IF2_STRA3
ID IF2_STRA3 Reviewed; 927 AA.
AC P0A3K6; Q9ZF20;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Translation initiation factor IF-2;
GN Name=infB; OrderedLocusNames=gbs0417;
OS Streptococcus agalactiae serotype III (strain NEM316).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=211110;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=3164 / Serotype III;
RX PubMed=10878130; DOI=10.1099/00221287-146-7-1661;
RA Hedegaard J., Hauge M., Fage-Larsen J., Mortensen K.K., Kilian M.,
RA Sperling-Petersen H.U., Poulsen K.;
RT "Investigation of the translation-initiation factor IF2 gene, infB, as a
RT tool to study the population structure of Streptococcus agalactiae.";
RL Microbiology 146:1661-1670(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NEM316;
RX PubMed=12354221; DOI=10.1046/j.1365-2958.2002.03126.x;
RA Glaser P., Rusniok C., Buchrieser C., Chevalier F., Frangeul L., Msadek T.,
RA Zouine M., Couve E., Lalioui L., Poyart C., Trieu-Cuot P., Kunst F.;
RT "Genome sequence of Streptococcus agalactiae, a pathogen causing invasive
RT neonatal disease.";
RL Mol. Microbiol. 45:1499-1513(2002).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000305}.
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DR EMBL; AJ251495; CAC00489.1; -; Genomic_DNA.
DR EMBL; AL766845; CAD46061.1; -; Genomic_DNA.
DR RefSeq; WP_000039152.1; NC_004368.1.
DR AlphaFoldDB; P0A3K6; -.
DR SMR; P0A3K6; -.
DR STRING; 211110.gbs0417; -.
DR EnsemblBacteria; CAD46061; CAD46061; CAD46061.
DR KEGG; san:infB; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_0_9; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000000823; 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..927
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137258"
FT DOMAIN 428..597
FT /note="tr-type G"
FT REGION 27..338
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..444
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 462..466
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 483..486
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 537..540
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 573..575
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 40..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 98..145
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 146..161
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..224
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 235..250
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 270..296
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 297..314
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 437..444
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 483..487
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 537..540
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 927 AA; 102401 MW; F6D7F59877FC682C CRC64;
MSKKRLHEIA KEIGKTSKEV VEQAQSLGLP VKSHASSVEE NDATRIVESF SSSKTKAPTN
SVQTNQGVKT ESKTVETKQG LSDDKPSTQP VAKPKPQSRN FKAEREARAK AEAEKRQHNG
DHRKNNRHND TRSDDRRHQG QKRSNGNRND NRQGQQNNRN KNDGRYADHK QKPQTRPQQP
AGNRIDFKAR AAALKAEQNA EYSRHSEQRF REEQEAKRQA AKEQELAKAA ALKAQEEAQK
AKEKLASKPV AKVKEIVNKV AATPSQTADS RRKKQTRSDK SRQFSNENED GQKQTKNKKN
WNNQNQVRNQ RNSNWNHNKK NKKGKTNGAP KPVTERKFHE LPKEFEYTEG MTVAEIAKRI
KREPAEIVKK LFMMGVMATQ NQSLDGDTIE LLMVDYGIEA HAKVEVDEAD IERFFADEDY
LNPDNLTERP PVVTIMGHVD HGKTTLLDTL RNSRVATGEA GGITQHIGAY QIEEAGKKIT
FLDTPGHAAF TSMRARGASV TDITILIVAA DDGVMPQTVE AINHSKAAGV PIIVAINKID
KPGANPERVI SELAEHGVIS TAWGGESEFV EISAKFGKNI QELLETVLLV AEMEELKADA
DVRAIGTVIE ARLDKGKGAV ATLLVQQGTL NVQDPIVVGN TFGRVRAMTN DLGRRVKVAG
PSTPVSITGL NEAPMAGDHF AVYADEKAAR AAGEERAKRA LLKQRQNTQR VSLENLFDTL
KAGEVKSVNV IIKADVQGSV EALAASLLKI DVEGVKVNVV HSAVGAINES DVTLAEASNA
VIIGFNVRPT PQARQQADAD DVEIRQHSII YKVIEEVEEA MKGKLDPEYQ EKILGEAIIR
ETFKVSKVGT IGGFMVINGK VTRDSSVRVI RDGVVIFDGK LASLKHYKDD VKEVGNAQEG
GLMIENYNDL KEDDTIEAYI MEEIKRK
