IF2_STRU0
ID IF2_STRU0 Reviewed; 949 AA.
AC B9DVB7;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=SUB1466;
OS Streptococcus uberis (strain ATCC BAA-854 / 0140J).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=218495;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-854 / 0140J;
RX PubMed=19175920; DOI=10.1186/1471-2164-10-54;
RA Ward P.N., Holden M.T.G., Leigh J.A., Lennard N., Bignell A., Barron A.,
RA Clark L., Quail M.A., Woodward J., Barrell B.G., Egan S.A., Field T.R.,
RA Maskell D., Kehoe M., Dowson C.G., Chanter N., Whatmore A.M., Bentley S.D.,
RA Parkhill J.;
RT "Evidence for niche adaptation in the genome of the bovine pathogen
RT Streptococcus uberis.";
RL BMC Genomics 10:54-54(2009).
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; AM946015; CAR43153.1; -; Genomic_DNA.
DR RefSeq; WP_015911778.1; NC_012004.1.
DR AlphaFoldDB; B9DVB7; -.
DR SMR; B9DVB7; -.
DR STRING; 218495.SUB1466; -.
DR PRIDE; B9DVB7; -.
DR EnsemblBacteria; CAR43153; CAR43153; SUB1466.
DR KEGG; sub:SUB1466; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_0_9; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000449; 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; 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; 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..949
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000190640"
FT DOMAIN 450..619
FT /note="tr-type G"
FT REGION 50..206
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 220..359
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 459..466
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 484..488
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 505..508
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 559..562
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 595..597
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 50..85
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 166..202
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..308
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 309..333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 459..466
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 505..509
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 559..562
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 949 AA; 105493 MW; 1441E2F32938DEA4 CRC64;
MSKKRLHEIA KEIGKTSKEV VEKAKSLGLD VKSHASSVSE EDAKKIVSTF TEKPKTETKP
KIKAVDETPK PKLEAVKEEV KVEKTQTVQE TVNPTVARPK SRNFKAEREA RAKEQAARQK
RNAQESTERR QDNRYQQKND QGSKNRNFNK SQGQAKDRRF DAKGSQQNNR QDSRIASNKP
NHNDKFNAAN RNQNNSQQER QVGAARIDFK ARAAALKAEQ NAEYMRHKET QLREQEEARR
LAERAKEEAR LAAQKAAEEK AKEAEKAAKT ERFEPKSAVA STVAPEAVKP VDKRRKKARP
EKSYEDQSSN ENGPKQNKKS WNNQNQVRNQ RNSNWNKKPK KGKNAKNNTV APKPVTERKF
HELPKEFEYT EGMTVVEIAK RIKREPAEIV KKLFMMGVMA TQNQSLDGDT IELLMVDYGI
EAKEKVQVDD ADIERFFEDD TYLNPDKLVE RAPVVTIMGH VDHGKTTLLD TLRNSRVATG
EAGGITQHIG AYQIEEAGKK ITFLDTPGHA AFTSMRARGA SVTDITILIV AADDGVMPQT
IEAINHSKAA EVPIIVAINK IDKPGANPER VISELAEHGI ISTAWGGDSE FVEISAKFNK
NIDELLETVL LVAEVEELKA DPTVRAIGTV IEARLDKGKG AVATLLVQQG TLHVQDPIVI
GNTFGRVRAM TNDLGRRVKV APPSTPVSIT GLNETPMAGD HFAVYEDEKA ARAAGEERAK
RALLKQRQNT QRVSLDNLFD TLKAGEIKTV NVIIKADVQG SVEALAASLL KIEVEGVRVN
VVHSAVGAIN ESDVTLAEAS NAVIIGFNVR PTPQARQQAE TDDVEIRLHS IIYKVIEEVE
EAMKGKLDPE YKEKILGEAV IRETFKVSKV GTIGGFMVLS GKITRDSNVR VIRDSVVIFD
GKLASLKHYK DDVKEVGNAQ EGGLMIEKFN DLQVDDNIEA YIMEEIVRK
