ID A0A0W8JJK3_9VIBR Unreviewed; 900 AA.
AC A0A0W8JJK3;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=VRK_05340 {ECO:0000313|EMBL:KUJ00403.1};
OS Vibrio sp. MEBiC08052.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1761910 {ECO:0000313|EMBL:KUJ00403.1, ECO:0000313|Proteomes:UP000054473};
RN [1] {ECO:0000313|EMBL:KUJ00403.1, ECO:0000313|Proteomes:UP000054473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MEBiC08052 {ECO:0000313|EMBL:KUJ00403.1,
RC ECO:0000313|Proteomes:UP000054473};
RA Kim Y.J., Lee J.-H., Kwon K.K.;
RT "Genome sequence of Vibrio sp. MEBiC08052.";
RL Submitted (DEC-2015) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KUJ00403.1}.
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DR EMBL; LQIY01000003; KUJ00403.1; -; Genomic_DNA.
DR RefSeq; WP_059119961.1; NZ_KQ947475.1.
DR AlphaFoldDB; A0A0W8JJK3; -.
DR STRING; 1761910.VRK_05340; -.
DR PATRIC; fig|1761910.3.peg.536; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000054473; Unassembled WGS sequence.
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:0016779; F:nucleotidyltransferase activity; IEA:UniProtKB-KW.
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; TRANSLATION INITIATION FACTOR IF-2, MITOCHONDRIAL; 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}; Nucleotidyltransferase {ECO:0000313|EMBL:KUJ00403.1};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00100}; Transferase {ECO:0000313|EMBL:KUJ00403.1}.
FT DOMAIN 399..568
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 48..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..312
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..550
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 48..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 68..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..312
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 408..415
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 454..458
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 508..511
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 900 AA; 99179 MW; 5866967F6C2FF094 CRC64;
MTELTVKALS EEIGTPVDRL LEQLADAGMT KTGSDSVSEN EKQKLLTFLR KEHGGSSSKD
EPTRLTLQRK TRSTLSVNAG GGKSKNVQVE VRKKRTYVKR SAIEDEAKRQ AEEAALREAE
EKAKLEAEKA RLEAQAKREA EEKAKREVEE QMKREAEEKA KREEKSSQKV ELSDEEKSKQ
EAARQEAEAL MRRQEEELRR KAEEESQRQL EKARELAEKN QERWSAAEEN KGAMEDEYTD
YHLTTSRYAQ EAEDEADRRD EGSRRAKAKK RASARDEQRQ ERDMRPRGGK GGRNSNRGRG
KPSSMQQGFD KNATVAKSDV VIGETIIVSE LAQKMSVKGT EVIKVMMKMG AMATINQVID
QETAQLVAEE MGHKVILRKE NELEEAVLSD RDSTSEAVPR APVVTIMGHV DHGKTSTLDY
IRRTHVASGE AGGITQHIGA YHVETDNGMI TFLDTPGHAA FTAMRARGAQ ATDIVVLVVA
ADDGVMPQTI EAIQHSKAAK VPLIVAVNKI DKEEANPDNV KNELAQYDII PEEWGGENMF
VHISAKQGTN VDALLEAILL QAEVLELTAV ADGMGSGVVV ESRLDKGRGP VATILVQSGT
LRKGDILLCG QEYGRVRAMR DEVGDEVLEA GPSIPVEVLG LSGVPAAGDE ATVVRDERKA
REVANYRQGK FREVKLARQQ KAKLENMFSN MTAGEVAELN IVLKADVQGS VEAITDALVK
LSTDEVKVNI VGSGVGGITE TDATLAAASN AIVLGFNVRA DASARRTIEA ENLDLRYYSI
IYQLIDEVKQ AMSGMLAPEF KQEIIGLAEV RDVFRSPKLG AIAGCMVTEG LIKRNNPIRV
LRDNVVIYEG ELESLRRFKD DVAEVKSGYE CGVGVKNYND VRVGDQIEVF ETVEIKRSID
//