ID A0A1J0VG73_9GAMM Unreviewed; 840 AA.
AC A0A1J0VG73;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=BOX17_08655 {ECO:0000313|EMBL:APE31015.1};
OS Halomonas aestuarii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1897729 {ECO:0000313|EMBL:APE31015.1, ECO:0000313|Proteomes:UP000181985};
RN [1] {ECO:0000313|Proteomes:UP000181985}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hb3 {ECO:0000313|Proteomes:UP000181985};
RA Koh H.-W., Rani S., Park S.-J.;
RT "Halolamina sediminis sp. nov., an extremely halophilic archaeon isolated
RT from solar salt.";
RL Submitted (NOV-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|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; CP018139; APE31015.1; -; Genomic_DNA.
DR RefSeq; WP_071943660.1; NZ_CP018139.1.
DR AlphaFoldDB; A0A1J0VG73; -.
DR KEGG; hsi:BOX17_08655; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000181985; 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}.
FT DOMAIN 340..509
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 48..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 343..491
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 73..109
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 183..226
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 349..356
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 395..399
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 449..452
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 840 AA; 90792 MW; C6CE15213F040E4C CRC64;
MSEMTVKDFA AKVGRDVPRL LEQMKEAGLG QKAENDAVSE EDKRQLLDYL TKSHGGSGGA
GAKNRITLTR KTRSRIKTGE RGKSIEVQVR KKRTYVKRAE EETAKSEPEA DAGPRQLVGD
MADSQQAQAD KDAREAEEAK ARAAEESARE AAAKLEAEKA VSEPEIPVPE LETQPAPEEP
PAPPKEGRPE PRRAAVKKAS GKGGKKGRDD RDDDRGDREE RRRGGKKVKR AERRGGRRGG
GAQGGGKHGF QKPTQPIVRE VSIPESISVA DLADKMSIKA NEVIKAMFTM GAAVTINQTI
DQDTAAIVVE EMGHKPKLVK DDALETEVLE GISYEGEEIT RSPVVTVMGH VDHGKTSLLD
YIRKAKVATG EAGGITQHIG AYHVEDDHGG VTFLDTPGHA AFTAMRARGA KATDVVVLVV
AADDGVMPQT IEAIEHSKAA EVPMVVAVNK IDKPGADPDR VKNELSQHGV ISEEWGGDTQ
FVHVSAHTGE GIEELLESIQ LVSEVLELKA VPEAPGKGVV VESRLDKGRG PVATVLVQNG
TLKKGDIVLA GLHYGRVRAL TNELGKQVDE AGPSTPVEIQ GLDGTPEAGD DFMVLADEKK
AREVANFRQG KYREVRLARQ QKAKLENMFS QMGQDVAAKL NIVLKADVQG SLEAIKGALE
ELSTDEVEVA VVSSGVGGIT GTDANLALAS DAIVVGFNVR ADAAAREIIE REGLDLRYYS
VIYQLVDEVK QAMSGMLAPE WKEEIVGVAE VRDVFRAPKI GAVAGCMVVE GTVHRNKKIR
VLRDNVVIYE GELESLRRYK DDVQEVRNGM ECGIGVKNYN DVQVGDKIEV FDQVKVERTL
//
