IF2_METSB
ID IF2_METSB Reviewed; 886 AA.
AC B8EIA7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 80.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Msil_2295;
OS Methylocella silvestris (strain DSM 15510 / CIP 108128 / LMG 27833 / NCIMB
OS 13906 / BL2).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Beijerinckiaceae; Methylocella.
OX NCBI_TaxID=395965;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15510 / CIP 108128 / LMG 27833 / NCIMB 13906 / BL2;
RX PubMed=20472789; DOI=10.1128/jb.00506-10;
RA Chen Y., Crombie A., Rahman M.T., Dedysh S.N., Liesack W., Stott M.B.,
RA Alam M., Theisen A.R., Murrell J.C., Dunfield P.F.;
RT "Complete genome sequence of the aerobic facultative methanotroph
RT Methylocella silvestris BL2.";
RL J. Bacteriol. 192:3840-3841(2010).
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; CP001280; ACK51226.1; -; Genomic_DNA.
DR RefSeq; WP_012591295.1; NC_011666.1.
DR AlphaFoldDB; B8EIA7; -.
DR SMR; B8EIA7; -.
DR STRING; 395965.Msil_2295; -.
DR EnsemblBacteria; ACK51226; ACK51226; Msil_2295.
DR KEGG; msl:Msil_2295; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_0_5; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 129583at2; -.
DR Proteomes; UP000002257; 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; IPR004161; EFTu-like_2.
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; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 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..886
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000118767"
FT DOMAIN 383..553
FT /note="tr-type G"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 50..229
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 253..272
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 392..399
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 417..421
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 439..442
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 493..496
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 529..531
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 1..20
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 71..87
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 88..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..183
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 392..399
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 439..443
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 493..496
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 886 AA; 95767 MW; 2CAE01D15CC706CF CRC64;
MSETKNPGDH TLSVSPTKTL SLKRPVEAGI VRQSFSHGRS KAVVVEKVKR RALGEPHVLR
ESAPALDVVA PAPQAAPPAP TQQPQPRVAS RPQPQQRSSS GVILRSLTEE EREARSRALS
GAHEREVEER KRAEIEAKAR DEREAREREE RAAAEARKRE EETRRLQEAE SKRRSESEAK
RRLAGGEPAP AGANAAPRKA PALSAAPGSA APSGQPGPAG AVGARPAEEE DAAKRIIRRP
GMPTKVIVAR PVKGAEQKSR GRLTVASATG DEEERTRSIA AFRRRTQRLK GHVSETKEKL
SREVVLPETI TIQELANRMS ERAVDVIKLM MKQGQMAKIT DVIDADTAQL IAEELGHTVK
RVAESDVEEG LFDSPDVEEH LISRPPVVTI MGHVDHGKTS LLDALRHANV VSGEAGGITQ
HIGAYQIVAS NGLPITFIDT PGHAAFTAMR ARGAKVTDIV VLVVAADDGV MPQTAEAISH
AKAAGVPIIV AINKIDKPDA KPERVRQELL QYEVQVESLG GDTLEVEVSA TKKINLDKLA
DLIALQAELL DLKASPDRPA EGTVIEARLD KGRGPVATVL VQRGTLKVGD LIVGGSQWGK
VRALIDDKGV NRQEAGPSMP VEVLGFSGSP EAGDRVGVVE NEARAREIAA YRDRQKREQA
AARGNLARGS LADMMSQLKT AARKEFPLVI KADVQGSLEA IVATLEKLNT DEVAARIIHA
GVGGITESDV TLAEASGAVL IGFNVRAHKE GRQLAEQQGL EIRYYNIIYN LVDDVKAAMS
GLLAPTLRED MLGNAEILEV FHISKVGKVA GCRVTDGRVE RGANVRLIRD NVVVHEGKLS
TLKRFKDEVK EVVAGQECGM AFEHYQDMRV GDVIECYRVE EIQRTL
