IF2_COXBU
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 03-AUG-2022, entry version 113.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CBU_1432;
OS Coxiella burnetii (strain RSA 493 / Nine Mile phase I).
OC Bacteria; Proteobacteria; 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 OMA; NRDNRTG; -.
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; 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; 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
