ID B9BMW2_9BURK Unreviewed; 969 AA.
AC B9BMW2;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 77.
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 ECO:0000313|EMBL:EEE07972.1};
GN ORFNames=BURMUCGD2_2187 {ECO:0000313|EMBL:EEE07972.1};
OS Burkholderia multivorans CGD2.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; Burkholderia cepacia complex.
OX NCBI_TaxID=513052 {ECO:0000313|EMBL:EEE07972.1, ECO:0000313|Proteomes:UP000004535};
RN [1] {ECO:0000313|EMBL:EEE07972.1, ECO:0000313|Proteomes:UP000004535}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGD2 {ECO:0000313|EMBL:EEE07972.1,
RC ECO:0000313|Proteomes:UP000004535};
RX PubMed=23105085; DOI=10.1128/JB.01306-12;
RA Varga J.J., Losada L., Zelazny A.M., Brinkac L., Harkins D., Radune D.,
RA Hostetler J., Sampaio E.P., Ronning C.M., Nierman W.C., Greenberg D.E.,
RA Holland S.M., Goldberg J.B.;
RT "Draft Genome Sequence Determination for Cystic Fibrosis and Chronic
RT Granulomatous Disease Burkholderia multivorans Isolates.";
RL J. Bacteriol. 194:6356-6357(2012).
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:EEE07972.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; ACFC01000003; EEE07972.1; -; Genomic_DNA.
DR RefSeq; WP_006404950.1; NZ_ACFC01000003.1.
DR AlphaFoldDB; B9BMW2; -.
DR GeneID; 66526358; -.
DR Proteomes; UP000004535; 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 469..638
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 49..85
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 100..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 472..620
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 210..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..352
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 478..485
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 524..528
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 578..581
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 969 AA; 103886 MW; 8A9E3F545F1551C4 CRC64;
MASNNVAQFA AELKMPAGVL LEQLQAAGVQ KASEDDALSE ADKARLLDHL RKSHGATDGD
KRKITLTRKH TSEIKQSDAT GKARTIQVEV RKKRTFVKRD DVSDVAEQGQ AQVAEADDDA
ELKRREEEAR REAALLEKQA QELRERQERL EREEAERRAR EEAAEAERRR AEEEAAAKRA
AAEAAAAQQA AQQAAAAQQA AAPADSAQDE ARAAAERAAQ REAAKKAEDA AREAAEKARA
EQEEIRKRRE AAEAEARAIR EMMNTPRKAV VKAVEPPKPA EPAKPAEAKG TLHKPAKPEG
AQARPAAKKP AAAPAATPAP AGAGDRNKKP GGGKGGWQDD AAKRRGIKTR GDSSGGVDRG
WRGGPKGRGR HQDNASSFQA PTEPIVREVH VPETISVADL AHKMAIKASE VIKVMMKMGQ
MVTINQVLDQ ETAMIVVEEL GHRALAAKLD DPEALLVEGE TGSDAEQLPR PPVVTVMGHV
DHGKTSLLDY IRRAKVAAGE AGGITQHIGA YHVETPRGVV TFLDTPGHEA FTAMRARGAK
ATDIVILVVA ADDGVMPQTK EAISHAKAGG VPIVVAINKI DKPEANPDRV KQELVAEGVV
PEEYGGDSPF VPVSAKTGAG IDDLLENVLL QAEVLELKAP VEAPAKGIVI EAKLDKGKGP
VATMLVQSGT LSRGDIVLAG SAYGRVRAML DENGKPTKEA GPSIPVEIQG LSEVPAAGEE
VIVLPDERKA REIALFRQGK FRDVKLAKQQ AAKLESMLEQ MGEGEVQNLP LIIKADVQGS
QEALVQSLLK LSTDEVRVQI VHSAVGGISE SDVNLATASK AVIIGFNTRA DAQARKLAEA
NGIDIRYYNI IYDAVDEVKA AMSGMLAPEK REVVTGMVEV RQVFKVPKVG TVAGCMVTDG
IVKRSSSVRV LRNNVVIFTG ELESLKRFKD DVKEVKQGFE CGMSVKNFND ILEGDQFEVF
EVTEVARTL
//
