ID   IF2_COXBU               Reviewed;         803 AA.
AC   Q83BS1;
DT   15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 118.
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=CBU_1432;
OS   Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Legionellales; Coxiellaceae;
OC   Coxiella.
OX   NCBI_TaxID=227377;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RSA 493 / Nine Mile phase I;
RX   PubMed=12704232; DOI=10.1073/pnas.0931379100;
RA   Seshadri R., Paulsen I.T., Eisen J.A., Read T.D., Nelson K.E., Nelson W.C.,
RA   Ward N.L., Tettelin H., Davidsen T.M., Beanan M.J., DeBoy R.T.,
RA   Daugherty S.C., Brinkac L.M., Madupu R., Dodson R.J., Khouri H.M.,
RA   Lee K.H., Carty H.A., Scanlan D., Heinzen R.A., Thompson H.A., Samuel J.E.,
RA   Fraser C.M., Heidelberg J.F.;
RT   "Complete genome sequence of the Q-fever pathogen, Coxiella burnetii.";
RL   Proc. Natl. Acad. Sci. U.S.A. 100:5455-5460(2003).
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; AE016828; AAO90929.1; -; Genomic_DNA.
DR   RefSeq; NP_820415.1; NC_002971.3.
DR   RefSeq; WP_010958223.1; NC_002971.4.
DR   AlphaFoldDB; Q83BS1; -.
DR   SMR; Q83BS1; -.
DR   STRING; 227377.CBU_1432; -.
DR   EnsemblBacteria; AAO90929; AAO90929; CBU_1432.
DR   GeneID; 1209338; -.
DR   KEGG; cbu:CBU_1432; -.
DR   PATRIC; fig|227377.7.peg.1431; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_6_0_6; -.
DR   OrthoDB; 9811804at2; -.
DR   Proteomes; UP000002671; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR   GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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; Reference proteome.
FT   CHAIN           1..803
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000137198"
FT   DOMAIN          302..471
FT                   /note="tr-type G"
FT   REGION          93..123
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          138..206
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..123
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;  88486 MW;  00C73115E6B3D5C9 CRC64;
     MADMSVKQLA DLVRTTPERL LEQLKEAGVA ITHVDQTISD EEKRKLLLHL KTSHSTETDK
     KRSKIVLKRK KLSVVKSGKK SVNVEIRSKR TYTKPVVEQK RETEPAPTQE VPPTSDTTNL
     NEKAEVNVAT LEKAVEAEVK EEAKKTPSEK KETPKKGPRK ETRRSRKPDK EDKWEREELH
     MTKLVEERRR RHKPAHMPDS DSASAKLEQG FARPTAPVVR EVALPESITV ADLAQKMSVK
     AAEVIKAMMK LGAMVTINQR IDQETAAIVV EEMGHKPKLI KEDVLEENLV ATLGEQTGEA
     VPRAPVVTIM GHVDHGKTSL LDYIRRTKVT STEAGGITQH IGAYHVETEL GMITFLDTPG
     HEAFTAMRAR GAKCTDIVVL VVAADDGVMP QTVEAIQHAR AAKVPVVVAV NKIDKPEADP
     ERIKTELSTH DVLPEEWGGD TMFQPISAKT GEGIDALLER ILLQAEVLEL KAVDNGPARG
     MVVESRLDRG RGPVATVLVT SGELHLGDIL LVGREYGRVR AMIGDDGRPC ESAGPSMPVE
     VLGLSGTSVA 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
//