ID   IF2_PARMW               Reviewed;         650 AA.
AC   Q7U8L9;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 115.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=SYNW0597;
OS   Parasynechococcus marenigrum (strain WH8102).
OC   Bacteria; Cyanobacteria; Synechococcales; Prochlorococcaceae;
OC   Parasynechococcus; Parasynechococcus marenigrum.
OX   NCBI_TaxID=84588;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WH8102;
RX   PubMed=12917641; DOI=10.1038/nature01943;
RA   Palenik B., Brahamsha B., Larimer F.W., Land M.L., Hauser L., Chain P.,
RA   Lamerdin J.E., Regala W., Allen E.E., McCarren J., Paulsen I.T.,
RA   Dufresne A., Partensky F., Webb E.A., Waterbury J.;
RT   "The genome of a motile marine Synechococcus.";
RL   Nature 424:1037-1042(2003).
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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; BX569690; CAE07112.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q7U8L9; -.
DR   SMR; Q7U8L9; -.
DR   STRING; 84588.SYNW0597; -.
DR   EnsemblBacteria; CAE07112; CAE07112; SYNW0597.
DR   KEGG; syw:SYNW0597; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_5_1_3; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000001422; 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; 1.
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..650
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000137271"
FT   DOMAIN          142..314
FT                   /note="tr-type G"
FT   REGION          1..40
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          151..158
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          176..180
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          201..204
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          255..258
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          291..293
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        23..37
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         151..158
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         201..205
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         255..258
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   650 AA;  70466 MW;  315F46C3010E0DEA CRC64;
     MVLSASLARP AKPKSQRKAA PKPMAAMRKR KKETTRQRQR RRAMELRAAR EAKQVRPEML
     IVPEDNLTVQ ELADMLSVES SEIIKSLFFK GIIATVTQTL DMNTIETVAE EFGVPVLQDD
     VEEAAKKTVE MIEEADKEHL IRRPPVVTVM GHVDHGKTSL LDAIRKARVA AGEAGGITQH
     IGAYQVEIDH NDEARKLTFL DTPGHEAFTA MRARGTKVTD VAVLVVAADD GVRPQTLEAI
     SHARAAEVPI VVAINKIDKE GASPDRVKQE LSEQNLLAED WGGDVVMVPV SAIKGENIDK
     LLEMLLLVTE VEDLQANPDR LARGTVIEAH LDKAKGPVAT LLVQNGTLKT GDVVAAGPVL
     GKVRAMVDDN RQRLKEAGPS FAVEALGFSE VPTAGDEFEV YPDEKSARAV VGDRASDARA
     TRLAQQMASR RVSLTAMSGQ ANEGELKELN LILKADVQGS VEAILGSLEQ LPKDEVQVRV
     LLSAPGEVTE TDVDLAAASG AVIVGFNTSM ASGAKKAADA TGVDVRDYDV IYKLLEDIQL
     AMEGLLEPEL VEEALGEAEV RAVFTIGKSA VAGCYVTTGK LQRNCKVRVH RGSQVVYDGD
     LDSLRRNKDD VKEVATGFEC GVGTDRFANW EDGDRIEAFK MVTQRRKLTT