IF2_NEIG1
ID IF2_NEIG1 Reviewed; 943 AA.
AC Q5F797;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=NGO1286;
OS Neisseria gonorrhoeae (strain ATCC 700825 / FA 1090).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=242231;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700825 / FA 1090;
RA Lewis L.A., Gillaspy A.F., McLaughlin R.E., Gipson M., Ducey T.F.,
RA Ownbey T., Hartman K., Nydick C., Carson M.B., Vaughn J., Thomson C.,
RA Song L., Lin S., Yuan X., Najar F., Zhan M., Ren Q., Zhu H., Qi S.,
RA Kenton S.M., Lai H., White J.D., Clifton S., Roe B.A., Dyer D.W.;
RT "The complete genome sequence of Neisseria gonorrhoeae.";
RL Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases.
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; AE004969; AAW89940.1; -; Genomic_DNA.
DR RefSeq; WP_010951232.1; NC_002946.2.
DR RefSeq; YP_208352.1; NC_002946.2.
DR AlphaFoldDB; Q5F797; -.
DR SMR; Q5F797; -.
DR STRING; 242231.NGO_1286; -.
DR PRIDE; Q5F797; -.
DR EnsemblBacteria; AAW89940; AAW89940; NGO_1286.
DR KEGG; ngo:NGO_1286; -.
DR PATRIC; fig|242231.10.peg.1512; -.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000000535; 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; 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..943
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228216"
FT DOMAIN 443..612
FT /note="tr-type G"
FT REGION 99..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 452..459
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 477..481
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 498..501
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 552..555
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 588..590
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 117..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..198
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 452..459
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 498..502
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 552..555
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 943 AA; 101018 MW; 5658682DFF512CC2 CRC64;
MSNTTVEQFA AELKRPVEDL LKQLKEAGVS KNSGSDSLTL DDKQLLNAYL TKKNGSNGGT
ISIRRTKTEV STVDGVKVET RKRGRTVNIP SAEELAAQVK AAQTQAAPVQ PEQTAEDAVK
ARAEAAARAE ARAKAEAEAA KLKAAKAGNK AKPAAQKPTE AKAETAPVAA ETKPAEPKEK
AVKPKHERNG KGKDAKKPAK PAAPAVPQPV VSAEEQAQRD EEARRAAALR AHQEALLKEK
QERQARREAM KQQAEQQAKA AQEAKTGRQR PAKPAEKPQA AAPAVENKPV NPAKAKKEDR
RNRDDEGQGR NAKGKGAKGG RDRNNARNGG DERVRGGKKG KKLKLEPNQH AFQAPTEPVV
HEVLVPETIT VADLAHKMAV KGVEMVKALM KKGMMVTINQ SIDQDTALIV VKKLGHIGKP
AAADDPEAFL GEGAEAEEAE ALPRPPVVTV MGHVDHGKTS LLDYIRRAKV VQGEAGGITQ
HIGAYHVKTP RGVITFLDTP GHEAFTAMRA RGAKATDIVI LVVAADDGVM PQTIEAIAHA
KAAGVPIVVA VNKIDKDTAN PERIRQELTQ HEVIPDDWGG TVQFIDVSAK KGTNIDALLE
AVLLEAEVLE LTAPVDAPAK GIIVEARLDK GRGAVATLLV QNGTLKKGDM LLAGTAFGKI
RAMVDENGKS ITEAGPSIPV EILGLSDVPN AGEDAMVLAD EKKAREIALF RQGKYRDVRL
AKQQAAKLEN MFNNMGETQA QSLSVIIKAD VQGSYEALAG SLKKLSADEV KVNVLHSGVG
GITESDVNLA IASGAFIIGF NVRADASSRK LAENENVEIR YYNIIYDAID DVKAAMSGML
SPEKKEQVTG TVEIRQVISV SKVGNIAGCM VTDGVVKRDS HIRLIRNNVV IHTGELASLK
RYKDDVKEVR MGFECGLMLK GYNEIMEGDQ LECFDIVEVA RTL
