IF2_ALCBS
ID IF2_ALCBS Reviewed; 898 AA.
AC Q0VSS1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=ABO_0329;
OS Alcanivorax borkumensis (strain ATCC 700651 / DSM 11573 / NCIMB 13689 /
OS SK2).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Oceanospirillales;
OC Alcanivoracaceae; Alcanivorax.
OX NCBI_TaxID=393595;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700651 / DSM 11573 / NCIMB 13689 / SK2;
RX PubMed=16878126; DOI=10.1038/nbt1232;
RA Schneiker S., Martins dos Santos V.A.P., Bartels D., Bekel T., Brecht M.,
RA Buhrmester J., Chernikova T.N., Denaro R., Ferrer M., Gertler C.,
RA Goesmann A., Golyshina O.V., Kaminski F., Khachane A.N., Lang S., Linke B.,
RA McHardy A.C., Meyer F., Nechitaylo T., Puehler A., Regenhardt D., Rupp O.,
RA Sabirova J.S., Selbitschka W., Yakimov M.M., Timmis K.N., Vorhoelter F.-J.,
RA Weidner S., Kaiser O., Golyshin P.N.;
RT "Genome sequence of the ubiquitous hydrocarbon-degrading marine bacterium
RT Alcanivorax borkumensis.";
RL Nat. Biotechnol. 24:997-1004(2006).
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; AM286690; CAL15777.1; -; Genomic_DNA.
DR RefSeq; WP_011587625.1; NC_008260.1.
DR AlphaFoldDB; Q0VSS1; -.
DR SMR; Q0VSS1; -.
DR STRING; 393595.ABO_0329; -.
DR PRIDE; Q0VSS1; -.
DR EnsemblBacteria; CAL15777; CAL15777; ABO_0329.
DR KEGG; abo:ABO_0329; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000008871; 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; 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 PANTHER; PTHR43381; PTHR43381; 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; SSF46955; SSF46955; 1.
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..898
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008193"
FT DOMAIN 398..567
FT /note="tr-type G"
FT REGION 51..70
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..303
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..414
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 432..436
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 453..456
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 507..510
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 543..545
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 51..66
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 114..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 407..414
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 453..457
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 507..510
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 898 AA; 98533 MW; E8FD7B5725DF994D CRC64;
MAETTVKKLA DIVGTPVEKL LTQMKDAGLP HGDASEVVSD EQKQQLLAHL RKSHGAEDEG
SGKKITLKRK STSTIKTTGA AGKSKTVNVE VRKKRTYMKR DVVEAEEREE AERLAAEEAA
RIAEEEKRAA QEAAKRAADD EAARLKEDEA RAKAEQERKA AGEKAAEEKS KRVSVPKVSA
TKKPAKEETP EEKAKREEAE RKQREADEAK RKQEAEARKK AEEEAARRTA EEAARIAAEL
EQRGEQEEKK PAVEDDKGSS IVNAAQEASY QREERQSRRR RRKPKVAGVV HGKMKSSMNK
QHGFKTPTEK KIYEVEVPET ITVGDLAQRM NIKAKSLIKS LMKMGEMATV NQPIDQETAF
LLVEEMGHKP VASKGQEELL EDHLAADLVT RDSVDSEHRA PVVTIMGHVD HGKTSLLDYI
RKAKVASGEA GGITQHIGAY HVEHEKGMIT FLDTPGHAAF TAMRARGAKA TDIVVIVVAA
DDGVMPQTEE AINHAKASGA PIIIAVNKID KEQADPDRVR NELATKDVIP EEWGGEYQFI
NVSAHSGEGV DDLLDAILLQ SELLELQAQA SGSATGVVIE SRIEKGRGTV ASILVQGGEL
QIGDMLLAGA HFGRVRAMVD ENGKAIKKAG PSIPVEVLGL NGAPEAGEQI QVVTDERKAR
EVAEFRQERD RELKLKRQQA SKLENLFENM GSAETKTVNI VLKTDVRGSL EALTSALNDL
GTDEVKVNLV SSGVGAINES DVNLAMTSEG VLLGFNVRAD SKAKRVCEQE GIDLRYYSVI
YELIDDVKQA MSGLLAPEKR EEILGVAQVR DVFRSSKFGA VAGCMVVEGT LYRNRPIRVL
RDDVVVFEGE LESLRRFKDD VPEVRNGMEC GIAVKSYNDV KEGDKIEVFE VKEVARFL
