IF2_BURCM
ID IF2_BURCM Reviewed; 971 AA.
AC Q0BFY3;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 17-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Bamb_1382;
OS Burkholderia ambifaria (strain ATCC BAA-244 / AMMD) (Burkholderia cepacia
OS (strain AMMD)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=339670;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-244 / AMMD;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Bruce D., Chain P.,
RA Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., Parke J., Coenye T., Konstantinidis K.,
RA Ramette A., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Burkholderia cepacia AMMD.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000440; ABI86940.1; -; Genomic_DNA.
DR RefSeq; WP_011656689.1; NZ_CP009798.1.
DR AlphaFoldDB; Q0BFY3; -.
DR SMR; Q0BFY3; -.
DR STRING; 339670.Bamb_1382; -.
DR PRIDE; Q0BFY3; -.
DR EnsemblBacteria; ABI86940; ABI86940; Bamb_1382.
DR GeneID; 44692061; -.
DR KEGG; bam:Bamb_1382; -.
DR PATRIC; fig|339670.21.peg.160; -.
DR eggNOG; COG0532; Bacteria.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000000662; 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..971
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008210"
FT DOMAIN 471..640
FT /note="tr-type G"
FT REGION 49..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 101..385
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..487
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 505..509
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 526..529
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 580..583
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 616..618
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 49..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 116..179
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 192..207
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 340..354
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 480..487
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 526..530
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 580..583
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 971 AA; 104324 MW; CBBB7D801CDDDAB5 CRC64;
MASNNVAQFA AELKMPAGVL LEQLQAAGVQ KASEDDALSE ADKARLLDHL RKSHGATDGD
KRKITLTRKH TSEIKQSDAT GKARTIQVEV RKKRTFVKRD DVAEGAEQGQ AQVAEADDDA
ELKRREEEAR REAELLEKQA QELRERQERL EREEAERRAR EEAAEAQRRR AEEEAAAKRA
AAAAVEAQQV AAQQAAEAQQ ETAGAQSAQD EARAAAERAA QREAAKKAED AAREAADKTR
AEQEEIRKRR EAAEAEARAI REMMNTPRKA MVKAVEPPKP VEPPKPVEAK GTLHKPAKPA
GASAARPAVK KPAGAAPATT APAGAGDRNK KPGGGKGGWQ DDAAKRRGIK TRGDSSGGVD
RGWRGGPKGR GRHQDSASTF QAPTEPIVRE VHVPETVSVA DLAHKMSIKA SEVIKVMMKM
GQMVTINQVL DQETAMIVVE ELGHRAVAAK LDDPEALLVE GETTTDAEQL PRPPVVTVMG
HVDHGKTSLL DHIRRAKVAA GEAGGITQHI GAYHVETPRG VITFLDTPGH EAFTAMRARG
AKATDIVVLV VAADDGVMPQ TKEAIAHAKA GGVPIVVAIN KIDKPEANPD RVKQELVAEG
VVPEEYGGDS PFVPVSAKTG VGIDDLLENV LLQAEVLELK APIEAPAKGI VIEAKLDKGK
GPVATILVQS GTLNRGDVVL AGSAYGRVRA MLDENGKPTK EAGPSIPVEI QGLSEVPGAG
EEVIVLPDER KAREIALFRQ GKFRDVKLAK QQAAKLESML EQMGEGEVQN LPLIIKADVQ
GSQEALVQSL LKLSTDEVRV QIVHSAVGGI SENDVNLATA SKAVIIGFNT RADAQARKLA
ESNGIDIRYY NIIYDAVDEV KAAMSGMLAP EKREVITGMV EVRQVFKVPK IGTVAGCMVT
DGIVKRSSSV RVLRNNVVIF TGELESLKRF KDDVKEVKQG FECGMSVKNF NDVTEGDQFE
VFEVTEVART L
