IF2_BACCR
ID IF2_BACCR Reviewed; 686 AA.
AC Q812X7;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=BC_3811;
OS Bacillus cereus (strain ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC
OS 15305 / NCIMB 9373 / NCTC 2599 / NRRL B-3711).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=226900;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14579 / DSM 31 / CCUG 7414 / JCM 2152 / NBRC 15305 / NCIMB 9373
RC / NCTC 2599 / NRRL B-3711;
RX PubMed=12721630; DOI=10.1038/nature01582;
RA Ivanova N., Sorokin A., Anderson I., Galleron N., Candelon B., Kapatral V.,
RA Bhattacharyya A., Reznik G., Mikhailova N., Lapidus A., Chu L., Mazur M.,
RA Goltsman E., Larsen N., D'Souza M., Walunas T., Grechkin Y., Pusch G.,
RA Haselkorn R., Fonstein M., Ehrlich S.D., Overbeek R., Kyrpides N.C.;
RT "Genome sequence of Bacillus cereus and comparative analysis with Bacillus
RT anthracis.";
RL Nature 423:87-91(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; AE016877; AAP10734.1; -; Genomic_DNA.
DR RefSeq; NP_833533.1; NC_004722.1.
DR RefSeq; WP_000036343.1; NZ_CP034551.1.
DR AlphaFoldDB; Q812X7; -.
DR SMR; Q812X7; -.
DR STRING; 226900.BC_3811; -.
DR EnsemblBacteria; AAP10734; AAP10734; BC_3811.
DR GeneID; 67508447; -.
DR KEGG; bce:BC3811; -.
DR PATRIC; fig|226900.8.peg.3928; -.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000001417; 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; 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; 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..686
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137168"
FT DOMAIN 188..357
FT /note="tr-type G"
FT REGION 53..98
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..204
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 222..226
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 243..246
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 297..300
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 333..335
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 53..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 197..204
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 243..247
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 297..300
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 686 AA; 75752 MW; B0C622F2B3215640 CRC64;
MSKIRVHEYA KKHNISSKDL MTKLKEMNIE VSNHMTMLDD EVVNKLDNEY QTEKPSVADE
FEVEEKVVRS KKNSNKKKKK GKGNEDKRQE NFAGRQQTQI VETPDKITFS GSLTVGDLAK
KLSKEPSEII KKLFMLGIMA TINQDLDKDT IELIANDYGI EVEEEVIVSE TEFETFIDEQ
DDEENLKERP AVVTIMGHVD HGKTTLLDSI RNSKVTAGEA GGITQHIGAY QVEVNDKKIT
FLDTPGHAAF TTMRARGAQV TDITILVVAA DDGVMPQTVE AINHAKAAGV PIIVAVNKMD
KPAANPDRVM QELTEYELVP EAWGGDTIFV PISAIQGEGI DNLLEMILLV SEVEEYKANP
NRYATGTVIE AQLDKGKGTI ATLLVQNGTL RVGDPIVVGT SFGRVRAMVS DIGRRVKVAG
PSTPVEITGL NEVPQAGDRF MAFADEKKAR QIGESRAQEA LVAQRGEKSK LSLEDLFQQI
QEGDVKEINL IVKADVQGSV EAMAASLRKI DVEGVKVKII HTGVGAITES DIILASASNA
IVIGFNVRPD VNAKRTAELE NVDIRLHRII YKVIEEIEAA MQGMLDPEFE EKVIGQAEVR
QTFKVTKVGT IAGCYVTDGK ITRDSGVRII RDGVVIFEGQ LDTLKRFKDD VKEVAQNYEC
GITIERYNDL KEGDIIEAYI MEEVKR
