IF2_NEIMA
ID IF2_NEIMA Reviewed; 962 AA.
AC Q9JTB5; A1ITA1;
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=NMA1897;
OS Neisseria meningitidis serogroup A / serotype 4A (strain DSM 15465 /
OS Z2491).
OC Bacteria; Proteobacteria; Betaproteobacteria; Neisseriales; Neisseriaceae;
OC Neisseria.
OX NCBI_TaxID=122587;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15465 / Z2491;
RX PubMed=10761919; DOI=10.1038/35006655;
RA Parkhill J., Achtman M., James K.D., Bentley S.D., Churcher C.M.,
RA Klee S.R., Morelli G., Basham D., Brown D., Chillingworth T., Davies R.M.,
RA Davis P., Devlin K., Feltwell T., Hamlin N., Holroyd S., Jagels K.,
RA Leather S., Moule S., Mungall K.L., Quail M.A., Rajandream M.A.,
RA Rutherford K.M., Simmonds M., Skelton J., Whitehead S., Spratt B.G.,
RA Barrell B.G.;
RT "Complete DNA sequence of a serogroup A strain of Neisseria meningitidis
RT Z2491.";
RL Nature 404:502-506(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; AL157959; CAM09014.1; -; Genomic_DNA.
DR PIR; A81817; A81817.
DR RefSeq; WP_010981249.1; NC_003116.1.
DR AlphaFoldDB; Q9JTB5; -.
DR SMR; Q9JTB5; -.
DR EnsemblBacteria; CAM09014; CAM09014; NMA1897.
DR KEGG; nma:NMA1897; -.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OMA; NRDNRTG; -.
DR BioCyc; NMEN122587:NMA_RS09585-MON; -.
DR Proteomes; UP000000626; 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_0000137226"
FT DOMAIN 462..631
FT /note="tr-type G"
FT REGION 101..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; 103096 MW; 2054240A3C3ABDEC CRC64;
MSNTTVEQFA AELKRPVEDL LKQLKEAGVS KNSGSDSLTL DDKQLLNAYL TKKNGSNGGT
ISIRRTKTEV STVDGVKVET RKRGRTVNIP SAEELAAQVK AAQTQAAPVR PEQTAEDAAK
ARAEAATRAE ARAKAEAEAA KLKAAKAGNK AKPAAQKPTE AKAETAPVAA ETKPAEESKA
EKAQADKMPS KKPAEPKEKA AKPKHERNGK GKDAKKPAKP AAPAVPQPVV SAEEQAQRDE
EARRAAALRA HQEALLKEKQ ERQARREAMK QQAEQQAKAA QEAKTGRQRP AKPAEKPQAA
APAVENKPVN PAKAKKENRR NRDDEGQGRN AKGKGGKGGR DRNNARNGDD ERVRGSKKGK
KLKLEPNQHA FQAPTEPVVH EVLVPETITV ADLAHKMAVK GVEVVKALMK MGMMVTINQS
IDQDTALIVV EELGHIGKPA AADDPEAFLD EGAEAVEAEA LPRPPVVTVM GHVDHGKTSL
LDYIRRAKVV QGEAGGITQH IGAYHVKTPR GVITFLDTPG HEAFTAMRAR GAKATDIVIL
VVAADDGVMP QTIEAIAHAK AAGVPMVVAV NKIDKEAANP ERIRQELTAH EVVPDEWGGD
VQFIDVSAKK GLNIDALLEA VLLEAEVLEL TAPVDAPAKG IIVEARLDKG RGAVATLLVQ
SGTLKKGDML LAGTAFGKIR AMVDENGKAI NEAGPSIPVE ILGLSDVPNA GEDAMVLADE
KKAREIALFR QGKYRDVRLA KQQAAKLENM FNNMGETQAQ SLSVIIKADV QGSYEALAGS
LKKLSTDEVK VDVLHSGVGG ITESDVNLAI ASGAFIIGFN VRADASSRKL AENENVEIRY
YNIIYDAIDD VKAAMSGMLS PEEKEQVTGT VEIRQVISVS KVGNIAGCMV TDGVVKRDSH
ARLIRNNVVI HTGELSSLKR YKDDVKEVRM GFECGLMIKG YNEIMEGDQL ECFDIVEVAR
TL
