ID   IF2_NEIMB               Reviewed;         962 AA.
AC   Q9JYD2;
DT   16-JUN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2000, sequence version 1.
DT   03-AUG-2022, entry version 123.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=NMB1643;
OS   Neisseria meningitidis serogroup B (strain MC58).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC   Neisseria.
OX   NCBI_TaxID=122586;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MC58;
RX   PubMed=10710307; DOI=10.1126/science.287.5459.1809;
RA   Tettelin H., Saunders N.J., Heidelberg J.F., Jeffries A.C., Nelson K.E.,
RA   Eisen J.A., Ketchum K.A., Hood D.W., Peden J.F., Dodson R.J., Nelson W.C.,
RA   Gwinn M.L., DeBoy R.T., Peterson J.D., Hickey E.K., Haft D.H.,
RA   Salzberg S.L., White O., Fleischmann R.D., Dougherty B.A., Mason T.M.,
RA   Ciecko A., Parksey D.S., Blair E., Cittone H., Clark E.B., Cotton M.D.,
RA   Utterback T.R., Khouri H.M., Qin H., Vamathevan J.J., Gill J., Scarlato V.,
RA   Masignani V., Pizza M., Grandi G., Sun L., Smith H.O., Fraser C.M.,
RA   Moxon E.R., Rappuoli R., Venter J.C.;
RT   "Complete genome sequence of Neisseria meningitidis serogroup B strain
RT   MC58.";
RL   Science 287:1809-1815(2000).
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; AE002098; AAF41992.1; -; Genomic_DNA.
DR   PIR; C81060; C81060.
DR   RefSeq; NP_274648.1; NC_003112.2.
DR   RefSeq; WP_002225000.1; NC_003112.2.
DR   AlphaFoldDB; Q9JYD2; -.
DR   SMR; Q9JYD2; -.
DR   STRING; 122586.NMB1643; -.
DR   PaxDb; Q9JYD2; -.
DR   EnsemblBacteria; AAF41992; AAF41992; NMB1643.
DR   KEGG; nme:NMB1643; -.
DR   PATRIC; fig|122586.8.peg.2115; -.
DR   HOGENOM; CLU_006301_6_0_4; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000000425; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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; IPR009061; DNA-bd_dom_put_sf.
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   SUPFAM; SSF46955; SSF46955; 1.
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..962
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000137227"
FT   DOMAIN          462..631
FT                   /note="tr-type G"
FT   REGION          99..366
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          471..478
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          496..500
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          517..520
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          571..574
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          607..609
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        115..145
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        174..217
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..272
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        310..365
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         471..478
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         517..521
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         571..574
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   962 AA;  103143 MW;  D7DDBC7A45F89AAC CRC64;
     MSNTTVEQFA AELKRPVEDL LKQLKEAGVS KNSGSDSLTL DDKQLLNAYL TKKNGSNSST
     ISIRRTKTEV STVDGVKVET RKRGRTVKIP SAEELAAQVK AAQTQAAPVR PEQTAEDAAK
     ARAEAAARAE ARAKAEAEAA KLKAAKAGNK AKPAAQKPTE AKAETAPVAA ETKPAEESKA
     EKAQADKMPS EKPAEPKEKA AKPKHERNGK GKDAKKPAKP AAPAVPQPVV SAEEQAQRDE
     EARRAAALRA HQEALLKEKQ ERQARREAMK QQAEQQAKAA QEAKTGRQRP AKPAEKPQAA
     APAVENKPVN PAKAKKEDRR NRDDEGQGRN AKGKGGKGGR DRNNARNGDD ERVRGGKKGK
     KLKLEPNQHA FQAPTEPVVH EVLVPETITV ADLAHKMAVK GVEVVKALMK MGMMVTINQS
     IDQDTALIVV EELGHIGKPA AADDPEAFLD EGAEAVEAEA LPRPPVVTVM GHVDHGKTSL
     LDYIRRTKVV QGEAGGITQH IGAYHVETPR GVITFLDTPG HEAFTAMRAR GAKATDIVIL
     VVAADDGVMP QTIEAIAHAK AAGVPMVVAV NKIDKEAANP ERIRQELTAH EVVPDEWGGD
     VQFIDVSAKK GLNIDALLEA VLLEAEVLEL TAPVDAPAKG IIVEARLDKG RGAVATLLVQ
     SGTLKKGDML LAGTAFGKIR AMVDENGKSI TEAGPSIPVE ILGLSDVPNA GEDAMVLADE
     KKAREIALFR QGKYRDVRLA KQQAAKLENM FNNMGETQAQ SLSVIIKADV QGSYEALAGS
     LKKLSTDEVK VNVLHSGVGG ITESDVNLAI ASGAFIIGFN VRADASSRKL AENENVEIRY
     YNIIYDAIND VKAAMSGMLS PEEKEQVTGT VEIRQVISVS KVGNIAGCMV TDGVVKRDSH
     VRLIRNNVVI HTGELASLKR YKDDVKEVRM GFECGLMLKG YNEIMEGDQL ECFDIVEVAR
     SL