ID L0M1H7_ENTBF Unreviewed; 895 AA.
AC L0M1H7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 65.
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 OrderedLocusNames=D782_0540 {ECO:0000313|EMBL:AGB76600.1};
OS Enterobacteriaceae bacterium (strain FGI 57).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae.
OX NCBI_TaxID=693444 {ECO:0000313|EMBL:AGB76600.1, ECO:0000313|Proteomes:UP000011002};
RN [1] {ECO:0000313|EMBL:AGB76600.1, ECO:0000313|Proteomes:UP000011002}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGI 57 {ECO:0000313|EMBL:AGB76600.1,
RC ECO:0000313|Proteomes:UP000011002};
RX PubMed=23469353; DOI=10.1128/genomeA.00238-12;
RA Aylward F.O., Tremmel D.M., Bruce D.C., Chain P., Chen A.,
RA Walston Davenport K., Detter C., Han C.S., Han J., Huntemann M.,
RA Ivanova N.N., Kyrpides N.C., Markowitz V., Mavrommatis K., Nolan M.,
RA Pagani I., Pati A., Pitluck S., Deshpande S., Goodwin L., Woyke T.,
RA Currie C.R.;
RT "Complete genome of Enterobacteriaceae bacterium strain FGI 57, a strain
RT associated with leaf-cutter ant fungus gardens.";
RL Genome Announc. 1:E00238-12(2013).
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}.
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DR EMBL; CP003938; AGB76600.1; -; Genomic_DNA.
DR AlphaFoldDB; L0M1H7; -.
DR STRING; 693444.D782_0540; -.
DR KEGG; ebf:D782_0540; -.
DR PATRIC; fig|693444.3.peg.527; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000011002; 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:UP000011002}.
FT DOMAIN 394..563
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 47..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 397..545
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 47..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..258
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 403..410
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 449..453
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 503..506
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 895 AA; 97564 MW; AC49EFD81FD9FFF3 CRC64;
MTDVTVKTLA AEIQTSVDRL VQQFADAGIP KSADDSVSAQ EKQTLLAHLN RENGSAPDKL
TLQRKTRSTL NIPGTGGKSK SVQIEVRKTR TFVKRDPQEA ERLAAEEQAQ REAEEQARRE
AEEAAKREAQ QKAEREAAEQ AKREAADKAK REAAEKDKVS NQQDDMTKTA QAEKARRESE
AAELKRKAEE EARRKLEEEA RRVAEEARRM AEENEKNGVN NTEPTEDTSD YHVTTSQHAR
QAEDENDREV EGGRGRGRNA KAARPAKKGN KHAESKADRE EARAAVRGGK GGKQRKGSAL
QQGFQKPAQA VNRDVVIGET ITVGELANKM AVKGSQVIKA MMKLGAMATI NQVIDQETAQ
LVAEEMGHKV ILRRENELEE AVMSDRDTGA AAEPRAPVVT IMGHVDHGKT SLLDYIRSTK
VASGEAGGIT QHIGAYHVQT DNGMITFLDT PGHAAFTSMR ARGAQATDIV VLVVAADDGV
MPQTIEAIQH AKAAQVPLVV AVNKIDKPEA DLDRVKNELS QYGVMPEEWG GEAQFIPVSA
KAGTGIDDLL NAILLQAEVL ELKAVRKGMA SGAVIESFLD KGRGPVATVL VREGTLHKGD
IVLCGFEYGR VRAMRNELGQ EVLEAGPSIP VEILGLSGVP AAGDEVTVVR DEKKAREVAL
YRQGKFREVK LARQQKSKLE NMFANMTEGE VHEVNVVLKA DVQGSVEAIS DSLLKLSTDE
VKVKIIGSGV GGITETDATL AAASNAILVG FNVRADASAR RVIEAESLDL RYYSVIYNLI
DEVKAAMSGM LSPELKQQII GLAEVRDVFK SPKFGAIAGC MVTEGIIKRH NPIRVLRDNV
VIYEGELESL RRFKDDVNEV RNGMECGIGV KNYNDVRVGD MIEVFEIIEI QRTIA
//
