IF2_CUPMC
ID IF2_CUPMC Reviewed; 979 AA.
AC Q1LLR6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-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=Rmet_2031;
OS Cupriavidus metallidurans (strain ATCC 43123 / DSM 2839 / NBRC 102507 /
OS CH34) (Ralstonia metallidurans).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Cupriavidus.
OX NCBI_TaxID=266264;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43123 / DSM 2839 / NBRC 102507 / CH34;
RX PubMed=20463976; DOI=10.1371/journal.pone.0010433;
RA Janssen P.J., Van Houdt R., Moors H., Monsieurs P., Morin N., Michaux A.,
RA Benotmane M.A., Leys N., Vallaeys T., Lapidus A., Monchy S., Medigue C.,
RA Taghavi S., McCorkle S., Dunn J., van der Lelie D., Mergeay M.;
RT "The complete genome sequence of Cupriavidus metallidurans strain CH34, a
RT master survivalist in harsh and anthropogenic environments.";
RL PLoS ONE 5:E10433-E10433(2010).
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; CP000352; ABF08910.1; -; Genomic_DNA.
DR RefSeq; WP_011516746.1; NC_007973.1.
DR AlphaFoldDB; Q1LLR6; -.
DR SMR; Q1LLR6; -.
DR STRING; 266264.Rmet_2031; -.
DR PRIDE; Q1LLR6; -.
DR EnsemblBacteria; ABF08910; ABF08910; Rmet_2031.
DR KEGG; rme:Rmet_2031; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_0_4; -.
DR OMA; RDVMMAG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000002429; 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; 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..979
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335501"
FT DOMAIN 479..646
FT /note="tr-type G"
FT REGION 50..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 488..495
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 513..517
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 534..537
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 588..591
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 624..626
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 50..78
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 279..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 488..495
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 534..538
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 588..591
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 979 AA; 104941 MW; B72464CECD3E8F1E CRC64;
MASTTVAQLA AELSRSPAAL LEQLQAAGVG KATPDDVITE SDKTRLLDYL KRSHGQSDDS
ARKKITLTKR ETSEIRQSDS TGKTRTVQVE VRKKRVLIKR DDVESHGDGA DSQESAEAAA
EEVRRDEEQR REQAEALARQ EAEAQAAREA AEREEAERRA KQEALEAEQR RQAELLAQKA
AEEAAAAQAA ADAAEETARE KAEEDKARLA TERAQAQKNA DDAKAAVDKA RAEQDSAKAA
ADKARAEQDA AARRRREAAE AEARAIQQML NAPPRVLKAP SERKAEEKKA EQTGTLHKPV
KPAGATTEAK KDDKKAAPAA TTTTAAAGDK KGAKGGKTGT WQDEGSRGKK GGGLKTRGDS
SGGVGGWRSG PRGRGGKHNA DDARSNFQAP TEPVVREVHV PETVSVADLA HKMAVKASEV
IKQMMKLGQM VTINQVLDQE TAMIVVEEMG HKAFAAKLDD PEALLVVDGE DHGDAEMLPR
PPVVTVMGHV DHGKTSLLDY IRRTKVAAGE AGGITQHIGA YHVETDRGVI TFLDTPGHEA
FTAMRARGAK ATDIVILVVA ADDGVMPQTK EAIAHAKAAG VPIVVAITKV DKPEANPDRV
KQELVAEQVV PEEYGGESPF VPVSAKTGQG IDDLLENVLL QAEVLELRAP VDAPAKGLVV
EAQLDKGKGP IATILVSSGT LKRGDVVLAG SAYGRVRAML DENGKPSKEA GPSIPVEIQG
LSEVPAAGEE VLVLPDERKA REIALFRQGK FRDVKLAKQQ AAKLETMLEQ MAEGEVQTLP
LIVKADVQGS QEALVQSLQK LSTSEVRVQI VHGGVGGISE SDVNLATASK AVIIGFNVRA
DAGARKLAEH NGIDIRYYNI IYDAVDEIKA AMSGMLAPEK RETTIGQVEV RQVFRVPKVG
AVAGCMVTDG LIKRNSMVRV LRNNVVIHDG ELDSLKRFKD DVKEVKQGFE CGLSIKNFND
VQEGDQLEVY EITEVARTL
