IF2_BRUME
ID IF2_BRUME Reviewed; 959 AA.
AC Q8YEB3;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 2.
DT 03-AUG-2022, entry version 125.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=BMEI1965;
OS Brucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=224914;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=16M / ATCC 23456 / NCTC 10094;
RX PubMed=11756688; DOI=10.1073/pnas.221575398;
RA DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA Haselkorn R., Kyrpides N.C., Overbeek R.;
RT "The genome sequence of the facultative intracellular pathogen Brucella
RT melitensis.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL53146.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AE008917; AAL53146.1; ALT_INIT; Genomic_DNA.
DR PIR; AG3497; AG3497.
DR RefSeq; WP_004684582.1; NZ_GG703778.1.
DR AlphaFoldDB; Q8YEB3; -.
DR SMR; Q8YEB3; -.
DR STRING; 224914.BMEI1965; -.
DR EnsemblBacteria; AAL53146; AAL53146; BMEI1965.
DR GeneID; 29594849; -.
DR KEGG; bme:BMEI1965; -.
DR PATRIC; fig|224914.52.peg.1610; -.
DR eggNOG; COG0532; Bacteria.
DR OMA; QVRPEMI; -.
DR PhylomeDB; Q8YEB3; -.
DR Proteomes; UP000000419; 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: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; 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; 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..959
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137178"
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; 104122 MW; 6B155B2F62779DDC CRC64;
MSDKTNDDKT LSVNPKKTLT LKRPGVEQST VRQNFSHGRT KAVVVETKKR KFSRPDEKPE
VEAAAAPKPA APAAAPQQAP ASAPVSASAA QASAPQPAPV KAPATKAPAA PSAPVTKPHV
AQQRPVHQRP GGQQAQRPRP ADRSGMVLNT LSRSEMDARR RALEEAQIRE VEERARAVEE
AKRRAEEDAR RAKEHEESAR 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
