ID A0A126ZGN6_9BURK Unreviewed; 974 AA.
AC A0A126ZGN6;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 39.
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=AX767_19520 {ECO:0000313|EMBL:AMM26298.1};
OS Variovorax sp. PAMC 28711.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Variovorax.
OX NCBI_TaxID=1795631 {ECO:0000313|EMBL:AMM26298.1, ECO:0000313|Proteomes:UP000070169};
RN [1] {ECO:0000313|EMBL:AMM26298.1, ECO:0000313|Proteomes:UP000070169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PAMC 28711 {ECO:0000313|EMBL:AMM26298.1,
RC ECO:0000313|Proteomes:UP000070169};
RA Park H.;
RT "Complete genome of Variovorax sp.";
RL Submitted (FEB-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 -!- 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; CP014517; AMM26298.1; -; Genomic_DNA.
DR RefSeq; WP_068632837.1; NZ_CP014517.1.
DR AlphaFoldDB; A0A126ZGN6; -.
DR STRING; 1795631.AX767_19520; -.
DR KEGG; vaa:AX767_19520; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000070169; 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; 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; 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; 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.
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:UP000070169}.
FT DOMAIN 474..641
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 95..136
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 152..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 275..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 477..625
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 152..187
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 483..490
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 529..533
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 583..586
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 974 AA; 104221 MW; 5A95B4EAB4472805 CRC64;
MSSTTVAEFA NELKKTPETL LDQLKSAGVA KAAPTDALTE ADKQRLLGFL KASHGTAEPE
RKKITLTKKS TSEIKQADAM GRARTIQVEV RKKRTFIQRD DGPGTTPEPE AAPAAAAVEP
AAPKIDEAEL GRREEEARRQ AELIRRQEEE LVEKRRQREE TEAREREKAD RDEQAEVAER
EAKAAQTAKE RASATAAVVG RRAPGFDAPA PAEPDAAVSK AAADAAAATQ AKEDAKAKAA
AESKARADEE SARAKDLDER RRKALAEAEA IRAMMNAPAR VLVPHKAPEK EVPKPAVKGT
LHKPATPAPR VGAPAAPGST APGASKDVKS AKLSSSWAGD PAKKKEIKTR GDASGGVGRG
NWRGGPRGRR GSNDRGGHDE HVQAAPVEAR VLDVHVPETI TVAELAHKMA VKAQEVIKQL
MKSGIMATMN QSLDQDTAMV IVEDMGHNAM VAALDDPEAF TDDDVAGLTA ESLPRAPVVT
VMGHVDHGKT SLLDYIRRAK VASGEAGGIT QHIGAYHVET ARGMVSFLDT PGHEAFTAMR
ARGAQATDIV ILVVAADDGV MPQTKEAIKH AKAAGVPIVV AINKIDKQDA NLDRVKQELV
AEEVVPEEYG GEVPFVSVSA KTGQGVDDLL EQVLLQAEVL ELRAPVDAAA KGLVIEARLD
KGRGPVATVL VQSGTLKAGD VVLAGSTYGR VRAMLDEDGK TIKTAGPSIP VEIQGLTEVP
QAGDEFMVMA DERRAREIAT YRAGKFRNTK LAKLQASNLQ NMFTDLSAGE VQTLRLIIKA
DVQGSQEALA QSLLKLATEE VKVQIVYAGV GGISENDINL AIASKAVVIG FNVRADSGAR
KLAEGNGVQL NYYSIIYDAV DEIKVAMSGM LAPERREEII GQAEIRTVFV ASKIGTVAGS
YITSGSVNRS AHFRLLRDNV VVYTGEVDSI KRMKDDVREV KEGFECGIKL KNYNDIKEGD
QLEFFEIKEI ARTL
//
