ID   IF2_BRUA2               Reviewed;         959 AA.
AC   Q2YQR7;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   07-FEB-2006, sequence version 1.
DT   27-MAR-2024, entry version 103.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN   OrderedLocusNames=BAB1_2165;
OS   Brucella abortus (strain 2308).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=359391;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2308;
RX   PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA   Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA   Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT   "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL   Infect. Immun. 73:8353-8361(2005).
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; AM040264; CAJ12121.1; -; Genomic_DNA.
DR   RefSeq; WP_002965227.1; NZ_KN046823.1.
DR   AlphaFoldDB; Q2YQR7; -.
DR   SMR; Q2YQR7; -.
DR   STRING; 359391.BAB1_2165; -.
DR   GeneID; 3788765; -.
DR   KEGG; bmf:BAB1_2165; -.
DR   PATRIC; fig|359391.11.peg.1402; -.
DR   HOGENOM; CLU_006301_10_0_5; -.
DR   PhylomeDB; Q2YQR7; -.
DR   Proteomes; UP000002719; Chromosome I.
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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
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   CDD; cd22265; UDM1_RNF168; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR004161; EFTu-like_2.
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; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF11987; IF-2; 1.
DR   Pfam; PF08364; IF2_assoc; 1.
DR   Pfam; PF04760; IF2_N; 1.
DR   SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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; GTP-binding; Initiation factor; Nucleotide-binding;
KW   Protein biosynthesis; Reference proteome.
FT   CHAIN           1..959
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000228176"
FT   DOMAIN          457..626
FT                   /note="tr-type G"
FT   REGION          1..374
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          466..473
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          491..495
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          512..515
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          566..569
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          602..604
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        12..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..63
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        154..243
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        296..312
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        322..374
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         466..473
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         512..516
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         566..569
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   959 AA;  104141 MW;  68B272FD63479FEE CRC64;
     MSDKTNDDKT LSVNPKKTLT LKRPGVEQST VRQNFSHGRT KAVVVETKKR KFSRPDEKPE
     VEAAAAPKPA APAAAPQQAP ASAPVSASAA QASAPQPAPV KAPATKAPAA PSAPVTKPHV
     AQQRPVHQRP GGQQAQRPRP ADRSGMVLNT LSRSEMDARR RALEEAQIRE VEERARAVEE
     AKRRAEEDAR RAKEREESAR RQAEEEARLK AEAEARRKAE EEAAKRMPQP EARSERRDDA
     RPAPYGARPQ QAGRPQGGRP QPAGRPQQGS PRPAPIIADA APIAGKPLPQ SQLRKPGQSD
     DDDDRRSGAA RRGVAAKPEV RAPKVVKGED DRRRGKLTLT SNLEEEGRSR SLSAMRRRQE
     KFKRSQMQET REKISREVTI PETITLQELA QRMAERSVDI IKYLMKQGQM MKPGDVIDAD
     TAQLIAEEFG HTVKRVAESD VEEGIFDVAD NESAMVSRPP VVTIMGHVDH GKTSLLDAIR
     HANVVSGEAG GITQHIGAYQ VVQNGQKITF IDTPGHAAFT AMRARGAQAT DIAILVVAAD
     DSVMPQTIES INHAKAAGVP IIVAINKIDK PAADPQKVRT ALLQHEVFVE SMGGEVLDVE
     VSAKNKINLD KLLDAVLLQA EMLDLKADPD RTAEGVVIEA QLDRGRGSVA TVLIQKGTLH
     PGDILVAGSE WGRVRALVND RGEHVKEAGP AMPVEILGLQ GTPQAGDRFA VVANEAKARE
     IAEYRQRLAR DKAVARQSGA RGSLEQMMNQ LQVSGTKEFP LVIKGDVQGS IEAITNALDK
     LGTDEVRARI VHSGAGGITE SDVSLAEASN AAIIGFNVRA NKQARDSAEQ QGIEIRYYNI
     IYDLIDDVKA AMSGLLSPER RETFLGNAEI LEVFNITKVG KVAGCRVTEG KVERGAGVRL
     IRDNVVIHEG KLKTLKRFKD EVAEVPSGQE CGMAFENYDD IRAGDVIEAF RVEHVSRTL
//