IF2_METFK
ID IF2_METFK Reviewed; 907 AA.
AC Q1GXD6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUN-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Mfla_0067;
OS Methylobacillus flagellatus (strain KT / ATCC 51484 / DSM 6875).
OC Bacteria; Proteobacteria; Betaproteobacteria; Nitrosomonadales;
OC Methylophilaceae; Methylobacillus.
OX NCBI_TaxID=265072;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KT / ATCC 51484 / DSM 6875;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Brettin T., Bruce D., Han C., Tapia R., Saunders E., Gilna P., Schmutz J.,
RA Larimer F., Land M., Kyrpides N., Anderson I., Richardson P.;
RT "Complete sequence of Methylobacillus flagellatus KT.";
RL Submitted (MAR-2006) 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; CP000284; ABE48338.1; -; Genomic_DNA.
DR RefSeq; WP_011478435.1; NC_007947.1.
DR AlphaFoldDB; Q1GXD6; -.
DR SMR; Q1GXD6; -.
DR STRING; 265072.Mfla_0067; -.
DR EnsemblBacteria; ABE48338; ABE48338; Mfla_0067.
DR KEGG; mfa:Mfla_0067; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000002440; 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; 1.
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..907
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008272"
FT DOMAIN 407..576
FT /note="tr-type G"
FT REGION 223..320
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 416..423
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 441..445
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 462..465
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 516..519
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 552..554
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 223..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 247..287
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 416..423
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 462..466
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 516..519
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 907 AA; 98032 MW; C90DF360ED285AD0 CRC64;
MGQSSVAQFA SELGLPAELL LEQLRGAGVN KTAYDDVLTE QDKTSLLEYL RKEHGVQEPK
NKITLTRKQV TEIKKSDSSG KARTIQVEVR KKRVLVRRDP ALEPVVAEES AEIAPAAVID
EPTLQAAPVV LPEPEPVVEA VPEPVAVEQE LESEPEPTVA PAEPEAGEVA VAVDEKPTAD
ARPKLTAREL LGAEELALRE REAKRQAALM AIQAEELRKK QELAQRRQEE AKRAAEAAAN
KLSEGTLHKP VAKEAPKPEE KNAKKTGKSG GKDWNDSDGK KRGGVKGRSD AGVAGQGWRA
KGSKSKSKNN ENQQHAFTAP TEPIVHDVLV PETITVGDLA HKMAVKASEV IKTLMKMGMM
VTINQVLDQE TAIIIVEEMG HNAKAAASND PEAFLDEAEH AEAVQEPRPP VVTVMGHVDH
GKTSLLDYIR RSRVASGEAG GITQHIGAYH VETPRGMVTF LDTPGHEAFT AMRARGAKAT
DVVILVVAAD DGVMPQTIEA VHHAKAANVP IVVAVNKIDK PEANPERVKQ ELVSHEVVPE
DWGGDTMFVE VSAKTGAGID NLLEAVLLQA EVLELKAPKN IPAKGLVIEG RLDKGRGPVS
TILVQSGTLQ RGDMILAGTA YGRVRAMLDE SGRDVKEAGP SIPVEILGLS DVPSAGEEVI
VLNDERKARE IALFRQGKFR DVKLAKQQAA KLESMFEQMG EGEVKVLHLI IKSDVQGSYE
ALSTSLQKLS TDEVKVNIIH TGVGAISESD VNLAAASKAV LIGFNVRADA GARKLIESTG
VDVRYYNIIY EAVDEVKAAL GGMLSPEQKE NVIGTVEIRE VFRISKVGSV AGCYVQDGVV
RRNSKVRLIR DNVVIHTGEL DSLKRFKDDV KEVKSNFECG LSLKNYNEIE VGDILEVFEV
VEVARTL
