IF2_PROM0
ID IF2_PROM0 Reviewed; 1114 AA.
AC A3PEY3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-APR-2007, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=P9301_16851;
OS Prochlorococcus marinus (strain MIT 9301).
OC Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC Prochlorococcus.
OX NCBI_TaxID=167546;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MIT 9301;
RX PubMed=18159947; DOI=10.1371/journal.pgen.0030231;
RA Kettler G.C., Martiny A.C., Huang K., Zucker J., Coleman M.L., Rodrigue S.,
RA Chen F., Lapidus A., Ferriera S., Johnson J., Steglich C., Church G.M.,
RA Richardson P., Chisholm S.W.;
RT "Patterns and implications of gene gain and loss in the evolution of
RT Prochlorococcus.";
RL PLoS Genet. 3:2515-2528(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; CP000576; ABO18308.1; -; Genomic_DNA.
DR RefSeq; WP_011863605.1; NC_009091.1.
DR AlphaFoldDB; A3PEY3; -.
DR SMR; A3PEY3; -.
DR STRING; 167546.P9301_16851; -.
DR PRIDE; A3PEY3; -.
DR EnsemblBacteria; ABO18308; ABO18308; P9301_16851.
DR KEGG; pmg:P9301_16851; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_3; -.
DR OMA; QVRPEMI; -.
DR Proteomes; UP000001430; 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; 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 PRINTS; PR00315; ELONGATNFCT.
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 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..1114
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008296"
FT DOMAIN 606..778
FT /note="tr-type G"
FT REGION 69..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 181..507
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 615..622
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 640..644
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 665..668
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 719..722
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 755..757
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 75..89
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..212
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..266
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..299
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..364
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 376..415
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..448
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 449..464
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..487
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 615..622
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 665..669
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 719..722
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1114 AA; 122173 MW; 95E459FBFB83AC40 CRC64;
MTISDKIRIY ELSRDLNLEN KDILDAAQKL SISVKSHSSS ISAEEAKKIK NLINKKNSDK
KILSINKPSI KKDNFKQNKS PSISSKKETP LKDNSNKKPL LIKPLNKPES VKIISNQLQN
SNKPNIVNTS QSRANLTNTN INSKTSQNLN QDKKTFENNI TPPIKSPAKP PIQLIAKPKN
INNNVKSNES SQNISSAGDN RRLSNKPDQN TNKPKTKNYD SKIKTPELVG APIRREDPKI
NPNKQNNKQN IAFKQTGSNR IGSPNRPGMP NNRPGLRNKP SDQGRPGSFN RQGNPNRPGM
PNNRPGLRNK PSDQGRHGSF NRQGNPNRPG MPNNRPGSKF NGQNSSGIRK PVSPNELLQL
QKNNNSEKDN KDKNNNAKQN INGPNQKAKA PNMRPNATPS SKKPPHRAFS NSSKKPGKTD
WDDSAKLEAL RSKNPQKQRQ KVHIIGENDD SLTSETSGYS GEKISILSAS LARPKKEKSE
ETKSQKSIKQ FKKKKKETTR QRQKRRAMEL KAAKEAKQVR PEMIIVPEDN LTVQELADKL
SLESSEIIKS LFFKGITATV TQSLDLATIE TVAEEFGVPV LQDDIQEAAE KTVDMIESDD
IDNLIRRPPV ITVMGHVDHG KTSLLDSIRE SRVASGEAGG ITQHIGAYQV EFEHESQKKK
LTFLDTPGHE AFTAMRARGT KVTDVAVLVV AADDGCRPQT LEAISHARAA KVPIVVAINK
IDKEGASPDR VKQELSEKDL IAEDWGGDTV MVPVSAIKKQ NIDKLLEMIL LVSEVEDLQA
NPDRFAKGTV IEAHLDKAKG PVATLLVQNG TLKSGDVLAA GSVLGKIRAM VDEHGNRIKE
AGPSFPVEAL GFSEVPTAGD EFEVYPDEKA GRAIVGERAT DARATKLAQQ MASRRVSLSS
LSTQANDGEL KELNLILKAD VQGSVEAILG SLEQLPKNEV QVRVLFSAPG EITETDIDLA
AASGSVIIGF NTSLASGAKR AADANDVDIR EYEVIYKLLE DIQLAMEGLL EPDLVEESLG
QAEVRATFSV GKGAIAGCYI QTGKLQRNCS LRVIRSEKVI FEGNLDSLKR AKDDVKEVNT
GFECGVGCDK FSSWIEGDVI EAFKFVTKKR TLSQ
