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IF2_STRA5
ID   IF2_STRA5               Reviewed;         927 AA.
AC   Q8E1H3;
DT   28-MAR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2003, sequence version 1.
DT   03-AUG-2022, entry version 118.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=SAG0381;
OS   Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=208435;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-611 / 2603 V/R;
RX   PubMed=12200547; DOI=10.1073/pnas.182380799;
RA   Tettelin H., Masignani V., Cieslewicz M.J., Eisen J.A., Peterson S.N.,
RA   Wessels M.R., Paulsen I.T., Nelson K.E., Margarit I., Read T.D.,
RA   Madoff L.C., Wolf A.M., Beanan M.J., Brinkac L.M., Daugherty S.C.,
RA   DeBoy R.T., Durkin A.S., Kolonay J.F., Madupu R., Lewis M.R., Radune D.,
RA   Fedorova N.B., Scanlan D., Khouri H.M., Mulligan S., Carty H.A.,
RA   Cline R.T., Van Aken S.E., Gill J., Scarselli M., Mora M., Iacobini E.T.,
RA   Brettoni C., Galli G., Mariani M., Vegni F., Maione D., Rinaudo D.,
RA   Rappuoli R., Telford J.L., Kasper D.L., Grandi G., Fraser C.M.;
RT   "Complete genome sequence and comparative genomic analysis of an emerging
RT   human pathogen, serotype V Streptococcus agalactiae.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:12391-12396(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. {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; AE009948; AAM99287.1; -; Genomic_DNA.
DR   RefSeq; NP_687415.1; NC_004116.1.
DR   RefSeq; WP_000039156.1; NC_004116.1.
DR   AlphaFoldDB; Q8E1H3; -.
DR   SMR; Q8E1H3; -.
DR   STRING; 208435.SAG0381; -.
DR   PRIDE; Q8E1H3; -.
DR   EnsemblBacteria; AAM99287; AAM99287; SAG0381.
DR   KEGG; sag:SAG0381; -.
DR   PATRIC; fig|208435.3.peg.376; -.
DR   HOGENOM; CLU_006301_5_0_9; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000000821; 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..927
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000137259"
FT   DOMAIN          428..597
FT                   /note="tr-type G"
FT   REGION          27..337
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:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         483..487
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         537..540
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   927 AA;  102429 MW;  EE47D3E177F87E56 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 GQKQTRNKKN
     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
 
 
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