IF2_PECAS
ID IF2_PECAS Reviewed; 900 AA.
AC Q6D9A5;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=ECA0712;
OS Pectobacterium atrosepticum (strain SCRI 1043 / ATCC BAA-672) (Erwinia
OS carotovora subsp. atroseptica).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Pectobacteriaceae; Pectobacterium.
OX NCBI_TaxID=218491;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCRI 1043 / ATCC BAA-672;
RX PubMed=15263089; DOI=10.1073/pnas.0402424101;
RA Bell K.S., Sebaihia M., Pritchard L., Holden M.T.G., Hyman L.J.,
RA Holeva M.C., Thomson N.R., Bentley S.D., Churcher L.J.C., Mungall K.,
RA Atkin R., Bason N., Brooks K., Chillingworth T., Clark K., Doggett J.,
RA Fraser A., Hance Z., Hauser H., Jagels K., Moule S., Norbertczak H.,
RA Ormond D., Price C., Quail M.A., Sanders M., Walker D., Whitehead S.,
RA Salmond G.P.C., Birch P.R.J., Parkhill J., Toth I.K.;
RT "Genome sequence of the enterobacterial phytopathogen Erwinia carotovora
RT subsp. atroseptica and characterization of virulence factors.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:11105-11110(2004).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; BX950851; CAG73627.1; -; Genomic_DNA.
DR RefSeq; WP_011092323.1; NC_004547.2.
DR AlphaFoldDB; Q6D9A5; -.
DR SMR; Q6D9A5; -.
DR STRING; 218491.ECA0712; -.
DR PRIDE; Q6D9A5; -.
DR EnsemblBacteria; CAG73627; CAG73627; ECA0712.
DR GeneID; 57207441; -.
DR KEGG; eca:ECA0712; -.
DR PATRIC; fig|218491.5.peg.710; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000007966; 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; Reference proteome.
FT CHAIN 1..900
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228197"
FT DOMAIN 399..568
FT /note="tr-type G"
FT REGION 48..310
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..415
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 433..437
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 454..457
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 508..511
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 544..546
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 56..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..164
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 176..266
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..295
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 408..415
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 454..458
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 508..511
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 900 AA; 98925 MW; 35F0D1D72D43971F CRC64;
MTDVTVKSLA AEIQTPVDRL VQQFADAGMT KSASDSVTQH EKETLLAHLN RDRGNAPSKL
TLQRKTRSTL NVPSTGGKSK SVQIEVRKTR TYVKRDPIEA QQAEEEEQAR REAEEQAQRA
AEEQVKREAD LRETAEKAKR AADEQAKREA AEKAKRDVAE KEKVTNQQNE NMTKPAQSEK
AKREAEAAEL KRKAEETARL KVEEEARRIA EEARRMAEEN AGRWEAESAT KPEESADYHV
TTSHHAREAE DENDRQVEGE RRTRTRAAKV TKQKKGNRQS ESKADREEAR AVTRGGKGKR
KPSSLQQSFN KPVQAVNRDV VIGETVTVAE LANKMAVKGS QVIKTMMRLG AMATINQVID
QETAQLVAEE MGHKVILRRE NELEEAVMSD RDMGVAAEFR APVVTIMGHV DHGKTSLLDY
IRSTKVAAGE AGGITQHIGA YHVETDNGMI TFLDTPGHAA FTAMRARGAQ ATDIVVLVVA
ADDGVMPQTI EAIQHAKAAQ VPVVVAVNKI DKPDADPDRV KTELSQYGIM PEEWGGESQF
VHVSAKAGTG IDELLNAILL QAEVLELKAV RSGMANGVVI ESFLDKGRGP VATVLVREGT
LNKGDIVLCG FEYGRIRAMR DELGREITSA GPSIPVEILG MSGVPAAGDE ATVVRDEKKA
REVALYRQGK FREVKLARQQ KSKLENMFAN MTEGEVSELN IVLKSDVQGS CEAISDSLQK
LSTDEVKVKI VGSGVGGITE TDATLAAASN AIILGFNVRA DASARRVVEA ESLDLRYYSV
IYDLIDEVKQ AMSGMLAPEY KQEIIGLAEV RDVFKSPKFG AVAGCMVTEG IVKRHNKIRV
LRDNVVIYEG ELESLRRFKD DVNEVRNGME CGIGVKNYND VRPGDMIEVF ETIEIKRTIA
