IF2_BART1
ID IF2_BART1 Reviewed; 842 AA.
AC A9IMT5;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=BT_0239;
OS Bartonella tribocorum (strain CIP 105476 / IBS 506).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bartonellaceae; Bartonella.
OX NCBI_TaxID=382640;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 105476 / IBS 506;
RX PubMed=18037886; DOI=10.1038/ng.2007.38;
RA Saenz H.L., Engel P., Stoeckli M.C., Lanz C., Raddatz G.,
RA Vayssier-Taussat M., Birtles R., Schuster S.C., Dehio C.;
RT "Genomic analysis of Bartonella identifies type IV secretion systems as
RT host adaptability factors.";
RL Nat. Genet. 39:1469-1476(2007).
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; AM260525; CAK00715.1; -; Genomic_DNA.
DR RefSeq; WP_012230632.1; NC_010161.1.
DR AlphaFoldDB; A9IMT5; -.
DR SMR; A9IMT5; -.
DR STRING; 382640.BT_0239; -.
DR PRIDE; A9IMT5; -.
DR EnsemblBacteria; CAK00715; CAK00715; BT_0239.
DR KEGG; btr:BT_0239; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_2_5; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001592; Chromosome.
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..842
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000075593"
FT DOMAIN 340..509
FT /note="tr-type G"
FT REGION 42..91
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 139..253
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 349..356
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 374..378
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 395..398
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 449..452
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 485..487
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 42..59
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..83
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..221
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 349..356
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 395..399
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 449..452
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 842 AA; 93356 MW; 1321BF7CF2BB07A5 CRC64;
MSENNNDKTT GKKTLTLKRS VLETSTVKQN FSHGRTKAVV VETKRRKITR PDEKAEPLQP
ITKPHVAPQR SKPRFEEKKP QEAMAKSNLS SAEMEARLRA LEEAHIQEKI TREQAEKEAR
LAKEREEILK QEIQEQEILQ KQEEEKPTVP ISSVSSDPSL IEKTDIPIVP KNTTVIEKRK
IDENQEEERH SRRANPAKSE IRAPKIVKGA DERRRGKLTL NSALDEEGSA RGRSMAAMRR
RQEKFKRAQN QEPREKISRE VVLPETITIQ ELAQRMTERS VDVIKFLMKQ GQMMKPGDVI
DADVAELIAV EFGHTVKRVL ESDVEEGIFN ITDNPQNMQP RPPVVTIMGH VDHGKTSLLD
AIRKANVVSG EAGGITQHIG AYQVEQNGQK ITFIDTPGHA AFTAMRARGA RVTDIAVLVV
AADDSVMPQT IESINHAKAA GVPIIVAINK IDKPAANAQK VRTELLQHEV FVETMGGETL
DVEVSAKTGQ NLDKLLEAIL LQAEMLDLKA DPQRTAEGVV IEAKLDRGRG SVATVLVQKG
TLHPSDIIVA GNEWGRVRAL IDDHGRHVKE AVPSTPIEIL GMQGTPQAGD RFAVVTHEAK
AREISEYRQR LARDKAVARQ TGSRGSLEQM MTKLQTTGVK EFSLIIKGDV QGSIEAIASA
LEKLGNDEVR ARVVHSGAGG ITESDISLAE ASNSAVIGFN VRANKQARDF AKTQGIEIRY
YNIIYDLVDD IKAAMSGLLS PEQRETFLGN AEILEVFNIT KIGKVAGCRV TEGKIERGAG
VRLIRDNIVI HEGKLKTLKR FKDEVNEVQS GQECGIAFEN YEDMRAGDII ETFRIEHINR
TL
