IF2_WOLSU
ID IF2_WOLSU Reviewed; 939 AA.
AC Q7M7X5;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=WS2016;
OS Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / LMG 7466 / NCTC
OS 11488 / FDC 602W) (Vibrio succinogenes).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Wolinella.
OX NCBI_TaxID=273121;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC
RC 11488 / FDC 602W;
RX PubMed=14500908; DOI=10.1073/pnas.1932838100;
RA Baar C., Eppinger M., Raddatz G., Simon J., Lanz C., Klimmek O.,
RA Nandakumar R., Gross R., Rosinus A., Keller H., Jagtap P., Linke B.,
RA Meyer F., Lederer H., Schuster S.C.;
RT "Complete genome sequence and analysis of Wolinella succinogenes.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:11690-11695(2003).
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:0000255|HAMAP-Rule:MF_00100}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|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:0000255|HAMAP-Rule:MF_00100}.
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DR EMBL; BX571662; CAE11018.1; -; Genomic_DNA.
DR RefSeq; WP_011139800.1; NC_005090.1.
DR AlphaFoldDB; Q7M7X5; -.
DR SMR; Q7M7X5; -.
DR STRING; 273121.WS2016; -.
DR EnsemblBacteria; CAE11018; CAE11018; WS2016.
DR KEGG; wsu:WS2016; -.
DR eggNOG; COG0532; Bacteria.
DR eggNOG; COG0810; Bacteria.
DR HOGENOM; CLU_006301_4_1_7; -.
DR OMA; VIFAMNK; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000422; 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; cd03702; IF2_mtIF2_II; 1.
DR Gene3D; 3.40.50.10050; -; 1.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
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 PANTHER; PTHR43381; PTHR43381; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 2.
DR SUPFAM; SSF50447; SSF50447; 2.
DR SUPFAM; SSF52156; SSF52156; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR00487; IF-2; 1.
DR TIGRFAMs; TIGR00231; small_GTP; 1.
DR PROSITE; PS51722; G_TR_2; 1.
DR PROSITE; PS01176; IF2; 1.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..939
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137284"
FT DOMAIN 438..607
FT /note="tr-type G"
FT REGION 57..274
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 447..454
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 472..476
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 493..496
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 547..550
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 583..585
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 73..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..225
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 447..454
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 493..497
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 547..550
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 939 AA; 102671 MW; B3D7BD9FB5CE3BC0 CRC64;
MQKVRVHEIA LELGIKSKEI IDKAKDLDLD LKTASSALPQ EEAAELVNYI LTGKSSRLKP
AAPAAPMPKE EEISPAPQEE SQMEPKEEPQ KEVKESVKEA PESLPESPKE EAFEAEIPKE
SVKVTPKTLE QEPPKEELVS IEPSLESASE TLSDSNPLPQ EKTETKETIV ATTLATQTDA
EIQESEEKKE TLAQATVQKR VGLRIVKKRS EEPAPKADRP SLEEARTPSR TAGLKTLQSL
LGESDESEAA LARKKKKEKK KPLPAPTKKN EQKIDLLGDR ALETVSSFDD EQEEIVLFDL
TIRDDINKED EVAKKVDTDR IKVQRKTPFL DQGIRRVKRR KRRPQTVADK ESISGTIEIP
EEIRAYEFAE KTGKSIGEVI KVLFNLGLMI TKNDFLDRDS IEILAEELEL DVVIKNTSEA
LEYTSEEEED EDEEGLEERP PVVTIMGHVD HGKTSLLDKI RNTKVAAGEA GGITQHIGAY
TVEKDGKKIS FIDTPGHEAF TEMRARGAEV TDIVIIVIAA DDGVKQQTIE ALNHAKAANV
PIIIALNKVD KPDANPDKVK AEAADLGYSP LEWGGEYEFV HISAKTGEGI DHLLETILVQ
SELLELKANP EKAAKAVVIE SSLEKGKGPV ATVIVQSGTL KVGDSIVADT AYGRVRALID
DCGKNIQSIG PSEVAVVTGL SETPMAGAVL VSVENDSIAR EYAEKRALYL RQKELSRSTK
VSFDELSAMV AEGQLKSLPV IIKADTQGSL EAIRGSLEKL RNEEVKINII HAGVGGITES
DVVLAGASDN SVILGFNVRP TGSVKNRAKE LGVEVKTYSI IYALLDDVRA VLGGMMSPVL
EEENTGQAEV RETFTIAKVG TIAGCLVTDG SIQRGIKVRL IRNGVVVFTG NIASLKRFKD
DAREVSKGYE CGIMLEGFND VQVGDVFETY KEVEKARKL
