ID IF2_STIAU Reviewed; 1054 AA.
AC P55875;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 27-MAR-2024, entry version 107.
DE RecName: Full=Translation initiation factor IF-2;
GN Name=infB;
OS Stigmatella aurantiaca.
OC Bacteria; Myxococcota; Myxococcia; Myxococcales; Cystobacterineae;
OC Archangiaceae; Stigmatella.
OX NCBI_TaxID=41;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=DW4;
RX PubMed=9079922; DOI=10.1128/jb.179.7.2348-2355.1997;
RA Bremaud L., Laalami S., Derijard B., Cenatiempo Y.;
RT "Translation initiation factor IF2 of the myxobacterium Stigmatella
RT aurantiaca: presence of a single species with an unusual N-terminal
RT sequence.";
RL J. Bacteriol. 179:2348-2355(1997).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000305}.
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DR EMBL; X87940; CAA61162.1; -; Genomic_DNA.
DR PIR; T43226; T43226.
DR AlphaFoldDB; P55875; -.
DR SMR; P55875; -.
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; IPR004161; EFTu-like_2.
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; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 2.
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.
FT CHAIN 1..1054
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137256"
FT DOMAIN 552..721
FT /note="tr-type G"
FT REGION 57..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 225..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 287..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 401..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 561..568
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 586..590
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 607..610
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 661..664
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 697..699
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 88..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 401..424
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 561..568
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 607..611
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 661..664
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1054 AA; 111324 MW; FFD519530B5D0669 CRC64;
MSKKRVHEIA KELKGHGIEL DNKEVVTELA GLGYDVKSHS SSLDDDQATA AVQKILDKRK
PKQAAAPVTA KGFVVRRKVG PPTGSGVYDA SQEPSQAASD VSSPPSEPVH EASGAEAAAS
ERVPEAAAVQ EPVAEAPRAA ASEPAAEAPK ATAPVAPEPT VEAPKAAAPV APEPTVEAPK
TEAPVAAAPI AEAPTPPART EVPVTSGRRA ASCRGAAPLP CSGKDPLALN SSPQSSAAFC
PDARNPGDCD FPSTSGRWHA WPSRGSSGRF AHGAGRPSGW TFARWTSGRP RAASRRTAVQ
RPSGRAGAGA SHGLQRRKGF GAGAQASGQP QNVTMVGGIP HAPTAPDARA LRPTATQAVV
ISRPLIQVRR VTPTTSSAKQ YPMAPGKKAI GEVREFKVVP DHAGRGRELV DVSKNKDKSP
RKRGGPNDTS ISKQELTDLA WGRVNIPLRG KKKKPTKKGA KTQITQMAED KKVIKLQEGI
SVSDLGQRMG VRTSDIIKKL MGLGKMATAN QMVDADTVEL IASDYGWKVD RVGFEVEDYL
PEVVARPEDA RTRPPVVTVM GHVDHGKTSL LDAIRAANVA SGEAGGITQH IGAYSVTTAR
GDITFLDTPG HEAFTSMRAR GANVTDIVIL VVAADDGVMP QTIEAIKHAK AAEVPIVVAL
NKMDVPGANP DRVKKDLANH ELVPEEWGGE TIMVPVSAKQ KMGIDLLLEN VVLQAEVLEL
TSNPSRPAVG AIIEGELDRG RGPVATVLVQ EGTLRVGDAV VTGTDYGRVR AMNNSRGESV
KEVLPGYCAE VIGLSGVPSA GDTINVVADE KAAKQIAEHR GMKERQSELS KVSRETLDQL
FAKTKAGGGP KELRVVIKAD VQGSAEAVKQ AVQKLTTHKV KVEVIDTGVG AITESDVMRA
AASKGVVLGF NVKPESGAES AAKAEGVMLR SFSIIYELID GVRSSMEELL EPIRTERKLG
RAEVRNTFNV PKLGTIAGAA VLDGVIKRGA FVRLMRENKQ LFAGKMASLR RFKDDVKEVA
QGFECGIGIE NFNDLKAGDI IEAYEIEETR QSLT
//
