IF2_STAS1
ID IF2_STAS1 Reviewed; 701 AA.
AC Q49X54;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 114.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=SSP1499;
OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS 20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=342451;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT pathogenesis of uncomplicated urinary tract infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
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; AP008934; BAE18644.1; -; Genomic_DNA.
DR RefSeq; WP_011303257.1; NZ_MTGA01000034.1.
DR AlphaFoldDB; Q49X54; -.
DR SMR; Q49X54; -.
DR STRING; 342451.SSP1499; -.
DR EnsemblBacteria; BAE18644; BAE18644; SSP1499.
DR KEGG; ssp:SSP1499; -.
DR PATRIC; fig|342451.11.peg.1501; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000006371; 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..701
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228247"
FT DOMAIN 203..372
FT /note="tr-type G"
FT REGION 48..123
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..219
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 237..241
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 258..261
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 312..315
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 348..350
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 61..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 106..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 212..219
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 258..262
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 312..315
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 701 AA; 77470 MW; 7649B09D3B7BF181 CRC64;
MSKKRIYEYA KDLKIKSKEI IHELKKMDVE VTSHMQTLED DQIKALDKIY KPEKAEQSEK
SQQKNTQNKQ QTTHNKGNQS NKGNQNNKPN NKKNNKNNKN NKNNKNNKQP KQEEPKEMPS
KITYQDGITV GELAEKLNVD SSGIIKKLFL LGIMANINQS LDDETLELIV DDYGVEIEKE
IVVDEEDLAI YFDDETEDEN AIERPAVVTI MGHVDHGKTT LLDSIRHTKV TAGEAGGITQ
HIGAYQIEND GKKITFLDTP GHAAFTTMRA RGAQVTDITI LVVAADDGVM PQTIEAINHA
KEAEVPTIVA VNKIDKPTSN PDRVMQELTE YGLIPEDWGG DTIFVPLSAL SGDGIEDLLE
MIVLTSEVQE LKANPEKNAV GTVIEAELDK SRGPSASLLV QNGTLNVGDS LVVGNTYGRI
RAMVNDLGQR IKTAGPSTPV EITGINDVPQ AGDRFVVFKD EKQARRIGEA RHEANVMQQR
QESKSVSLDN LFEQMKQGEM KDLNVIIKGD VQGSVEALAA SLMKIDVEGV NVRIIHTAVG
AINESDVTLA NASNGIIIGF NVRPDTGAKR AADNEGVDMR LHRVIYNVIE EIESAMKGML
DPEFEEQVIG QAEVRQTFKV SKVGTIAGSY VIDGKITRNA GVRVIRDGIV QFEGELDTLK
RFKDDAKEVA QGYECGITIE KYNDLKEGDI IEAFEMVEIK R
