IF2_AERS4
ID IF2_AERS4 Reviewed; 898 AA.
AC A4SJR5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 15-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=ASA_1010;
OS Aeromonas salmonicida (strain A449).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=382245;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=A449;
RX PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J.,
RA Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C.,
RA Brown L.L.;
RT "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into
RT the evolution of a fish pathogen.";
RL BMC Genomics 9:427-427(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; CP000644; ABO89137.1; -; Genomic_DNA.
DR RefSeq; WP_005317521.1; NC_009348.1.
DR AlphaFoldDB; A4SJR5; -.
DR SMR; A4SJR5; -.
DR STRING; 382245.ASA_1010; -.
DR EnsemblBacteria; ABO89137; ABO89137; ASA_1010.
DR KEGG; asa:ASA_1010; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000225; 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..898
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008192"
FT DOMAIN 398..567
FT /note="tr-type G"
FT REGION 96..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 407..414
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 432..436
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 453..456
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 507..510
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 543..545
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 96..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 181..218
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 226..265
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 273..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 407..414
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 453..457
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 507..510
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 898 AA; 98376 MW; 016CE102CEA0A3A2 CRC64;
MAEVSVKQLA TDIDTPVDRL LQQFVDAGIS KSKADDLVSE SEKQTLLAHL KKQHGGDELT
APARMTLQRK TKSTISVQGT GGKNKEVQVE VRKTRTYVKR SALEDEQRQA EAEETARLEA
EEKARSEAEN KVRLDAEEKA RREAEQARRE AEEKARIEAQ SKARQAPQPA KAASSTAQQE
AEKMAKREAE ELKRQQEQTA LQKAEELAAK KAEEARLMAE QNGPRWAEEE AARAKESSDY
HLTTNKHAQA AEDELDRKEE TSRRTAAAAV KAPKKAGRRE DDRDSRNPRA RKGKRGKMAM
PNAMKHGFNK PAAVVNRDVV IGETITVAEL ANKMAVKGVE VIKAMMKMGA MATINQVIDQ
ETAQLVAEEM GHKVVLRREN ELEEAVLSDR DETSEAKSRA PVVTIMGHVD HGKTSLLDYI
RKAKVAAGEA GGITQHIGAY HVETDSGMIT FLDTPGHAAF TSMRARGAKS TDIVVLVVAA
DDGVMPQTIE AIQHAKAAEV PIVVAVNKID KPEADPDRVK TELARYNVMS EDWGGDSQFV
HVSAKSGEGI DDLLEAILIQ SEVLELKAVV DGMASGVVIE SFLDKGRGPV ATVLVQEGTL
RQGDIVLCGL EYGRIRAMRD ELGREIKEAG PSLPVEILGL SGVPSAGDEA TVVRDEKKAR
EVALYRQGKF RDVKLARQQK AKLENMFANM TEGEVSEVNV VIKADVQGSV QAICDALVQL
STDEVKVKIV GSGVGGITET DATLAAASSA ILVGFNVRAD ASARKVIESE SLDLRYYSVI
YDLIDEVKQA MSGKLAPEYR QEIIGLAEVR SVFKSPKFGA VAGCMVTEGV VKRSNRIRVL
RDNVVIYEGE LESLRRFKDD VNEVRNGYEC GIAVKNYNDV REGDQIEVYE TIEIQRTL
