IF2_NEIMF
ID IF2_NEIMF Reviewed; 962 AA.
AC A1KV51;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=NMC1557;
OS Neisseria meningitidis serogroup C / serotype 2a (strain ATCC 700532 / DSM
OS 15464 / FAM18).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=272831;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700532 / DSM 15464 / FAM18;
RX PubMed=17305430; DOI=10.1371/journal.pgen.0030023;
RA Bentley S.D., Vernikos G.S., Snyder L.A.S., Churcher C., Arrowsmith C.,
RA Chillingworth T., Cronin A., Davis P.H., Holroyd N.E., Jagels K.,
RA Maddison M., Moule S., Rabbinowitsch E., Sharp S., Unwin L., Whitehead S.,
RA Quail M.A., Achtman M., Barrell B.G., Saunders N.J., Parkhill J.;
RT "Meningococcal genetic variation mechanisms viewed through comparative
RT analysis of serogroup C strain FAM18.";
RL PLoS Genet. 3:230-240(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; AM421808; CAM10752.1; -; Genomic_DNA.
DR RefSeq; WP_002220489.1; NC_008767.1.
DR AlphaFoldDB; A1KV51; -.
DR SMR; A1KV51; -.
DR PRIDE; A1KV51; -.
DR EnsemblBacteria; CAM10752; CAM10752; NMC1557.
DR KEGG; nmc:NMC1557; -.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 55182at2; -.
DR Proteomes; UP000002286; 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.
FT CHAIN 1..962
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008287"
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; 103055 MW; 1C9B752FD9F0D107 CRC64;
MSNTTVEQFA AELKRPVEDL LKQLKEAGVS KTGGGDSLTL DDKQLLNAYL TKKNGSNSST
ISIRRTKTEV STVDGVKVET RKRGRTVNIP SAEELAAQVK AAQTQAAPVR PEQTAEDAAK
ARAEAAARAE ARAKAEAEAA KLKAAKAGNK AKPAAQKPTE AKAETAPVAA ETKPAEESKA
EKAQADKMPS KKPAEPKEKA 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
YNIIYDAIDD VKAAMSGMLS PEEKEQVTGT VEIRQVISVS KVGNIAGCMV TDGVVKRDSH
VRLIRNNVVI HTGELASLKR YKDDVKEVRM GFECGLMLKG YNEIMEGDQL ECFDIVEVAR
SL
