IF2_SHEWM
ID IF2_SHEWM Reviewed; 894 AA.
AC B1KRR0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 87.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Swoo_3561;
OS Shewanella woodyi (strain ATCC 51908 / MS32).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=392500;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51908 / MS32;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Kuske C.R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Lykidis A., Zhao J.-S., Richardson P.;
RT "Complete sequence of Shewanella woodyi ATCC 51908.";
RL Submitted (FEB-2008) 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; CP000961; ACA87825.1; -; Genomic_DNA.
DR RefSeq; WP_012326158.1; NC_010506.1.
DR AlphaFoldDB; B1KRR0; -.
DR SMR; B1KRR0; -.
DR STRING; 392500.Swoo_3561; -.
DR EnsemblBacteria; ACA87825; ACA87825; Swoo_3561.
DR KEGG; swd:Swoo_3561; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000002168; 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..894
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093825"
FT DOMAIN 394..563
FT /note="tr-type G"
FT REGION 52..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 93..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..410
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 428..432
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 449..452
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 503..506
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 539..541
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 58..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 93..112
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 126..152
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 162..196
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 403..410
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 449..453
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 503..506
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 894 AA; 95999 MW; 9F9CF55BB85A3D80 CRC64;
MAETTVEKLA TEVGKSADRL VEQFSDAGIK KSKTDSVSEA EKQQLLEFLK KQHGGDSAPT
KMTLQRKSVS TLSVGTGSDS KDVKVEVRKK RTFVKRDPAA EAEAEAAAKL EAEAKAAAEA
AAKAQADAEA KAKAEAKAKA DAEAKEKAKA NAAAKAKTAP TAEEKAAQDE ADRLQAAKDD
VAKAKADEEA KAAAEAARIL AEENSARWAE EEKQRKELEK NVDHHVTTSS EARAAEDTAD
ANAEKRDRRP RKAPAAAPAN APANTGKGKR RGGKDNRRDS RNARGGRNAR NNRSVAPESM
DHAFTKPVAV VKTDVSIGET VSVAELASKM SIKATEIIKQ MMKMGSMVTI NQVLDQETAQ
LVAEEMGHKV VLIRENELEH QVLADRDGNI QAESRAPVVT IMGHVDHGKT SLLDHIRMAK
VASGEAGGIT QHIGAYHVET DNGMITFLDT PGHAAFTAMR ARGAKATDIV ILVVAADDGV
MPQTIEAIQH AKAGGVPLIV AVNKMDKPEA DPERVKSELS QHGVMSEDWG GNNMFVHVSA
KSGEGIDELL EGILLEAEVL ELKAIREGMA AGVVVESKLD KGRGPVATVL VQEGTLKQGD
IVLCGLEYGK VRAMRDENGR SVTEAGPSIP VEILGLSGVP SAGDEATVVR DERKAREVAL
YRQGKFRDIK LARQQKSKLE NMFANMTEGE VQELNIVLKA DVQGSLEAIC DSLNGLSTDE
VKVNIIARGV GGLTETDASL AAASNAIMVG FNVRADAQAR KVIESESVDL RYYSIIYQLI
DEVRDAMSGL LAPEFKQEII GLAEVRDVFK SPKIGAIAGC MVTEGTIKRS APIRVLRDNV
VIYEGELESL RRFKDDVNDV RNGMECGIGV KNYNDVRVGD QIEVFETVEI ARSL
