ID IF2_COXBN Reviewed; 803 AA.
AC A9KBM1;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 94.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CBUD_0563;
OS Coxiella burnetii (strain Dugway 5J108-111).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC Coxiella.
OX NCBI_TaxID=434922;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Dugway 5J108-111;
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 -!- SEQUENCE CAUTION:
CC Sequence=ABS76663.2; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000733; ABS76663.2; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_043880842.1; NC_009727.1.
DR AlphaFoldDB; A9KBM1; -.
DR SMR; A9KBM1; -.
DR KEGG; cbd:CBUD_0563; -.
DR HOGENOM; CLU_006301_6_1_6; -.
DR Proteomes; UP000008555; 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; 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; 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; 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; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..803
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000075601"
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..178
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 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; 88538 MW; BAA248030B3E5C2E CRC64;
MADMSVKQLA DLVRTTPERL LEQLKEAGVA ITHVDQTISD EEKRKLLLHL KTSHSTETDK
KRSKIVLKRK KLSVVKSGKK SVNVEIRSKR TYTKPVVEQK RETEPAPTQE VPLTSDTTNL
NEKAEVNVAT LEKAVEAEVK EEAKKTPSEK KETPKKGPRK ETRRSRKPDK EDKWEREELH
MTKLVEERRR RHKPAHMPDS DNASAKLEQG FARPTAPVVR EVALPESITV ADLAQKMSVK
AAEVIKAMMK LGAMVTINQR IDQETAAIVV EEMGHKPKLI KEDVLEENLV ATLGEQTGEA
VPRAPVVTIM GHVDHGKTSL LDYIRRTKVT STEAGGITQH IGAYHVETEL GMITFLDTPG
HEAFTAMRAR GAKCTDIVVL VVAADDGIMP 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 YEGLLESLRR YKEDVAEVRQ GTECGIGVKN
YNDVKVGDQI EVYEKTQVHR TIA
//
