IF2_ALKOO
ID IF2_ALKOO Reviewed; 719 AA.
AC A8MFA8;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 04-DEC-2007, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Clos_1528;
OS Alkaliphilus oremlandii (strain OhILAs) (Clostridium oremlandii (strain
OS OhILAs)).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Alkaliphilus.
OX NCBI_TaxID=350688;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OhILAs;
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 Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Stolz J.F., Dawson A., Fisher E.,
RA Crable B., Perera E., Lisak J., Ranganathan M., Basu P., Richardson P.;
RT "Complete genome of Alkaliphilus oremlandii OhILAs.";
RL Submitted (OCT-2007) 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}.
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; CP000853; ABW19071.1; -; Genomic_DNA.
DR RefSeq; WP_012159383.1; NC_009922.1.
DR AlphaFoldDB; A8MFA8; -.
DR SMR; A8MFA8; -.
DR STRING; 350688.Clos_1528; -.
DR EnsemblBacteria; ABW19071; ABW19071; Clos_1528.
DR KEGG; aoe:Clos_1528; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000269; 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; 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; PF04760; IF2_N; 2.
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..719
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000057649"
FT DOMAIN 221..390
FT /note="tr-type G"
FT REGION 54..75
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 97..122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 230..237
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 255..259
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 276..279
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 330..333
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 366..368
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 230..237
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 276..280
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 330..333
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 719 AA; 78336 MW; 0133C7018C36FB1A CRC64;
MSKIRVYQLA KKLGISNKEL IDKLKELSIE VNSHMSTVDN ENADVLIELF TEQNKEETKP
NVDEKPPNQD TLTDNVNESA ESIQNVDKKH FKKEINSTKN VTPNGNNKKD KKKKNKKDKR
KNYIANNDVS AESKGEQVIQ LKNKLTVKEL SETLNKSASE IITKLIGLGI MATINQELDY
DTASIIAAEF GIEVEPMTDI DAEEDVFDII IEPDKPEDLK HRSPVVTVMG HVDHGKTSLL
DAIRKTKVTN SEAGGITQHI GASEIKVNDK KIVFLDTPGH EAFTSMRARG AKVTDVAILV
VAADDGVMPQ TIEAISHAKA AEVPIIVAIN KMDKPSANPD RVKQELADQG LLIEEWGGDV
ISVPVSARSG ENIDALLEMV LLVSEMSELK ANPNRKAIGT VIEAQLDVGK GPVATVLVQN
GTLFIGDSVV IGNTYGRIRA MMNDSGKRVK VAGPSTAVEI TGLSEVPEAG DQLFAVDDDK
AAKAIVEKRI NKIKEEQLKA GQKISLDALF SQMEQGQLKD LNLIIKADTQ GSVEAVKQSL
VKLSNDEVVI NPIHGGVGGI TESDVMLATA SNAIIIGFNV RPTSNAASAA KKENVDIRTY
RIIYKAIEDI EAAMKGMLDP EFVEEELGKA EVRATFKVPG AGTIGGCYVI EGKILRNAKI
RLVRDNIVIH EGSIDSLKRF KDDAKEVATG YECGIGISQF NDLKEGDIIE AYHMKEIER
