ID   IF2_PROM4               Reviewed;        1113 AA.
AC   A9BCI5;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   15-JAN-2008, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=P9211_16161;
OS   Prochlorococcus marinus (strain MIT 9211).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=93059;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9211;
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; CP000878; ABX09547.1; -; Genomic_DNA.
DR   RefSeq; WP_012196168.1; NC_009976.1.
DR   AlphaFoldDB; A9BCI5; -.
DR   SMR; A9BCI5; -.
DR   STRING; 93059.P9211_16161; -.
DR   EnsemblBacteria; ABX09547; ABX09547; P9211_16161.
DR   KEGG; pmj:P9211_16161; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_3; -.
DR   OMA; QVRPEMI; -.
DR   Proteomes; UP000000788; 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..1113
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000093813"
FT   DOMAIN          605..777
FT                   /note="tr-type G"
FT   REGION          56..446
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          470..504
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          614..621
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          639..643
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          664..667
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          718..721
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          754..756
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        56..75
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        78..93
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        127..149
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        157..205
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        246..263
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        411..446
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        486..500
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         614..621
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         664..668
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         718..721
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   1113 AA;  120927 MW;  8250709D4B650519 CRC64;
     MTSSGKIRIY ELSRDLNLEN KDVLNAAKKL SIPAKSHSSS ISNAEANEIK AFLNKQSNQS
     INNKTKQNSS KEILSLKKAG SKPIKDEITK KKANLPPKAS AESQSSKPRI ETSKAPVAPI
     KPIKEPVQKA NTSNQSKGVI NNLIQPQKPS PLQPKQPKSI HLENNASKQN IEDNNNFQER
     SPRTQLVQKP PLPTKNNEPP QQKTSIPKRP ITPPARPSKP ILDNRSSVKS RPIIEAPRKK
     TGPDRNSPVQ PRTQNNQNRQ RIPNKPGKPP LRGNPPVELV GAPIRRSNKP NNNVKGPRDG
     GYRPGPPNRN DPSNQQGHVK RDIKAPIRQR PGMPPGMRKP VAPGELMQLQ KPTGRSQPPA
     PRRVGAPAPP SQRADSTKDR QGKSPGAKQP VNRPTPATAP KKPSHRPPGS GPTKRRSDWD
     DAAKLEALRN KAPQKQRQKV HIIGENDDAL TTETSGFAAE QEAMVLSASL ARPAKPKSTK
     KSNSKATVVT RKRKKESTRQ RQRRRAMELR AAREAKQVRP EMIIIPEGNL TVQELADKLS
     VESSEIIKSL FFKGITATVT QSLDLSTIET VAEEFGVPVL QDDIEEAATK TAEMLDEADK
     DHLIRRPPVV TVMGHVDHGK TSLLDAIRKA RVASGEAGGI TQHIGAYQVE LEHEKKKRKL
     TFLDTPGHEA FTAMRARGTK VTDVAVLVVA ADDGVRPQTL EAISHARAAK VPIVVAINKI
     DKEGASPDRV KQELSEQELV AEEWGGEVVM VPVSAIKGEN IDKLLEMVLL VTEVEDLQAN
     PDRLAKGTVI EAHLDKAKGP VATLLIQNGT LKSGDVLAAG PVLGKVRAMV DENGIRLKEA
     GPSCPVEALG FNEVPTAGDE FEVYPDEKSA RAVVGDRASD ARATRLAQQM ASRRVSLSSM
     SGQANEGDLK ELNIILKADV QGSIEAILGS LEQLPKDEVQ VRVLLSAPGE VTETDVDLAA
     ASGAVIVGFN TSMASGAKKA ADANSVDVRD YEVIYKLLED IQLAMEGLLE PDMVEESLGE
     AEVRAIFSIG KSAVAGCYIT NGKLQRNCKV RVKRGSQIVF EGDLDSLRRN KDVVKDVGSG
     FECGVGCDRF ANWKEGDIIQ GYKLVTKRRT LGP