IF2_METPP
ID IF2_METPP Reviewed; 948 AA.
AC A2SH40;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Mpe_A1921;
OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Methylibium.
OX NCBI_TaxID=420662;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1;
RX PubMed=17158667; DOI=10.1128/jb.01259-06;
RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W.,
RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M.,
RA Hristova K.R.;
RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta-
RT proteobacterium Methylibium petroleiphilum PM1.";
RL J. Bacteriol. 189:1931-1945(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; CP000555; ABM94879.1; -; Genomic_DNA.
DR RefSeq; WP_011829516.1; NC_008825.1.
DR AlphaFoldDB; A2SH40; -.
DR SMR; A2SH40; -.
DR STRING; 420662.Mpe_A1921; -.
DR PRIDE; A2SH40; -.
DR EnsemblBacteria; ABM94879; ABM94879; Mpe_A1921.
DR KEGG; mpt:Mpe_A1921; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_4; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000366; 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; IPR013575; IF2_assoc_dom_bac.
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; PF08364; IF2_assoc; 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.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..948
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008275"
FT DOMAIN 448..615
FT /note="tr-type G"
FT REGION 256..362
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..464
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 482..486
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 503..506
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 557..560
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 593..595
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 259..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 300..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 457..464
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 503..507
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 557..560
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 948 AA; 101248 MW; A1A5F4F817E09EE8 CRC64;
MAVTTVAQFA AELNRPAAAL LEQLHSAGVA KASTDDALTE ADKERLLDFL RSSHGTGSAE
RKKITLTKKS TTEIKQADAS GKARTIQVEV RKKRTFIRRD DAPAAVEETT AAAPVIDEAE
LQKREEEASR QAELLRRQEE DLAEKRRARE AQEQAEREAA EARQRAAAEA AAAALEAAAA
EPVVPAKVEA TGVKAAAPDT APAVAAPAEP PKPALRVVKA ADIEAEEKQK AADLAKRRKA
AEDEASAIRA MMNAPKKVLV AKKPEEPKPA EGIKGTIHKP TAKPGAPAAA GAAGAAKPGD
KKSVKSEKLS SSWADDAAKK RAALRGGARP DAGGRGGWKA PRGGRRGGDR GDSPSTFTAP
AEAQVYEVHV PETISVADLA HKMSVKASEV IKQLMKLGQM VTINQQLDQE TAMILVEEMG
HKAFTAKLDD PDAFLEDDVE VTDVPLEPRA PVVTVMGHVD HGKTSLLDYI RTTRVAAGEA
GGITQHIGAY HVETPRGMIT FLDTPGHEAF TAMRARGAKA TDLVILVVAA DDGVMPQTKE
AIHHAKAAEV PLIVAINKID KPGTNLERVR SELIAEQVVP EDFGGDSPFV QVSAKTGQGI
DELLEQVLLQ AEVLELQAQV AAPAKGLVIE AQLDKGRGPV ATVLVQSGTL KRGDVVLAGS
TYGRVRAMLD ENGKPATEAG PSIPVEIQGL TEVPQAGDEF MVLSDERRAR EIATFRSGKY
RDVKLSKQQA AKLENMFETM GQGEVQTLPL IIKADVQGSQ EALGASLLKL STAEVKVQIV
HAAVGGISES DVNLAIASKA VIIGFNVRAD AGARKLAEGN NVDLRYYNII YDAVDEIKSA
MTGMLAPEQK EELIGTAEIR TVFVASKIGT VAGSMVTSGI VRRNARFRLL RENVVVYSGE
IESVRRMKDD VREVKEGFEC GIKLKNYNDI KEGDQLEVFE IKEVARTL
