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   27-MAR-2024, entry version 104.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN   OrderedLocusNames=Sama_0961;
OS   Shewanella amazonensis (strain ATCC BAA-1098 / SB2B).
OC   Bacteria; Pseudomonadota; 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   KEGG; saz:Sama_0961; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_6_3_6; -.
DR   OrthoDB; 9811804at2; -.
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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
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; IPR004161; EFTu-like_2.
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; PF03144; GTP_EFTU_D2; 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.
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
//