IF2_PARXL
ID IF2_PARXL Reviewed; 989 AA.
AC Q140U6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 22-AUG-2006, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Bxeno_A1605;
GN ORFNames=Bxe_A2820;
OS Paraburkholderia xenovorans (strain LB400).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Paraburkholderia.
OX NCBI_TaxID=266265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LB400;
RX PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA Chain P.S.G., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M., Lao V.,
RA Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A., Marx C.J.,
RA Parnell J.J., Ramette A., Richardson P., Seeger M., Smith D., Spilker T.,
RA Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B., Tiedje J.M.;
RT "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp genome
RT shaped for versatility.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(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; CP000270; ABE30143.1; -; Genomic_DNA.
DR RefSeq; WP_011487846.1; NZ_CP008760.1.
DR AlphaFoldDB; Q140U6; -.
DR SMR; Q140U6; -.
DR STRING; 266265.Bxe_A2820; -.
DR EnsemblBacteria; ABE30143; ABE30143; Bxe_A2820.
DR KEGG; bxb:DR64_502; -.
DR KEGG; bxe:Bxe_A2820; -.
DR PATRIC; fig|266265.5.peg.1671; -.
DR eggNOG; COG0532; Bacteria.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001817; 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..989
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008218"
FT DOMAIN 489..658
FT /note="tr-type G"
FT REGION 28..60
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..505
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 523..527
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 544..547
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 598..601
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 634..636
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 35..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..282
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 353..373
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 498..505
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 544..548
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 598..601
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 989 AA; 106048 MW; A76E6E9F7474E71E CRC64;
MASNNVAQFA AELKMPAGVL LEQLQAAGVT KASEDDSLSE TDKARLLDHL RKSHGSTDAD
KRKITLTKRH TSEIKQSDAT GKARTIQVEV RKKRTFVRRD ETSAENGDAS NHVAEAEVDD
LELQRREEEA RHEAELLEKQ AQELKARQEQ LEREEAERQA REAAAEVERR RAEEEAAKKR
AAAAAEAAAR EQQTQASKPA QAAQPAAAKA EPVAAKAAEP VVARQSEQDD ERAAAERAAQ
REAAKKAEDA ARQAAEKARA EQEEIAKRRA AAEAEARAIR EMMNTPRKAQ VKAPEPAPKP
AEPAKAAEAK GTLHKPARPA GEAPARPAAK KPAAAAPAAT TTPSAGDKKK PGGGKGGWQD
DAAKRRGIKT RGDTSGGVDR GWRGGPKGRG KHQDQNTTFQ APTEPIVREV HVPETITVAD
LAHKMAVKAS EVIKSMMKLG QMVTINQMLD QETAMIIVEE LGHHAVAAKL DDPEAMLVEG
EVSDAESLPR PPVVTVMGHV DHGKTSLLDY IRRAKVAAGE AGGITQHIGA YHVETPRGVI
TFLDTPGHEA FTAMRARGAK ATDIVILVVA ADDGVMPQTK EAIAHAKAGG VPLVVAINKI
DKPDANPERV KQELVAEGVV PEEYGGDSPF VSVSAKTGAG IDDLLENVLL QAEVLELKAP
VEAPAKGLVI EAKLDKGKGP VATILVQSGT LNRGDVVLAG SAYGRVRAML DETGKPTKSA
GPSIPVEIQG LSEVPQAGEE VIVMPDERKA REVALFRQGK FRDVKLAKQQ AAKLENMLEQ
MGEGEVQYMP LIVKADVQGS QEALVQSLLK LSTDEVRVQI VHGAVGGISE SDVNLATASK
AVIIGFNTRA DAQARKLAEA NGVDIRYYNI IYDAVDDVKA AMSGMLAPEK REVVTGTVEV
RQVFKVPKIG AVAGCMVTDG FVKRSSSVRV LRNNVVIFTG ELDSLKRFKD DVKEVRQGFE
CGMSIKNFND IVEGDQFEVF EVTEVARSL
