ID A0A1B1Z4A7_9BACI Unreviewed; 764 AA.
AC A0A1B1Z4A7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 35.
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 ORFNames=ABE41_009920 {ECO:0000313|EMBL:ANX12327.1};
OS Fictibacillus arsenicus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Fictibacillus.
OX NCBI_TaxID=255247 {ECO:0000313|EMBL:ANX12327.1, ECO:0000313|Proteomes:UP000077412};
RN [1] {ECO:0000313|EMBL:ANX12327.1, ECO:0000313|Proteomes:UP000077412}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=G25-54 {ECO:0000313|EMBL:ANX12327.1,
RC ECO:0000313|Proteomes:UP000077412};
RA Zheng Z.;
RT "Complete genome sequence of Fictibacillus arsenicus G25-54, a strain with
RT toxicity to nematodes and a potential arsenic-resistance activity.";
RL Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
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|ARBA:ARBA00025162, ECO:0000256|HAMAP-
CC Rule:MF_00100, 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; CP016761; ANX12327.1; -; Genomic_DNA.
DR RefSeq; WP_066289533.1; NZ_CP016761.1.
DR AlphaFoldDB; A0A1B1Z4A7; -.
DR STRING; 255247.ABE41_009920; -.
DR KEGG; far:ABE41_009920; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000077412; 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: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; 1.10.10.2480; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; IPR004161; EFTu-like_2.
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; 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; 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:UP000077412}.
FT DOMAIN 265..434
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 49..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 268..416
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 57..75
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 76..105
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..183
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 274..281
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 320..324
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 374..377
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 764 AA; 83928 MW; 623BD9D6355FADCD CRC64;
MSKIRVYEYA KQKNVQSKDI IEKLKTMDVH VANHMSMIDQ AALTKLDEAY NSKAQKDQPA
KPKNQNQLPK TDKNRNNSGN DTKSNKKEVQ KESNMKIKKE TDNRNSSQSK SPQTQGAKPG
NSNSQNAAKN NNSKNSNNRN QNNNNRNNNN RNNNNKNQNR NKQNRGGGSQ QQAPQKKVLE
TPSKITFTDT LQVGELAKKL NKDTSEIIKK LMGLGIMATI NQELDKEAIE LIAADYDVEV
EEEIIVDETE FENYEVVDDE KDMQVRPPVV TIMGHVDHGK TTLLDAIRNT KVTAGEAGGI
TQHIGAYQIT NNGKQITFLD TPGHAAFTTM RARGAQVTDI TILVVAADDG VMPQTVEAIN
HAKAAEVPII VAVNKMDKEA ANPDRVMQEL TEHGLVSEAW GGDTIFVNVS AIKGDGIDDL
LEMINLVSEV EELKANPNRT AAGTVIEAQL DKGRGSVATL LVQSGTLNVG DPIVVGHTYG
RVRAMVNDLG RRVKSVGPST PVEITGLNDV PQAGDPFMVF ADEKKARQVG ESRFKKQQDA
QRKESSKLNL DDLFNQIKEG EIKDINVIIK GDVQGSVEAL AGSLQKIDVE GVKVKIIHSG
VGAINEYDIM LASASNAIVI GFNVRPDAGA KRTADAEKVD VRLHRIIYNV IEEIESAMKG
MLDPEFEEKV IGQVEVRTTF KVSKVGTIAG CYVTEGKITR DSTVRLIRDG VVSYEGKIDA
LKRFKDDAKE VSAGYECGIT LEKFNDIKEG DIIEAYIMEE IKVK
//
