IF2_SHEPW
ID IF2_SHEPW Reviewed; 900 AA.
AC B8CKH3;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=swp_1218;
OS Shewanella piezotolerans (strain WP3 / JCM 13877).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Alteromonadales;
OC Shewanellaceae; Shewanella.
OX NCBI_TaxID=225849;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WP3 / JCM 13877;
RX PubMed=18398463; DOI=10.1371/journal.pone.0001937;
RA Wang F., Wang J., Jian H., Zhang B., Li S., Wang F., Zeng X., Gao L.,
RA Bartlett D.H., Yu J., Hu S., Xiao X.;
RT "Environmental adaptation: genomic analysis of the piezotolerant and
RT psychrotolerant deep-sea iron reducing bacterium Shewanella piezotolerans
RT WP3.";
RL PLoS ONE 3:E1937-E1937(2008).
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; CP000472; ACJ28012.1; -; Genomic_DNA.
DR RefSeq; WP_020911390.1; NC_011566.1.
DR AlphaFoldDB; B8CKH3; -.
DR SMR; B8CKH3; -.
DR STRING; 225849.swp_1218; -.
DR PRIDE; B8CKH3; -.
DR EnsemblBacteria; ACJ28012; ACJ28012; swp_1218.
DR KEGG; swp:swp_1218; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000753; 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..900
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000117337"
FT DOMAIN 400..569
FT /note="tr-type G"
FT REGION 119..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..416
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 434..438
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 455..458
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 509..512
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 545..547
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 119..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..273
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 277..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 409..416
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 455..459
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 509..512
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 900 AA; 96531 MW; C66FDB0EC9C8E637 CRC64;
MADTTVDKLA KEVGKSADRL VEQFSQAGIK KSANDTVSES EKQQLLDFLK KQHGGDAAPQ
KMTLQRKSVS TLSVAGSGGQ SKDVKVEVRK KRTFVKRDEA AEAELAAAAK AEEEAKAAAA
KAEAEAKAKA DAEAKQKADA EAKAKAEKAA KAKSEKQEAA PAQTADEKAA KDEADKLQAA
KDEVAKAKAD AEAAAATEEA RRLAEENAKR WADEEKARKE AEKTGDHHVT TSTEARAAED
TADANAEKRG RRPRKPSANA GNNANSNSNA GSGRPGGKGK RGKDNRRDNR NSRNSRNARS
VAPESMDQAF NKSAVVVKAE VSIGETVSVS ELASKMSVKA TEIIKQMMKM GSMVTINQVL
DQETAQLVAE EMGHKVILTR ENELEHQVLA DRNGDVKVEP RAPVVTIMGH VDHGKTSLLD
YIRRAKVASG EAGGITQHIG AYHVETGNGM ITFLDTPGHA AFTAMRARGA KATDIVILVV
AADDGVMPQT IEAIQHAKAG GVPLIVAVNK IDKPEADPER VKSELSQHGV MSEDWGGENM
FVHVSAKSGE GIDELLEGIL LESEVLELKA VREGMAAGVV VESKLDKGRG PVATVLVQEG
TLKQGDIVLC GLEYGKVRAM KDENGKAITE AGPSIPVEIL GLSGVPSAGD EATVVRDERK
AREVALYRQG KFRDVKLARQ QKSKLENMFA NMVEGEVQEL NLVLKADVQG SLEAIADSLN
KLSTDEVKVN IIARGVGGLT ETDATLAAAS NAIMVGFNVR ADAQARKVVD SESVDLRYYS
IIYQLIDEVR DAMGGMLAPE FRQEIIGLAE VRDVFKSPKI GAIAGCMVTE GTIKRSAPIR
VLRENVVIYE GELESLRRFK DDVSDVRNGM ECGIGVKNYN DVRVGDQIEV FETVEIARTL
