ID   IF2_PROM2               Reviewed;        1119 AA.
AC   A8G6Z5;
DT   05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   13-NOV-2007, sequence version 1.
DT   03-AUG-2022, entry version 89.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=P9215_17631;
OS   Prochlorococcus marinus (strain MIT 9215).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=93060;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9215;
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; CP000825; ABV51376.1; -; Genomic_DNA.
DR   RefSeq; WP_012008392.1; NC_009840.1.
DR   AlphaFoldDB; A8G6Z5; -.
DR   SMR; A8G6Z5; -.
DR   STRING; 93060.P9215_17631; -.
DR   PRIDE; A8G6Z5; -.
DR   EnsemblBacteria; ABV51376; ABV51376; P9215_17631.
DR   KEGG; pmh:P9215_17631; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_7_0_3; -.
DR   OMA; QVRPEMI; -.
DR   OrthoDB; 347113at2; -.
DR   Proteomes; UP000002014; 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.
FT   CHAIN           1..1119
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000057660"
FT   DOMAIN          610..782
FT                   /note="tr-type G"
FT   REGION          64..463
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          477..507
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          619..626
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          644..648
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          669..672
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          723..726
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          759..761
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        64..108
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        113..166
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        178..226
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        275..295
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        313..331
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        361..419
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        420..452
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        477..491
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         619..626
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         669..673
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         723..726
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   1119 AA;  122886 MW;  986210AB529AE03E CRC64;
     MTISDKIRIY ELSRDLNLDN KDILGAAQKL SISVKSHSSS ISAEEAEKIK NLINKKNPDK
     KILSIKKPSI KKDNYKQNKE DKSSLISSVE EKPFKDNPEK KPLLKKPLNK PESLKIISNQ
     PKSLNKPTIT NSSQSQANLT NQNLNSKTSQ NLNQDKRNFR NNLTPPIKSP TKPPIQLIAK
     PKNTTKNVQS NESSQNILNS GGGRQISNKP DQNSSKSKTK NINNRMSPPE LVGAPIRREG
     PNKQNNKQKT SFKQTVPNRP GMLNRPGLRN KPSDQGRPGS FNRQTNTNRP GAPSSNKPGM
     PNRPGLRNKP SDQGRPGSFN RQVNTNRSGA PIRPGMPNRP GSKFNGPKSP GMRKPVSPNE
     LLKLQKTNKS ENDKQVINNN EKQNSETTKQ KVKAPNSRPH TAPNSKKLPH RTFSNNSKKP
     GKTDWDDSAK LEALRNKNPQ KQRQKVRIIG ENDDSLTSET SGYSGEKFSI LSASLARPKK
     EKSDESKSQK TIKQFKKKKK ETTRQRQKRR AMELKAAKEA KQIRPEMIIV PEDNLTVQEL
     ADKLSLESSE IIKSLFFKGI TATVTQSLDL ATIETVAEEF GVPVLQDDIQ EAAEKTVDMI
     ESEDLDNLIK RPPVITVMGH VDHGKTSLLD SIRESRVASG EAGGITQHIG AYQVEFEHES
     KKKKLTFLDT PGHEAFTAMR ARGTKVTDVA VLVVAADDGC RPQTLEAISH ARAAKVPIVV
     AINKIDKEGA SPDRVKQELS EKNLIAEDWG GDTVMVPVSA IKKQNINKLL EMILLVSEVE
     DLQANPDRFA KGTVIEAHLD KAKGPVATLL VQNGTLKSGD VLAAGSVLGK IRAMVDEHGN
     RIKDAGPSFP VEALGFSEVP TAGDEFEVYP DEKTARAIVG ERATDARATK LAQQMASRRV
     SLSSLSTQAN DGELKELNLI LKADVQGSVE AILGSLEQLP KNEVQVRVLL SAPGEITETD
     IDLAAASGSV IIGFNTSLAS GAKKAADAND VDVREYEVIY KLLEDIQLAM EGLLEPDLVE
     ESLGKAEVRA TFSVGKGAIA GCYIQTGKLQ RNCSLRVIRS EKVIFEGNLD SLKRSKDDVK
     EVNTGFECGV GCDKFSSWIE GDIIEAFKFV TKKRTLTQE