IF2_SHEAM
ID IF2_SHEAM Reviewed; 882 AA.
AC A1S462;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-FEB-2007, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Sama_0961;
OS Shewanella amazonensis (strain ATCC BAA-1098 / SB2B).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=326297;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1098 / SB2B;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Munk A.C., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Fredrickson J.,
RA Richardson P.;
RT "Complete sequence of Shewanella amazonensis SB2B.";
RL Submitted (DEC-2006) 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: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; CP000507; ABL99168.1; -; Genomic_DNA.
DR RefSeq; WP_011759077.1; NC_008700.1.
DR AlphaFoldDB; A1S462; -.
DR SMR; A1S462; -.
DR STRING; 326297.Sama_0961; -.
DR PRIDE; A1S462; -.
DR EnsemblBacteria; ABL99168; ABL99168; Sama_0961.
DR KEGG; saz:Sama_0961; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000009175; 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..882
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008327"
FT DOMAIN 382..551
FT /note="tr-type G"
FT REGION 67..202
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 223..278
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..398
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 416..420
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 437..440
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 491..494
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 527..529
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 83..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 163..202
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 223..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 261..278
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 391..398
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 437..441
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 491..494
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 882 AA; 95960 MW; FBB2AA4E6C2155CF CRC64;
MTEITVEKLA TEVGKTVDRL IEQFAQAGIK KAKADTVSES EKQQLLDFLK KQHGADAQPT
KMTLQRKTVS TLSVSSGGGQ SKDVKVEVRK KRTFVKRDGN EAALKAEEEA RAQAEAQAKA
EAEAKAKAEA EAKAKADAEA KAKAKAEAEA KAKASASAAK EQPKPVESEE AKAEAARLKS
QQEEAAKSKA AQEEAAAKEK ARLLAEENAA RWAEEERRRI EAERYGDHHV TTSKVARAAE
DSADLDDEKR GRRNRNKTQT KSKRGGKDAR EGREKHMKYK STPESMAHGF NKPVAAVTRD
VRIGETVTVA ELAQKMAVKA TEIIKAMMKM GSMVTINQVL DQETAQLVAE EMGHKVVLLR
ENELEHQVLA DRDDEGTTKL EPRAPVVTIM GHVDHGKTSL LDYIRRTKVA AGEAGGITQH
IGAYHVETDN GMITFLDTPG HAAFTAMRAR GAKATDIVIL VVAADDGVMP QTIEAIQHAK
AGNVPLIVAV NKMDKPEADI DRVKNELSQH GVMSEDWGGE NMFCYVSAKT GQGVDELLEA
ILLQAEVLEL KAVRDGMAAG VVIESQLDKG RGPVATVLVQ EGTLRQGDIV LCGLEYGKIR
AMKDENGRPI MEAGPSIPVE ILGLSGVPSA GDEATVVRDE RKAREVALYR QGKFRDVKLA
RQQKSKLENM FANMTEGEVQ ELNIVLKADV QGSLEAITDS LRKLSTDEVK VNIIASGVGA
LTETDATLAA ASNAIMVGFN VRADAQARKT IESEAVDLRY YSVIYDLIDE VKSAMSGMLS
PEFKQQIIGL AEVRDVFKSP KLGAIAGCMV IEGIVKRSAP IRVLRENVVI YEGELESLRR
FKDDVNEVRN GMECGIGVKN YNDVRVGDQI EVFETIEVAR TL
