IF2_CROS8
ID IF2_CROS8 Reviewed; 903 AA.
AC A7MQE1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=ESA_03561;
OS Cronobacter sakazakii (strain ATCC BAA-894) (Enterobacter sakazakii).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Cronobacter.
OX NCBI_TaxID=290339;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-894;
RX PubMed=20221447; DOI=10.1371/journal.pone.0009556;
RA Kucerova E., Clifton S.W., Xia X.Q., Long F., Porwollik S., Fulton L.,
RA Fronick C., Minx P., Kyung K., Warren W., Fulton R., Feng D., Wollam A.,
RA Shah N., Bhonagiri V., Nash W.E., Hallsworth-Pepin K., Wilson R.K.,
RA McClelland M., Forsythe S.J.;
RT "Genome sequence of Cronobacter sakazakii BAA-894 and comparative genomic
RT hybridization analysis with other Cronobacter species.";
RL PLoS ONE 5:E9556-E9556(2010).
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; CP000783; ABU78774.1; -; Genomic_DNA.
DR RefSeq; WP_004385059.1; NC_009778.1.
DR AlphaFoldDB; A7MQE1; -.
DR SMR; A7MQE1; -.
DR PRIDE; A7MQE1; -.
DR EnsemblBacteria; ABU78774; ABU78774; ESA_03561.
DR GeneID; 56732218; -.
DR KEGG; esa:ESA_03561; -.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000260; 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..903
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008241"
FT DOMAIN 402..571
FT /note="tr-type G"
FT REGION 49..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..418
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 436..440
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 457..460
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 511..514
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 547..549
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 61..80
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..163
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 178..268
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 276..297
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 411..418
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 457..461
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 511..514
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 903 AA; 98677 MW; B47CB46A500E2E12 CRC64;
MTDVTVKALA AEIQTSVDRL VQQFADAGIP KSAEDSVTAQ EKQALLAHLN REHGSGPDKL
TLQRKTRSTL NIQGTGGKSK SVQIEVRKKR TFVKRDPQEA ERLAAEEQAK REAEEQARRE
AEEAAKREAE EKAKREAGDK AKREAEEQAK RDAADKAKRE AAETSKVSNQ QTDEVSKAAQ
AEKARREAEA LELKRKAEEE ARRKLEENAR RVAEEARRMA EENATKWESG SEEESEDTSD
YHVTTSQHAR QAEDDSDREV EGGRGRARPA KVARQKKSNK HSESKADREE ARAAVRGGKG
GKRKGSSLQQ GFNKPAQAVN RDVVIGETIT VAELANKMAV KGSQVIKAMM KLGAMATINQ
VIDQETAQLV AEEMGHKVIL RRENELEEAV MSDRDMGAQA EPRAPVVTIM GHVDHGKTSL
LDYIRSTKVA SGEAGGITQH IGAYHVQTDN GMITFLDTPG HAAFTAMRAR GAQATDIVVL
VVAADDGVMP QTIEAIQHAK AAKVPVVVAV NKIDKPDADP DRVKNELSQH GIIPEEWGGD
CQFVHVSAKA GTGIDELLDA ILLQSEVLEL KAVRKGMASG VVIESFLDKG RGPVATVLVR
EGTLNKGDIV LCGFEYGRVR AMRNELNQEV QEAGPSIPVE ILGLSGVPAA GDEVTVVRDE
KKAREVALYR QGKFREVKLA RQQKSKLENM FANMTEGEVH EVNIVLKADV QGSVEAISDS
LLKLSTDEVK VKIVGSGVGG ITETDATLAA ASNAILVGFN VRADASARRV IEAESLDLRY
YSVIYNLIDE VKAAMSGMLS PELKQQIIGL AEVRDVFKSP KFGAIAGCMV TEGTIKRHNP
IRVLRDNVVI YEGELESLRR FKDDVNEVRN GMECGIGVKN YNDVRVGDMI EVFEIIEIQR
SID
