVE
ALEESLTKIE VGEEVELRVI HRGVGGINES DINLATAENT IVLGFNVRAE GKAAEVANRE
GVEIRYYSVI YRAIEDIEQA LKGMLKPEYE EVELGRAEVR EVFKSSKVGT IAGCMVTDGI
MRRNAKARLL RDNVVISENL TVTSLKRFKD DATEVRDGFE CGLTLSYSDI KVDDIIETYE
MREKPRA
//
