IF2_PELPD
ID IF2_PELPD Reviewed; 921 AA.
AC A1AMM1;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Ppro_0963;
OS Pelobacter propionicus (strain DSM 2379 / NBRC 103807 / OttBd1).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfuromonadales;
OC Desulfuromonadaceae; Pelobacter.
OX NCBI_TaxID=338966;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2379 / NBRC 103807 / OttBd1;
RG US DOE Joint Genome Institute;
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 Saunders E., Brettin T., Bruce D., Han C., Tapia R., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Lovley D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Pelobacter propionicus DSM 2379.";
RL Submitted (OCT-2006) 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}.
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DR EMBL; CP000482; ABK98591.1; -; Genomic_DNA.
DR RefSeq; WP_011734898.1; NC_008609.1.
DR AlphaFoldDB; A1AMM1; -.
DR SMR; A1AMM1; -.
DR STRING; 338966.Ppro_0963; -.
DR EnsemblBacteria; ABK98591; ABK98591; Ppro_0963.
DR KEGG; ppd:Ppro_0963; -.
DR eggNOG; COG0532; Bacteria.
DR eggNOG; COG3266; Bacteria.
DR HOGENOM; CLU_006301_5_1_7; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 79180at2; -.
DR Proteomes; UP000006732; 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..921
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008295"
FT DOMAIN 421..590
FT /note="tr-type G"
FT REGION 81..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 175..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 219..301
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..437
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 455..459
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 476..479
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 530..533
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 566..568
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 94..112
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 430..437
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 476..480
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 530..533
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 921 AA; 98625 MW; FAA1A062D89F4D7C CRC64;
MSKIRVSNLA EKLGLEHKEV LARLKEIGVD AKTATSLVDE DVLKKLMPSL SPDGAEEVRV
TTTIIRRRAK AAPVVEPAPA AVAESLEEKP AEPVAPAAPT PPEVPAAAPA PPKAAAAPAE
AATMNARIIA PPPAPVETAA PVAAAPVAAA TAPPEKALPT PPVVEAPVVE AKPEPVVEKP
KVPAQPDKPS ANQARILGRM EIPGVTTRPT RVVRRDGTVA PAAEHAQRRP SPAAGAPSRG
AAPDRSRMKP ATLPPSAPPA ADDRRKFGGK SAAPHSEGAG KGGKKGGAST AKKKEQPKKH
EILEKRERVF DPVYRGSRKK VKERASETRK TEITIPKAIK RIIKISETIS VGELAKRMGI
KANDLIKSLM KMGMMVTINH ALDFETTVIL ASEYGYEVEN MAVDLDEILE STPDAPETLV
KRPPVVTIMG HVDHGKTSLL DAIREANVIA GEAGGITQHI GAYDVELNGR KITFLDTPGH
EAFTAMRARG AKVTDIVILV VAADDGVMPQ TREAINHSKA AGVPIVVAIN KIDKPEAKPE
RVKQELMEFG LVASEWGGDA TMVEVSAKKR LNLEGLLEMV LLQADLMELK ANPDKEAKGT
IVEAKLDRGR GPVATVLVQE GTLKNGDYCV VGVHSGRVRA IHNDRGEKVN EAGPSMPVEV
IGLSGVPDAG DVFVSLKDEK QAKEIATLRQ IKQREIEMAK HSKVTLEDLY KQIQSGDVKD
LNVIVKGDVQ GSVEVVSDSF RKLSTDAVRL NVIHSGVGAI TETDVNLAAA SNTIIIGFNV
RPEVKAQAMA EKEGVDIRLY SIIYDAVEDV KKAMEGLLDP TLKEKYLGRA EIREVFSVPK
IGNIAGSYVQ DGKMLRNAQA RLLRDNVVIY EGKLSSLRRI KDDVKEVAAG YECGIGLENY
NNIRIGDIIE AFEIEKVATK L
