IF2_MANSM
ID IF2_MANSM Reviewed; 820 AA.
AC Q65SK9;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 25-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=MS1444;
OS Mannheimia succiniciproducens (strain MBEL55E).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Basfia.
OX NCBI_TaxID=221988;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MBEL55E;
RX PubMed=15378067; DOI=10.1038/nbt1010;
RA Hong S.H., Kim J.S., Lee S.Y., In Y.H., Choi S.S., Rih J.-K., Kim C.H.,
RA Jeong H., Hur C.G., Kim J.J.;
RT "The genome sequence of the capnophilic rumen bacterium Mannheimia
RT succiniciproducens.";
RL Nat. Biotechnol. 22:1275-1281(2004).
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; AE016827; AAU38051.1; -; Genomic_DNA.
DR RefSeq; WP_011200618.1; NC_006300.1.
DR AlphaFoldDB; Q65SK9; -.
DR SMR; Q65SK9; -.
DR STRING; 221988.MS1444; -.
DR EnsemblBacteria; AAU38051; AAU38051; MS1444.
DR KEGG; msu:MS1444; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000607; 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; 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..820
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228211"
FT DOMAIN 320..489
FT /note="tr-type G"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 113..234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 329..336
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 354..358
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 375..378
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 429..432
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 465..467
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 113..153
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 329..336
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 375..379
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 429..432
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 820 AA; 89538 MW; C5FB76637A3D7F17 CRC64;
MTDKETQNEN APKKLSLQRR VKTTVAGGKV QVEVRKSRKI DTEAAKKAAE EAKLKAQEAA
EKAAAEKAEK EAAEKAKKNA EKARVAAAVK KPEPVKVVDA EKDRIKAEEA ELRRKADELA
RQKAEEQARK AAEEAKRLAE LAADRETTEV SDDFSDYHLT STYAREAEDE EERRKEGRGR
GKNKVGKAKK GGRDDNGSKD ERNADRRNQK DVKGKGKQGK KGSSAIQQAF TKPAQAVNRD
VVIGETITVA ELANKMAVKA TEIIKTMMKM GEMVTINQVI DQETAQLVAE EMGHKVILRK
ENELEESVLE DRDVNAEKVT RAPVVTIMGH VDHGKTSLLD YIRKAKVAAG EAGGITQHIG
AYHVETNGKM ITFLDTPGHA AFTSMRARGA KATDIVVLVV AADDGVMPQT IEAIQHARAA
SVPLVVAVNK IDKPEANPDR VEQELLQYDV VSEKFGGDTQ FVYVSAKKGT GVDELLDAIL
LQSEVLELTA VKEGMATGVV IESYLDKGRG PVATILVQSG TLNRGDILLC GFEYGRVRAM
RDELGKDVES AGPSIPVEVL GLSGVPAAGD EATVVRDEKK AREVALYRQG KFREVKLARQ
QKAKLENMFS NMAEGDVAEL NVIVKADVQG SVEAIVQSLQ ELSTEEVKVK VVGSGVGGIT
ETDATLAAAS NAIIVGFNVR ADASARRIIE TENIDLRYYS IIYELLNEIK AAMSGMLQPE
FKQEIIGLAE VRDVFRSPKF GAIAGCMVTE GVIKRNNPIR VLRDNVVIFE GELESLRRFK
DDVNEVRNGM ECGIGVKNYN DVKVGDQIEV FEVVEIKRSI
