IF2_HYPNA
ID IF2_HYPNA Reviewed; 853 AA.
AC Q0C5Z5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=HNE_0114;
OS Hyphomonas neptunium (strain ATCC 15444).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomonadales;
OC Hyphomonadaceae; Hyphomonas.
OX NCBI_TaxID=228405;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15444;
RX PubMed=16980487; DOI=10.1128/jb.00111-06;
RA Badger J.H., Hoover T.R., Brun Y.V., Weiner R.M., Laub M.T., Alexandre G.,
RA Mrazek J., Ren Q., Paulsen I.T., Nelson K.E., Khouri H.M., Radune D.,
RA Sosa J., Dodson R.J., Sullivan S.A., Rosovitz M.J., Madupu R.,
RA Brinkac L.M., Durkin A.S., Daugherty S.C., Kothari S.P., Giglio M.G.,
RA Zhou L., Haft D.H., Selengut J.D., Davidsen T.M., Yang Q., Zafar N.,
RA Ward N.L.;
RT "Comparative genomic evidence for a close relationship between the
RT dimorphic prosthecate bacteria Hyphomonas neptunium and Caulobacter
RT crescentus.";
RL J. Bacteriol. 188:6841-6850(2006).
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; CP000158; ABI75987.1; -; Genomic_DNA.
DR RefSeq; WP_011645148.1; NC_008358.1.
DR AlphaFoldDB; Q0C5Z5; -.
DR SMR; Q0C5Z5; -.
DR STRING; 228405.HNE_0114; -.
DR PRIDE; Q0C5Z5; -.
DR EnsemblBacteria; ABI75987; ABI75987; HNE_0114.
DR KEGG; hne:HNE_0114; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_1_5; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 98374at2; -.
DR Proteomes; UP000001959; 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; 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; 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..853
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335479"
FT DOMAIN 347..515
FT /note="tr-type G"
FT REGION 1..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..265
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 356..363
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 381..385
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 403..406
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 457..460
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 493..495
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 21..36
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 94..161
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 356..363
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 403..407
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 457..460
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 853 AA; 91692 MW; 14BCD8402F83280B CRC64;
MSDTNDQGNS GGRKPLTVVR KTSGTVKQSF SHGRSKQVVV ETKKRRPVSS GGGQGGDSGP
STPSASDGME AKLVALAAKL GITVAELKAR QKVLEQRKAE EASRAKDTEA ERAAQDRLRT
EQERKQQEAR EREEAELRRR AEEEAAKLAD VASREAVERP SKAPRAAPAA QTPPAADGEA
DAGRSKRSSG GGASKPARDD RADRAREVAT KPSRGDAERR RGKLTIASAL GDDADRQRSL
ASVRRARERE RERRVGGGDS NDKTSIEVTL PETITLQDLA QRMNERVADV VKFMFKQGEM
LRGNDIVDAD MAELIAGEFG HTVRRVSEAD VEIGLEGTDD RDEDLQPRAP IVTIMGHVDH
GKTSLLDALR KTDVAGGEAG GITQHIGAYQ VQLKSGERIT FLDTPGHAAF TAMRARGANA
TDIAILVVAA DDSVKPQTIE SISHAKAAGV PIVVAITKSD LHDANPEKVL TDLLQYDIQV
EAMGGVTQAV KVSAKTGAGL DELTDAISIQ AEILELKANP NRQADGVVIE SKLDKGRGPV
ATVLVKRGTL KRGDIVVAGA NWGKVRALVD ERGQQLADAG PSLPVEVLGL DGAPDPGDAI
VVVDSEARAR EITEYRIRTK RQVAGNASVA ARASLDQLMN RLKDGAIVTS ELPIVLKGDV
QGSVEAITMS LDKISTEEVR AKVIHGAVGG ISESDVLLAR SSNAPIFAFN VRANKQARDL
AEREGVEIRY YSIIYDLLDD VKATLSGMLA PEKRETFLGY ADILEVFNIT KVGKVAGCRI
SEGKVMRGCG VRLLRDNVVI HEGKLKTLKR FKDEVSEVNA GMECGMAFER YDDIRVGDKI
ECFQVEEIAR TLA
