IF2_COXB2
ID IF2_COXB2 Reviewed; 803 AA.
AC B6IZ61;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-DEC-2008, sequence version 1.
DT 03-AUG-2022, entry version 81.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CbuG_0577;
OS Coxiella burnetii (strain CbuG_Q212) (Coxiella burnetii (strain Q212)).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=434923;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CbuG_Q212;
RX PubMed=19047403; DOI=10.1128/iai.01141-08;
RA Beare P.A., Unsworth N., Andoh M., Voth D.E., Omsland A., Gilk S.D.,
RA Williams K.P., Sobral B.W., Kupko J.J. III, Porcella S.F., Samuel J.E.,
RA Heinzen R.A.;
RT "Comparative genomics reveal extensive transposon-mediated genomic
RT plasticity and diversity among potential effector proteins within the genus
RT Coxiella.";
RL Infect. Immun. 77:642-656(2009).
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 ---------------------------------------------------------------------------
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; CP001019; ACJ17989.1; -; Genomic_DNA.
DR RefSeq; WP_012569826.1; NC_011527.1.
DR AlphaFoldDB; B6IZ61; -.
DR SMR; B6IZ61; -.
DR KEGG; cbg:CbuG_0577; -.
DR HOGENOM; CLU_006301_6_1_6; -.
DR OMA; NRDNRTG; -.
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; IPR009061; DNA-bd_dom_put_sf.
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; PF04760; IF2_N; 2.
DR SUPFAM; SSF46955; SSF46955; 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..803
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093779"
FT DOMAIN 302..471
FT /note="tr-type G"
FT REGION 95..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..209
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..318
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 336..340
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 357..360
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 411..414
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 447..449
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 108..125
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 138..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 311..318
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 357..361
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 411..414
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 803 AA; 88492 MW; 48A75053C989D444 CRC64;
MADMSVKQLA DLVRTTPERL LEQLKEAGVA ITHVDQTISD EEKRKLLLHL KTSHSTETDK
KRSKIVLKRK KLSVVKSGKK SVNVEIRSKR TYTKPVVEQK RETEPAPTQE VPLTSDTTNL
NEKAEVNVAT LEKAVEAEVK EEAKKTPSEK KETPKKGPRK ETRRSRKPDK EDKWEREELH
MTKLVEERRR RHKPAHVPDS DSASAKLEQG FARPTAPVVR EVALPESITV ADLAQKMSVK
AAEVIKAMMK LGAMVTINQR IDQETAAIVV EEMGHKPKLI KEDVLEENLV ATLGEQIGEA
VPRAPVVTIM GHVDHGKTSL LDYIRRTKVT STEAGGITQH IGAYHVETEL GMITFLDTPG
HEAFTAMRAR GAKCTDIVVL VVAADDGVMP QTVEAIQHAR AAKVPVVVAV NKIDKPEADP
ERIKTELSTH DVLPEEWGGD TMFQPISAKT GEGIDALLER ILLQAEVLEL KAVDNGPARG
MVVESRLDRG RGPVATVLVT SGELHLGDIL LVGREYGRVR AMIGDDGRPC ESAGPSMPVE
VLGLSGTPVA GEEAIVVPDE RKAREIARFR QGKYREVRLA KKQTAHLERI FDRMGEGKQN
TLNIVLKADV QGSLEALTEA LNKLSTDEVK VNIIASGVGG ITESDVNLAI ASDAVVIGFN
VRADAPTRVL VEREGVDLRY YSIIYDLIDE VKKALSGLLA PEFEEKIVGL AEVRDVFRSS
KIGAIAGCMV VEGVVRRHLP IRVLRDNVVI YEGQLESLRR YKEDVAEVRQ GTECGIGVKN
YNDVKVGDQI EVYEKTQVHR TIA
