IF2_CUPTR
ID IF2_CUPTR Reviewed; 963 AA.
AC B3R1E4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=RALTA_A1850;
OS Cupriavidus taiwanensis (strain DSM 17343 / BCRC 17206 / CCUG 44338 / CIP
OS 107171 / LMG 19424 / R1) (Ralstonia taiwanensis (strain LMG 19424)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=977880;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17343 / BCRC 17206 / CCUG 44338 / CIP 107171 / LMG 19424 / R1;
RX PubMed=18490699; DOI=10.1101/gr.076448.108;
RA Amadou C., Pascal G., Mangenot S., Glew M., Bontemps C., Capela D.,
RA Carrere S., Cruveiller S., Dossat C., Lajus A., Marchetti M., Poinsot V.,
RA Rouy Z., Servin B., Saad M., Schenowitz C., Barbe V., Batut J., Medigue C.,
RA Masson-Boivin C.;
RT "Genome sequence of the beta-rhizobium Cupriavidus taiwanensis and
RT comparative genomics of rhizobia.";
RL Genome Res. 18:1472-1483(2008).
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; CU633749; CAQ69791.1; -; Genomic_DNA.
DR RefSeq; WP_012353108.1; NC_010528.1.
DR AlphaFoldDB; B3R1E4; -.
DR SMR; B3R1E4; -.
DR STRING; 977880.RALTA_A1850; -.
DR PRIDE; B3R1E4; -.
DR EnsemblBacteria; CAQ69791; CAQ69791; RALTA_A1850.
DR GeneID; 29760508; -.
DR KEGG; cti:RALTA_A1850; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR BioCyc; CTAI977880:RALTA_RS08915-MON; -.
DR Proteomes; UP000001692; 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.
FT CHAIN 1..963
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093780"
FT DOMAIN 463..632
FT /note="tr-type G"
FT REGION 53..377
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..479
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 497..501
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 518..521
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 572..575
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 608..610
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 53..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..108
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 117..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 302..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 472..479
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 518..522
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 572..575
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 963 AA; 103804 MW; B6F782AAE2E05491 CRC64;
MASTTVAQLA AELSRSAAAL LEQLQAAGVG KATPEDIITE SDKTRLLDYL KRSHGQADDS
ARKKITLTKR ETSEIRQSDA TGKTRTVQVE VRKKRVLIKR DDAAPEHQAD GAEAQAHVVD
AAEEARREEE ERRQAEQLAR QEAEAKAARE AAEREEAERR ARQEALEAEQ RRQAELAARK
AEEEAAASRA VTEANEDTSR KKAEDEKARV AAERAEAQKA ADEAKAAADK ARAEQEIAAR
KRREAAEAEA RAIQQMLNAP ARVLKAPSER KAEEKKAEQT GTLHKPVKPA GTEAKPGEKK
PVTATATTTT DKKGKVVKAG TSSTWQDEGS RKKGSGLKTR GDSSGGVGGW RGGPRGRGGR
QQQHDDSRSN FQAPTEPVVR EVHVPETISV ADLAHKMAVK ASEVIKQMMK LGQMVTINQV
LDQETAMIVV EEMGHKAYAA KLDDPEALLV VDGEEHEDAE LLPRPPVVTV MGHVDHGKTS
LLDYIRRTKV AAGEAGGITQ HIGAYHVETD RGVITFLDTP GHEAFTAMRA RGAKATDIVI
LVVAADDGVM PQTKEAIAHA KAAGVPIVVA INKVDKPEAN PDRVKQELVA EQVVPEEYGG
DSPFVPVSAK TGAGIEDLLE QVSLQAEVLE LKAPVDAPAK GLVVEAQLDK GKGPIATILV
SSGTLKRGDV VLAGSAYGRV RAMLDENGKA TKEAGPSIPV EIQGLSEVPA AGEEVLVLPD
ERKAREIALF RQGKFRDVKL AKQQAAKLEN MLEQMTEGEV QTLPLIVKAD VQGSQEALVQ
SLQKLSTAEV RVQIVHGGVG GISESDVNLA TASKAVIIGF NVRADAGARK LAEHNGIDIR
YYNIIYDAVD EIKAAMSGML APEKRETTTG TVEVRQVFRV PKVGAVAGCM VTDGVVKRNS
LVRVLRNNVV IHDGELDSLK RFKDDVKEVK QGFECGLSIK NFNDVQEGDQ LEVYEITEVA
RTL
