IF2_STRPN
ID IF2_STRPN Reviewed; 958 AA.
AC Q97S57;
DT 10-OCT-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=SP_0556;
OS Streptococcus pneumoniae serotype 4 (strain ATCC BAA-334 / TIGR4).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=170187;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-334 / TIGR4;
RX PubMed=11463916; DOI=10.1126/science.1061217;
RA Tettelin H., Nelson K.E., Paulsen I.T., Eisen J.A., Read T.D.,
RA Peterson S.N., Heidelberg J.F., DeBoy R.T., Haft D.H., Dodson R.J.,
RA Durkin A.S., Gwinn M.L., Kolonay J.F., Nelson W.C., Peterson J.D.,
RA Umayam L.A., White O., Salzberg S.L., Lewis M.R., Radune D.,
RA Holtzapple E.K., Khouri H.M., Wolf A.M., Utterback T.R., Hansen C.L.,
RA McDonald L.A., Feldblyum T.V., Angiuoli S.V., Dickinson T., Hickey E.K.,
RA Holt I.E., Loftus B.J., Yang F., Smith H.O., Venter J.C., Dougherty B.A.,
RA Morrison D.A., Hollingshead S.K., Fraser C.M.;
RT "Complete genome sequence of a virulent isolate of Streptococcus
RT pneumoniae.";
RL Science 293:498-506(2001).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AE005672; AAK74712.1; -; Genomic_DNA.
DR PIR; G95064; G95064.
DR RefSeq; WP_000039196.1; NZ_AKVY01000001.1.
DR AlphaFoldDB; Q97S57; -.
DR SMR; Q97S57; -.
DR STRING; 170187.SP_0556; -.
DR EnsemblBacteria; AAK74712; AAK74712; SP_0556.
DR KEGG; spn:SP_0556; -.
DR eggNOG; COG0532; Bacteria.
DR eggNOG; COG3064; Bacteria.
DR OMA; CHICSIW; -.
DR PhylomeDB; Q97S57; -.
DR BioCyc; SPNE170187:G1FZB-576-MON; -.
DR Proteomes; UP000000585; 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..958
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137263"
FT DOMAIN 460..627
FT /note="tr-type G"
FT REGION 50..224
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 288..374
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 469..476
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 494..498
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 515..518
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 569..572
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 605..607
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 64..84
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..122
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 132..159
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 160..184
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 292..326
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 327..361
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 469..476
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 515..519
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 569..572
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 958 AA; 105810 MW; 3A0725BCC8E65D38 CRC64;
MSKKRLYEIA KELGKESKEV VARAKELGLD VKSHSSSVEE AVAAKIAASF KPAAAPKVEA
KPAAPKVSAE KKAEKSEPAK PAVAKEEAKP AAPKASAEKK AEKSEPVKPA VAKEEAKPAE
PVTPKTEKVA AKPQSRNFKA EREARAKEQA ERRKQNKGNN RDQQQNGNRQ KNDGRNGGKQ
GQSNRDNRRF NDQAKKQQGQ QKRRNERRQQ EDKRSNQAAP RIDFKARAAA LKAEQNAEYA
RSSEERFKQY QAAKEALAQA NKRKEPEEIF EEAAKLAEQA QQVQAVVEVV PEKKEPAVDT
RRKKQARPDK NRDDYDHEED GPRKQQKNRS SQNQVRNQKN SNWNNNKKNK KGNNKNNRNQ
TPKPVTERKF HELPTEFEYT DGMTVAEIAK RIKREPAEIV KKLFMMGVMA TQNQSLDGET
IELLMVDYGI EAKQKVEVDN ADIERFFVED GYLNEDELVE RPPVVTIMGH VDHGKTTLLD
TLRNSRVATG EAGGITQHIG AYQIVENGKK ITFLDTPGHA AFTSMRARGA SVTDITILVV
AADDGVMPQT IEAINHSKAA NVPIIVAINK IDKPGANPER VIGELAEHGV MSTAWGGDSE
FVEISAKFNQ NIEELLETVL LVAEIQELKA DPTVRAIGTV IEARLDKGKG AVATLLVQQG
TLNVQDPIVV GNTFGRVRAM TNDLGRRVKV AGPSTPVSIT GLNEAPMAGD HFAVYEDEKS
ARAAGEERAK RALMKQRQAT QRVSLENLFD TLKAGELKSV NVIIKADVQG SVEALSASLQ
KIDVEGVKVT IVHSAVGAIN ESDVTLAEAS NAFIVGFNVR PTPQARQQAE ADDVEIRLHS
IIYKVIEEME EAMKGMLDPE FEEKVIGEAV IRETFKVSKV GTIGGFMVIN GKVARDSKVR
VIRDGVVIYD GELASLKHYK DDVKEVTNGR EGGLMIDGYN DIKMDDVIEA YVMEEIKR
