ID   IF2_PROM3               Reviewed;        1124 AA.
AC   A2C6Q5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   20-FEB-2007, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=P9303_04131;
OS   Prochlorococcus marinus (strain MIT 9303).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Prochlorococcus.
OX   NCBI_TaxID=59922;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MIT 9303;
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; CP000554; ABM77165.1; -; Genomic_DNA.
DR   AlphaFoldDB; A2C6Q5; -.
DR   SMR; A2C6Q5; -.
DR   STRING; 59922.P9303_04131; -.
DR   PRIDE; A2C6Q5; -.
DR   EnsemblBacteria; ABM77165; ABM77165; P9303_04131.
DR   KEGG; pmf:P9303_04131; -.
DR   HOGENOM; CLU_006301_5_1_3; -.
DR   OMA; QVRPEMI; -.
DR   BioCyc; PMAR59922:G1G80-384-MON; -.
DR   Proteomes; UP000002274; 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..1124
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000008298"
FT   DOMAIN          615..787
FT                   /note="tr-type G"
FT   REGION          32..451
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          480..523
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          624..631
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          649..653
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          674..677
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          728..731
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          764..766
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        94..119
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        187..204
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        221..235
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        424..451
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        496..510
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         624..631
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         674..678
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         728..731
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   1124 AA;  119452 MW;  48CE8078F7DB8A05 CRC64;
     MTSSGKIRIY ELSKDLGLEN KDVLHAAEKL SIAAKSHSSS ISDDEAKRIR GLLRQGSAAN
     SAPPSKSEPG KTILSVKKAA PTAIKDVAPP MRKATSSSEI SQVKPSAPAN PTPTSPERLS
     RESVAHPAPP TRPVNPTTTP TSSPPKTAAR PVNAPISRPA TPSRPSAPTP RSANKPSSPV
     PPSTGSKDPR AGQTSTSSKA TTVSGGGPRP KIISRPQSPA APGRSAPPAK PSIPSDRKAP
     KPELVGRPKP KRPVVAPPSR PEPEGQRPDK KRPGISPRPI GGPNQRANTP QRPGAPIRQG
     KTRPGQPRSA GNTLELVGKP IRRDRSDAGS AGRDSNNRPG APTRPGMPAG MRKPVAPGEL
     MQLQKPTGRP GTPPPRRPDG TSVGTRGGSE GATPPVERPA SPTAPKRPGH RPAQAPAAGA
     PRRPGRPDWD DSAKLEALRN KSPQKQRQKV HIIGENDDAL TAETSGYAGE QQAVVLTASL
     ARPAKPKSQK KPASKPVAAL RKRKKETTRQ RQRRRAMELR AAREAKQVRP EMLIVPEANL
     TVQELADMLS IESSEIIKSL FFKGITATVT QSLDLPTIEA VAEEFGVPVL QDDIEEAAKK
     TTEMIEETDL AHLIRRPPVV TVMGHVDHGK TSLLDAIRKA RVAAVEAGGI TQHIGAYQVE
     IDHGGQPRKI TFLDTPGHQA FTAMRARGTK VTDIAVLVVA ADDGVRPQTL EAISHARAAK
     VPIIVAINKT DKEGASPERV KQELSDQNLL SEEWGGDVVM VPVSAIKGEN IDKLLEMILL
     VTEVEDLQAN PDRLAKGTVI EAHLDKAKGP VATLLIQNGT LKTGDVLAAG PVLGKVRAMV
     DDSGARLKQA GPADAVEALG FSEVPTAGDE FEVYPDEKSA RAVVGERASD ARATRLAQQM
     ASRRVSLAAM SGQASDGELK ELNLILKADV QGSVEAILGS LEQLPKDEVQ VRVLLSAPGE
     ITETDVDLAA ASGAVIVGFN TSMASGAKRA ADATGVDVRD YDVIYKLLED IQMAMEGLLE
     PELVEESLGE AEVRAVFTIG KSAVAGCYIT TGKLQRNCRV RVRRAKQVVF EGDLDSLRRN
     KDDVKEVATG FECGIGCDRF ANWEERDIIE AHKLVTKRRT LSSS