IF2_CUPNH
ID IF2_CUPNH Reviewed; 962 AA.
AC Q0K9B9;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=H16_A2306;
OS Cupriavidus necator (strain ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442
OS / H16 / Stanier 337) (Ralstonia eutropha).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=381666;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 17699 / DSM 428 / KCTC 22496 / NCIMB 10442 / H16 / Stanier 337;
RX PubMed=16964242; DOI=10.1038/nbt1244;
RA Pohlmann A., Fricke W.F., Reinecke F., Kusian B., Liesegang H., Cramm R.,
RA Eitinger T., Ewering C., Poetter M., Schwartz E., Strittmatter A., Voss I.,
RA Gottschalk G., Steinbuechel A., Friedrich B., Bowien B.;
RT "Genome sequence of the bioplastic-producing 'Knallgas' bacterium Ralstonia
RT eutropha H16.";
RL Nat. Biotechnol. 24:1257-1262(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; AM260479; CAJ93402.1; -; Genomic_DNA.
DR RefSeq; WP_010809483.1; NZ_CP039287.1.
DR AlphaFoldDB; Q0K9B9; -.
DR SMR; Q0K9B9; -.
DR STRING; 381666.H16_A2306; -.
DR EnsemblBacteria; CAJ93402; CAJ93402; H16_A2306.
DR GeneID; 57644436; -.
DR KEGG; reh:H16_A2306; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000008210; Chromosome 1.
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; 2.
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..962
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008310"
FT DOMAIN 462..631
FT /note="tr-type G"
FT REGION 52..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 121..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 471..478
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 496..500
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 517..520
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 571..574
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 607..609
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 52..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..249
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 266..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 319..337
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 471..478
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 517..521
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 571..574
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 962 AA; 103710 MW; AB8F163CF73F5741 CRC64;
MASTTVAQLA AELSRSAAAL LEQLQAAGVG KATPEDIITE SDKTRLLDYL KRSHGQADDS
SRKKITLTKR ETSEIRQSDG TGKTRTVQVE VRKKRVLIKR DEAAPDAQAD AVEAQAPVVD
AVEEARRDEE ERQQAELLAR QEAEAKAARE AAEREEAERR ARQEALEAEQ RRQAELAARK
AEEEAAASRA VTEANEDSSR KKAEDEKARV TAERAEAQKA ADEAKAAADK ARAEQEVAAR
KRREAAEAEA RAIQQMLNAP PRVLKAPSER KAEEKKAEQT GTLHKPVKPA GATTEAKKDE
KKPATTTTTT ATADKKGKVV KAGWQDDSSR KKGSGLKTRG DTSGGVGGWR GGPRGRGGRQ
QQHDDSRSSF QAPTEPVVRE VHVPETVSVA DLAHKMAVKA SEVIKQMMKL GQMVTINQVL
DQETAMIVVE EMGHKAYAAK LDDPEALLVV GGEEHTDAEL LPRPPVVTVM GHVDHGKTSL
LDYIRRTKVA AGEAGGITQH IGAYHVETDR GVITFLDTPG HEAFTAMRAR GAKATDIVIL
VVAADDGVMP QTKEAIAHAK AAGVPIVVAI NKIDKPDANP DRVKQELVAE QVVPEEYGGD
SPFVPVSAKM GTGVEDLLEQ VLLQAEVLEL TAPVDAPAKG LVVEAQLDKG KGPIATILVS
SGTLKRGDVV LAGSAYGRVR AMLDENGKPT KEAGPSIPVE IQGLSEVPAA GEEVLVLPDE
RKAREIALFR QGKFRDVKLA KQQAAKLENM LEQMAEGEVQ TLPLIVKADV QGSQEALVQS
LQKLSTAEVR VQIVHGGVGG ISESDVNLAT ASKAVIIGFN VRADAGARKL AEHNGIDIRY
YNIIYDAVDE IKAAMSGMLA PEKRETTIGQ VEVRQVFRVP KIGAVAGCMV TDGLVKRNSL
VRVLRNNVVI HDGELDSLKR FKDDVKEVKQ GFECGLSIKN FNDVQEGDQL EVYEITEVAR
TL
