IF2_SHESM
ID IF2_SHESM Reviewed; 885 AA.
AC Q0HLG1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 03-OCT-2006, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=Shewmr4_1026;
OS Shewanella sp. (strain MR-4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=60480;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MR-4;
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 Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Nealson K.,
RA Konstantinidis K., Klappenbach J., Tiedje J., Richardson P.;
RT "Complete sequence of Shewanella sp. MR-4.";
RL Submitted (AUG-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; CP000446; ABI38106.1; -; Genomic_DNA.
DR RefSeq; WP_011621817.1; NC_008321.1.
DR AlphaFoldDB; Q0HLG1; -.
DR SMR; Q0HLG1; -.
DR KEGG; she:Shewmr4_1026; -.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
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.
FT CHAIN 1..885
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008335"
FT DOMAIN 385..554
FT /note="tr-type G"
FT REGION 135..159
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 184..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 394..401
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 419..423
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 440..443
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 494..497
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 530..532
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 184..256
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..284
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 394..401
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 440..444
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 494..497
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 885 AA; 96188 MW; 0A0A8414698CC8E1 CRC64;
MADTTVEKLA TEVGKSVERL IEQFSQAGIK KGHTDNVSEA EKQQLLDYLK KQHGGDNAPT
KMTLQRKTVS TLSVAGNGGQ SKDVKVEVRK TRTFVKRDAN DAVLKAEEEA KAKAEAEAKA
KAEAEAKAKA EAEVKAKAEA EAKAKAEAEA KAKAKAAAEV KVIKELSPEA EAARVEAERL
KAVQAEATKR KQDEEAAKAA EKARLLAEEN SKRWAEEERQ RLEAERYSDH HITTSKVARA
AEDSSDMDEE KRGRRARNKN TAKSKRGGKD ARDGREKHMR NRSTAPESMA HGFNKPVAAV
NRDVRIGETV TVAELAHLMA VKATEIIKQM MKMGSMVTIN QVLDQETAQL VAEEMGHKVV
LIRENELEQQ VLSERDEEGV VKLEPRAPVV TIMGHVDHGK TSLLDYIRRA KVAAGEAGGI
TQHIGAYHVE TDNGMITFLD TPGHAAFTAM RARGAKATDI VVLVVAADDG VMPQTIEAIQ
HAKAGNVPLI VAVNKMDKPE ADIDRVKSEL AQHGVMSEDW GGDNMFAFVS AKTGAGVDDL
LEGILLQAEV LELKAVRDGM AAGVVIESQL DKGRGPVATI LVQEGTLRQG DIVLCGLEYG
KIRAMKDENG RSITEAGPSI PVEILGLSGV PSAGDEATVV RDERKAREVA LYRQGKFRDV
KLARQQKSKL ENMFANMTEG EVKELNIVLK ADVQGSLEAI TDSLMGLSTD EVKVNIIARG
VGALTETDAT LAAASNAIMV GFNVRADAQA RKTIESESVD LRYYSVIYNL IDEVKAAMTG
MLSPEFKQQI IGLAEVRDVF KSPKLGAIAG CMVTEGTIKR SAPIRVLRDN VVIFEGELES
LRRFKDDVNE VRNGMECGIG VKNYNDVRVG DQIEVFETVE VARTL
