IF2_SHESA
ID IF2_SHESA Reviewed; 889 AA.
AC A0KTZ6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 12-DEC-2006, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=Shewana3_1030;
OS Shewanella sp. (strain ANA-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=94122;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANA-3;
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 Chertkov O., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Newman D.,
RA Salticov C., Konstantinidis K., Klappenback J., Tiedje J., Richardson P.;
RT "Complete sequence of chromosome 1 of Shewanella sp. ANA-3.";
RL Submitted (SEP-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; CP000469; ABK47265.1; -; Genomic_DNA.
DR RefSeq; WP_011716143.1; NC_008577.1.
DR AlphaFoldDB; A0KTZ6; -.
DR SMR; A0KTZ6; -.
DR STRING; 94122.Shewana3_1030; -.
DR EnsemblBacteria; ABK47265; ABK47265; Shewana3_1030.
DR KEGG; shn:Shewana3_1030; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000002589; 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.
FT CHAIN 1..889
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008334"
FT DOMAIN 389..558
FT /note="tr-type G"
FT REGION 115..293
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..405
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 423..427
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 444..447
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 498..501
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 534..536
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 115..260
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 267..288
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 398..405
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 444..448
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 498..501
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 889 AA; 96509 MW; CA848C00CB406F13 CRC64;
MADTTVEKLA TEVGKSVERL IEQFSQAGIK KGQTDNVSEA EKQQLLDYLK KQHGGESAPT
KMTLQRKTVS TLSVAGNGGQ SKDVKVEVRK TRTFVKRDVS EAVLKAEEEA KAKAEAEAQA
KAEAEAKARA EAEAKAKADA EAKAEAKAKA DAEAKAKAKA ATDAKTTKDT SPEAEAARVE
AERLKAAQAE ATKRKQDEEA AKAAEKARLL AEENSKRWDE EERQRKEAER YSDHHITTSK
VARAAEDSSD MDEEKRGRRA RNKNTAKTKR GGKDARDGRE KHMRNRSTAP ESMAHGFNKP
VAAVTRDVRI GETVTVAELA HLMAVKATEI IKQMMKMGSM VTINQVLDQE TAQLVAEEMG
HKVVLIRENE LEQQVLSERD EEGGVKLEPR APVVTIMGHV DHGKTSLLDY IRRAKVAAGE
AGGITQHIGA YHVETENGMI TFLDTPGHAA FTAMRARGAK ATDIVVLVVA ADDGVMPQTI
EAIQHAKAGN VPLIVAVNKM DKPEADIDRV KSELAQHGVM SEDWGGDNMF AFVSAKTGAG
VDDLLEGILL QAEVLELKAV RDGMAAGVVI ESQLDKGRGP VATILVQEGT LRQGDIVLCG
LEYGKIRAMK DENGRSITEA GPSIPVEILG LSGVPSAGDE ATVVRDERKA REVALYRQGK
FRDVKLARQQ KSKLENMFAN MTEGEVKELN IVLKADVQGS LEAITDSLMG LSTDEVKVNI
IARGVGALTE TDATLAAASN AIMVGFNVRA DAQARKTIES ESVDLRYYSV IYNLIDEVKA
AMTGMLSPEF KQQIIGLAEV RDVFKSPKLG AIAGCMVTEG TIKRSAPIRV LRDNVVIFEG
ELESLRRFKD DVNEVRNGME CGIGVKNYND VRVGDQIEVF ETVEVARTL
