ID B7J4D4_ACIF2 Unreviewed; 875 AA.
AC B7J4D4;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000256|HAMAP-Rule:MF_00100,
GN ECO:0000313|EMBL:ACK79700.1};
GN OrderedLocusNames=AFE_0391 {ECO:0000313|EMBL:ACK79700.1};
OS Acidithiobacillus ferrooxidans (strain ATCC 23270 / DSM 14882 / CIP 104768
OS / NCIMB 8455) (Ferrobacillus ferrooxidans (strain ATCC 23270)).
OC Bacteria; Pseudomonadota; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=243159 {ECO:0000313|EMBL:ACK79700.1, ECO:0000313|Proteomes:UP000001362};
RN [1] {ECO:0000313|EMBL:ACK79700.1, ECO:0000313|Proteomes:UP000001362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23270 / DSM 14882 / CIP 104768 / NCIMB 8455
RC {ECO:0000313|Proteomes:UP000001362};
RX PubMed=19077236; DOI=10.1186/1471-2164-9-597;
RA Valdes J., Pedroso I., Quatrini R., Dodson R.J., Tettelin H., Blake R.II.,
RA Eisen J.A., Holmes D.S.;
RT "Acidithiobacillus ferrooxidans metabolism: from genome sequence to
RT industrial applications.";
RL BMC Genomics 9:597-597(2008).
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:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000644}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000645}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000256|ARBA:ARBA00007733, ECO:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000644}.
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; CP001219; ACK79700.1; -; Genomic_DNA.
DR RefSeq; WP_012536117.1; NC_011761.1.
DR AlphaFoldDB; B7J4D4; -.
DR STRING; 243159.AFE_0391; -.
DR PaxDb; 243159-AFE_0391; -.
DR GeneID; 66431447; -.
DR KEGG; afr:AFE_0391; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_0_6; -.
DR Proteomes; UP000001362; 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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
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; IPR004161; EFTu-like_2.
DR InterPro; IPR013575; IF2_assoc_dom_bac.
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; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF08364; IF2_assoc; 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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00100};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00100}; Reference proteome {ECO:0000313|Proteomes:UP000001362}.
FT DOMAIN 375..544
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 180..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..526
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 233..279
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 384..391
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 430..434
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 484..487
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 875 AA; 92783 MW; 990192F347B4F751 CRC64;
MTVTVANFAA ELGVTNARLL EQLNAAGISK NTAEDVVTED DKHRLLASLR SAHGEGGGEP
RRITLNRTST TEIKQSVGAG KSRTVQVEVR RKRTYVKREA IAEEATESVI PEQLPADAQV
TTALLESAPV VEAVSAGGPA PVSEEPEPVE EVVGQPEQVP YDVAAASGEV AVVQEAPRSE
VKLAAAPSRT SERPAPDRGR TSTAGTDRAR PAAAPASRAP AAAPPPKGKK AGPAGRGGDD
DARRGGAARR GGRRSEDGGN ADALARRRKS ADKRNHGRGG PAVSEWAVAP VIREVALPET
ITVGELASRM AIKATDVIKT MMKMGVMATI NQVIDQETAA IVVEELGHKV KLVGITSPEA
FLTEDGAAET PVMGRRPPVV TVMGHVDHGK TSLLDRIRST QVASGEAGGI TQHIGAYHVE
TPKGMVTFLD TPGHEAFTAM RARGAQATDI VVLVVAADDG VMPQTIEAIH HAKAAKVPIV
VAVNKIDKPS VDPERIRQEL AGHDVVPEEW GGDTQFVNVS AKTGLHIDDL LDAILLQAEM
LDLDVQINGP AKGVVIESRL DRGRGVVASV LVRQGTLHTG DMLLAGAQFG RVRALVDDAG
RPAQSVAPGM PAEVLGLGDV PQAGDEVVVV ADERKAREVA LFRQGKFRDV RLAKSQKATL
ESLFEAAADG QLQQLNLLIK ADVQGSAEAL TTTLERLSTS EVKVNVIHSG VGGITESDVN
LAAASQAVII GFNVRAEAPA RRLIEHSGVD VRYHSIIYDA VDEVKAAMSG MLAPEIRERI
LGHAQVREIF RVPKVGMVAG CMVTDGLLRR SAKVRVIRQD VVIHSGEMDS LRRFKEDVKE
VREGFECGVG IRNFNDLKNG DVIEAFETTE VARTV
//
