ID B1T1I3_9BURK Unreviewed; 972 AA.
AC B1T1I3;
DT 20-MAY-2008, integrated into UniProtKB/TrEMBL.
DT 20-MAY-2008, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000256|HAMAP-Rule:MF_00100};
GN ORFNames=BamMEX5DRAFT_1649 {ECO:0000313|EMBL:EDT42553.1};
OS Burkholderia ambifaria MEX-5.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=396597 {ECO:0000313|EMBL:EDT42553.1, ECO:0000313|Proteomes:UP000004814};
RN [1] {ECO:0000313|EMBL:EDT42553.1, ECO:0000313|Proteomes:UP000004814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MEX-5 {ECO:0000313|EMBL:EDT42553.1,
RC ECO:0000313|Proteomes:UP000004814};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Larimer F., Land M.L., Hauser L.,
RA Tiedje J., Richardson P.;
RT "Sequencing of the draft genome and assembly of Burkholderia ambifaria MEX-
RT 5.";
RL Submitted (MAR-2008) 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:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000644}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|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:0000256|ARBA:ARBA00007733, ECO:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000644}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EDT42553.1}.
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DR EMBL; ABLK01000035; EDT42553.1; -; Genomic_DNA.
DR RefSeq; WP_006757629.1; NZ_ABLK01000035.1.
DR AlphaFoldDB; B1T1I3; -.
DR PATRIC; fig|396597.7.peg.6592; -.
DR Proteomes; UP000004814; Unassembled WGS sequence.
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; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.56.50; Putative DNA-binding domain, N-terminal subdomain of bacterial translation initiation factor IF2; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 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 NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 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; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46955; Putative DNA-binding domain; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS01176; IF2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00100};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00100}.
FT DOMAIN 472..641
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 49..86
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 99..386
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 475..623
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
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 341..355
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 481..488
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 527..531
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 581..584
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 972 AA; 104385 MW; F776B8883A5EEB3D CRC64;
MASNNVAQFA AELKMPAGVL LEQLQAAGVQ KASEDDALSE ADKARLLDHL RKSHGATDGD
KRKITLTRKH TSEIKQSDAT GKARTIQVEV RKKRTFVKRD DVAEGAEQGQ AQVAEADDDA
ELKRREEEAR REAELLEKQA QELRERQERL EREEAERRAR EEAAEAERRR AEEEAVVKRA
AAEAAAAQQV AAQQAAEAQQ ESAGAQSAQD EARAAAERAA QREAAKKAED AAREAADKTR
AEQEEIRKRR EAAEAEARAI REMMNTPRKA VVKAVEPPKP VEPPKPVEAK GTLHKPAKPA
GAGAARPAVK KPAGAAPATT QAPAGAGDRN KKPGGGKGGW QDDAAKRRGI KTRGDSSGGV
DRGWRGGPKG RGRHQDSAST FQAPTEPIVR EVHVPETVSV ADLAHKMSIK ASEVIKVMMK
MGQMVTINQV LDQETAMIVV EELGHRAVAA KLDDPEALLV EGETTTDAEQ LPRPPVVTVM
GHVDHGKTSL LDHIRRAKVA AGEAGGITQH IGAYHVETPR GVITFLDTPG HEAFTAMRAR
GAKATDIVVL VVAADDGVMP QTKEAIAHAK AGGVPIVVAI NKIDKPEANP DRVKQELVAE
GVVPEEYGGD SPFVPVSAKT GVGIDDLLEN VLLQAEVLEL KAPIEAPAKG IVIEAKLDKG
KGPVATILVQ SGTLNRGDIV LAGTAYGRVR AMLDENGKPT KEAGPSIPVE IQGLSEVPGA
GEEVIVLPDE RKAREIALFR QGKFRDVKLA KQQAAKLESM LEQMGEGEVQ NLPLIIKADV
QGSQEALVQS LLKLSTAEVR VQIVHSAVGG ISENDVNLAT ASKAVIIGFN TRADAQARKL
AEANGIDIRY YNIIYDAVDE VKAAMSGMLA PEKREVITGM VEVRQVFKVP KIGTVAGCMV
TDGIVKRSSS VRVLRNNVVI FTGELESLKR FKDDVKEVKQ GFECGMSVKN FNDVIEGDQF
EVFEVTEVAR TL
//
