IF2_STAES
ID IF2_STAES Reviewed; 720 AA.
AC Q8CST4;
DT 28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=SE_0945;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO04542.1; -; Genomic_DNA.
DR RefSeq; NP_764500.1; NC_004461.1.
DR RefSeq; WP_002456223.1; NZ_WBME01000001.1.
DR AlphaFoldDB; Q8CST4; -.
DR SMR; Q8CST4; -.
DR STRING; 176280.SE_0945; -.
DR EnsemblBacteria; AAO04542; AAO04542; SE_0945.
DR KEGG; sep:SE_0945; -.
DR PATRIC; fig|176280.10.peg.920; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000001411; 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.
FT CHAIN 1..720
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137254"
FT DOMAIN 222..391
FT /note="tr-type G"
FT REGION 48..138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 231..238
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 256..260
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 277..280
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 331..334
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 367..369
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 56..72
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 73..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 123..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 231..238
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 277..281
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 331..334
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 720 AA; 79343 MW; 07FB5A6A59CF970C CRC64;
MSKKRIYEYA KELNLKSKEI IDELKSMNVE VSNHMQALEE EQIKALDKKF KASQAKDTNK
QNTQNNHQKS NNKQNSNDKE KQQSKNNSKP TKKKEQNNKG KQQNKNNKTN KNQKNNKNKK
NNKNNKPQNE VEETKEMPSK ITYQEGITVG ELAEKLNVES AGIIKKLFLL GIMANINQSL
DEETLELIAD DYGVEIEKEV VVDEEDLSIY FDDETDDSDA IERPAVVTIM GHVDHGKTTL
LDSIRNTKVT EGEAGGITQH IGAYQIENSG KKITFLDTPG HAAFTTMRAR GAQVTDITIL
VVAADDGVMP QTIEAINHAK EAEVPTIVAV NKIDKPTANP DRVMQELTEY GLIPEDWGGD
TIFVPLSALS GDGIDDLLEM IGLVAEVQEL KANPNKQAVG TVIEAELDKS RGPAASLLVQ
NGTLNVGDAI VVGNTYGRIR AMVNDLGKRI KSAGPSTPVE ITGINDVPLA GDRFVVFGDE
KQARRIGEAR HEASVIQQRQ ESKNVSLDNL FEQMKQGEMK DLNVIIKGDV QGSVEALAAS
LMKIDVEGVN VRIIHTAVGA INESDVTLAN ASNGIIIGFN VRPDAGAKRA AEAENVDMRL
HRVIYNVIEE IESAMKGLLD PEFEEQVIGQ AEVRQTFKVS KVGTIAGSYV TEGKITRNAG
VRVIRDGIVL FEGELDTLKR FKDDAKEVAQ GYECGITIEK YNDLKEGDII EAFEMVEIQR
