IF2_ALIB4
ID IF2_ALIB4 Reviewed; 890 AA.
AC A8EWD7;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Abu_2043;
OS Aliarcobacter butzleri (strain RM4018) (Arcobacter butzleri).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Arcobacteraceae; Aliarcobacter.
OX NCBI_TaxID=367737;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RM4018;
RX PubMed=18159241; DOI=10.1371/journal.pone.0001358;
RA Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Woesten M.M.S.M.,
RA Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G., Malek J.A.,
RA Rogosin A., Stanker L.H., Mandrell R.E.;
RT "The complete genome sequence and analysis of the Epsilonproteobacterium
RT Arcobacter butzleri.";
RL PLoS ONE 2:E1358-E1358(2007).
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; CP000361; ABV68260.1; -; Genomic_DNA.
DR RefSeq; WP_012147925.1; NC_009850.1.
DR AlphaFoldDB; A8EWD7; -.
DR SMR; A8EWD7; -.
DR STRING; 367737.Abu_2043; -.
DR EnsemblBacteria; ABV68260; ABV68260; Abu_2043.
DR KEGG; abu:Abu_2043; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_4_1_7; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001136; 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..890
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335455"
FT DOMAIN 387..554
FT /note="tr-type G"
FT REGION 110..216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 396..403
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 421..425
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 442..445
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 496..499
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 532..534
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 110..133
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 145..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 396..403
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 442..446
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 496..499
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 890 AA; 97262 MW; 59D97729EA9DF258 CRC64;
MSDTVRVYEI AEEAGASSQD VIAKAKDLGI ELKSPQTAVS YEDAEEITKY MMTGKSERLA
TKPAKVKKVV KKEEVKKETE EIETPKEKIE TVQKVEKEII KKPELKKVEI SKPISKAPQK
SEEESENLEN PNKIVPKRKG LVIIKKKRPK EEELEEQQTI TENQSKKQMK SLSEILGGVD
DEEKSYNEPK NKENDDIKKQ KVKKEKKKPL IKTQDHGKKL DVDREYSDEF ASSDDSLLGE
EIVLLDMDLS DSYKIFDEPK PQNIVNQSRS SKPAAFGNVP QGLKRGKRKK RIVRTQEKAE
ITSVTIPEDI RVYEFAEACG KSPAEVITVL FSLGMMVTKN DFLKQDELEI LGEEFGIEVT
VKDALEDVNY VETYNDEEDI DTSSFVTRPP VVTIMGHVDH GKTSLLDKIR SSKVAAGEAG
GITQHITSYT VTKNGQEITF VDTPGHAAFS AMRARGANVT DIIIIVVAAD DGVKMQTEEV
ISHAKASGCP IIVAMNKMDK ETANPDMVKA QMAEKGLTPI DWGGDIEFIG VSARTGDGIE
DLLENILLQA EILELKADPT AKAKATVIEA SLEKGRGPVA NVIVQNGTLK IGDNIVCDTT
FGRVKAITDD NGKPVKELGL SQTGTVLGLN EVPTTGSVLV AMDTEKEVRE IATTRAEHAR
AKELSKSTKV SLEEMSGLIA EGKIKQLPVI IKADVGGSLE AIKGSLEKIA NDEVKVKVVH
AAVGGITESD LVLAGASGEC IILGFNVRPT GSVKAKAKAD GVTINTYSII YDLIDDVKHA
LSGMMSAVIR EENTGQAEVR DTFVVPKVGT VAGCLVTDGK VIRGGHARII RDGVVTYTGK
ISSLKRFKDD VKEVANGYEC GIMFDKFNDI KVGDFIETFI QIEEKVSVDD
