IF2_GEOSE
ID IF2_GEOSE Reviewed; 741 AA.
AC P04766;
DT 13-AUG-1987, integrated into UniProtKB/Swiss-Prot.
DT 13-AUG-1987, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Translation initiation factor IF-2;
GN Name=infB;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3025563; DOI=10.1007/bf02428037;
RA Brombach M., Gualerzi C.O., Nakamura Y., Pon C.L.;
RT "Molecular cloning and sequence of the Bacillus stearothermophilus
RT translational initiation factor IF2 gene.";
RL Mol. Gen. Genet. 205:97-102(1986).
RN [2]
RP PROTEIN SEQUENCE OF 4-13; 19-25; 27-30; 147-165; 309-321 AND 520-532.
RX PubMed=2265694; DOI=10.1016/0014-5793(90)80495-5;
RA Severini M., Choli T., La Teana A., Gualerzi C.O.;
RT "Proteolysis of Bacillus stearothermophilus IF2 and specific protection by
RT GTP.";
RL FEBS Lett. 276:14-16(1990).
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.
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
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; X04399; CAA27987.1; -; Genomic_DNA.
DR PIR; A27892; A27892.
DR PDB; 1D1N; NMR; -; A=643-741.
DR PDB; 1Z9B; NMR; -; A=515-635.
DR PDB; 2LKC; NMR; -; A=241-414.
DR PDB; 2LKD; NMR; -; A=241-414.
DR PDB; 2NBG; NMR; -; A=394-514.
DR PDBsum; 1D1N; -.
DR PDBsum; 1Z9B; -.
DR PDBsum; 2LKC; -.
DR PDBsum; 2LKD; -.
DR PDBsum; 2NBG; -.
DR AlphaFoldDB; P04766; -.
DR BMRB; P04766; -.
DR SMR; P04766; -.
DR EvolutionaryTrace; P04766; -.
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; cd03702; IF2_mtIF2_II; 1.
DR Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR43381; PTHR43381; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 2.
DR SUPFAM; SSF50447; SSF50447; 2.
DR SUPFAM; SSF52156; SSF52156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00487; IF-2; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS01176; IF2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; GTP-binding;
KW Initiation factor; Nucleotide-binding; Protein biosynthesis.
FT CHAIN 1..741
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137170"
FT DOMAIN 242..411
FT /note="tr-type G"
FT REGION 48..158
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 251..258
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 276..280
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 297..300
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 351..354
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 387..389
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 48..127
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 251..258
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 297..301
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 351..354
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT CONFLICT 312
FT /note="R -> A (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 246..251
FT /evidence="ECO:0007829|PDB:2LKC"
FT TURN 253..256
FT /evidence="ECO:0007829|PDB:2LKC"
FT HELIX 257..265
FT /evidence="ECO:0007829|PDB:2LKC"
FT STRAND 271..274
FT /evidence="ECO:0007829|PDB:2LKD"
FT STRAND 276..278
FT /evidence="ECO:0007829|PDB:2LKC"
FT STRAND 285..288
FT /evidence="ECO:0007829|PDB:2LKC"
FT STRAND 291..296
FT /evidence="ECO:0007829|PDB:2LKC"
FT STRAND 300..305
FT /evidence="ECO:0007829|PDB:2LKC"
FT STRAND 308..310
FT /evidence="ECO:0007829|PDB:2LKD"
FT STRAND 317..323
FT /evidence="ECO:0007829|PDB:2LKC"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:2LKD"
FT HELIX 330..339
FT /evidence="ECO:0007829|PDB:2LKC"
FT HELIX 340..342
FT /evidence="ECO:0007829|PDB:2LKC"
FT STRAND 346..351
FT /evidence="ECO:0007829|PDB:2LKC"
FT TURN 352..354
FT /evidence="ECO:0007829|PDB:2LKC"
FT HELIX 360..367
FT /evidence="ECO:0007829|PDB:2LKC"
FT TURN 368..371
FT /evidence="ECO:0007829|PDB:2LKC"
FT TURN 375..378
FT /evidence="ECO:0007829|PDB:2LKC"
FT STRAND 379..385
FT /evidence="ECO:0007829|PDB:2LKC"
FT STRAND 388..391
FT /evidence="ECO:0007829|PDB:2LKC"
FT HELIX 392..407
FT /evidence="ECO:0007829|PDB:2LKC"
FT TURN 408..411
FT /evidence="ECO:0007829|PDB:2LKC"
FT STRAND 414..418
FT /evidence="ECO:0007829|PDB:2NBG"
FT STRAND 420..428
FT /evidence="ECO:0007829|PDB:2NBG"
FT TURN 429..431
FT /evidence="ECO:0007829|PDB:2NBG"
FT STRAND 432..438
FT /evidence="ECO:0007829|PDB:2NBG"
FT STRAND 449..452
FT /evidence="ECO:0007829|PDB:2NBG"
FT STRAND 455..458
FT /evidence="ECO:0007829|PDB:2NBG"
FT STRAND 462..464
FT /evidence="ECO:0007829|PDB:2NBG"
FT STRAND 469..473
FT /evidence="ECO:0007829|PDB:2NBG"
FT STRAND 478..482
FT /evidence="ECO:0007829|PDB:2NBG"
FT STRAND 493..495
FT /evidence="ECO:0007829|PDB:2NBG"
FT HELIX 500..506
FT /evidence="ECO:0007829|PDB:2NBG"
FT STRAND 508..511
FT /evidence="ECO:0007829|PDB:2NBG"
FT STRAND 541..550
FT /evidence="ECO:0007829|PDB:1Z9B"
FT HELIX 551..561
FT /evidence="ECO:0007829|PDB:1Z9B"
FT STRAND 570..579
FT /evidence="ECO:0007829|PDB:1Z9B"
FT HELIX 583..592
FT /evidence="ECO:0007829|PDB:1Z9B"
FT STRAND 595..600
FT /evidence="ECO:0007829|PDB:1Z9B"
FT HELIX 607..612
FT /evidence="ECO:0007829|PDB:1Z9B"
FT TURN 613..615
FT /evidence="ECO:0007829|PDB:1Z9B"
FT STRAND 647..653
FT /evidence="ECO:0007829|PDB:1D1N"
FT STRAND 660..662
FT /evidence="ECO:0007829|PDB:1D1N"
FT STRAND 666..670
FT /evidence="ECO:0007829|PDB:1D1N"
FT STRAND 672..674
FT /evidence="ECO:0007829|PDB:1D1N"
FT STRAND 677..684
FT /evidence="ECO:0007829|PDB:1D1N"
FT STRAND 686..694
FT /evidence="ECO:0007829|PDB:1D1N"
FT STRAND 696..699
FT /evidence="ECO:0007829|PDB:1D1N"
FT STRAND 701..703
FT /evidence="ECO:0007829|PDB:1D1N"
FT STRAND 713..717
FT /evidence="ECO:0007829|PDB:1D1N"
FT STRAND 728..733
FT /evidence="ECO:0007829|PDB:1D1N"
SQ SEQUENCE 741 AA; 82061 MW; 3C573EA77DC27735 CRC64;
MSKMRVYEYA KKQNVPSKDV IHKLKEMNIE VNNHMAMLEA DVVEKLDHQY RPKAEKKTET
KNEKKAEKKT DKPKRPMPAK TADFSDEEIF DDVKEAAKPA KKKGAAKGKE TKRTEAQQQE
KKAFQAAKKK GKGPAKGKKQ AAPAAKQVPQ PAKKEKELPK KITFEGSLTV AELAKKLGRE
PSEIIKKLFM LGVMATINQD LDKDAIELIC SDYGVEVEEK VTIDETNFEA IEIADAPEDL
VERPPVVTIM GHVDHGKTTL LDAIRHSKVT EQEAGGITQH IGAYQVTVND KKITFLDTPG
HEAFTTMRAR GRQVTDIVIL VVAADDGVMP QTVEAINHAK AANVPIIVAI NKMDKPEANP
DRVMQELMEY NLVPEEWGGD TIFCKLSAKT KEGLDHLLEM ILLVSEMEEL KANPNRRAVG
TVIEAKLDKG RGPVATLLVQ AGTLKVGDPI VVGTTYGRVR AMVNDSGRRV KEAGPSMPVE
ITGLHDVPQA GDRFMVFEDE KKARQIGEAR AQRQLQEQRS VKTRVSLDDL FEQIKQGEMK
ELNLIVKADV QGSVEALVAA LQKIDVEGVR VKIIHAAVGA ITESDISLAT ASNAIVIGFN
VRPDANAKRA AESEKVDIRL HRIIYNVIEE IEAAMKGMLD PEYEEKVIGQ AEVRQTFKVS
KVGTIAGCYV TDGKITRDSK VRLIRQGIVV YEGEIDSLKR YKDDVREVAQ GYECGLTIKN
FNDIKEGDVI EAYVMQEVAR A
