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Database: UniProt
Entry: Q044B7
LinkDB: Q044B7
Original site: Q044B7 
ID   IF2_LACGA               Reviewed;         882 AA.
AC   Q044B7;
DT   20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 97.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=LGAS_0814;
OS   Lactobacillus gasseri (strain ATCC 33323 / DSM 20243 / BCRC 14619 / CIP
OS   102991 / JCM 1131 / KCTC 3163 / NCIMB 11718 / NCTC 13722 / AM63).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=324831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 33323 / DSM 20243 / BCRC 14619 / CIP 102991 / JCM 1131 / KCTC
RC   3163 / NCIMB 11718 / NCTC 13722 / AM63;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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; CP000413; ABJ60205.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q044B7; -.
DR   SMR; Q044B7; -.
DR   KEGG; lga:LGAS_0814; -.
DR   HOGENOM; CLU_006301_5_0_9; -.
DR   Proteomes; UP000000664; 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; cd01887; IF2_eIF5B; 1.
DR   CDD; cd03702; IF2_mtIF2_II; 1.
DR   CDD; cd03692; mtIF2_IVc; 1.
DR   Gene3D; 1.10.10.2480; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 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   NCBIfam; TIGR00487; IF-2; 1.
DR   NCBIfam; TIGR00231; small_GTP; 1.
DR   PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR   Pfam; PF00009; GTP_EFTU; 1.
DR   Pfam; PF11987; IF-2; 1.
DR   Pfam; PF04760; IF2_N; 2.
DR   SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 2.
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..882
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000335481"
FT   DOMAIN          383..552
FT                   /note="tr-type G"
FT   REGION          50..299
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          392..399
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          417..421
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          438..441
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          492..495
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          528..530
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        63..98
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        109..186
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        234..264
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        279..297
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         392..399
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         438..442
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         492..495
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   882 AA;  98854 MW;  1856D4098F9D150A CRC64;
     MMAKKRIYEV AKELGIENKI VVKKAQDLGF DVKSHMSSLD DKQVSKLVDS FKSANTTKPS
     TEKDSKNSSR KEKTKIKVSV GAIRRRDNKN DHDNRHGNNK RRNNKFKKQQ NDRRAERNKP
     QTEAKSAARD LLNKFKKKQR AEASELNAQT EASRRKWHQE QNPQRSKVKK VENTRKPKEE
     KLEGAAAVKA RVQASQKPVG PKIIKPSPAR NKAKRPTVKK VEPIAPVVPA PQKEETKPTR
     KKDFTRKKRE VPDYERERSE HSDKARRRRN KKNKRINQSK EIKKQPTQRK ERPLPETLVY
     EEGMNAQDLG KLLHREPAEI VKKLFMLGVM TNQNQSLDKD TIELLAAEYG IEAQEKVHED
     ISDIDTLYTK EMEESKASKH QEKRPPVVTI MGHVDHGKTT LLDRLRHTNV SEHEAGGITQ
     KIGAYQVRID DRLITFLDTP GHAAFSNMRA RGAEITDIVV LVVAADDGVM PQTIEAIDHA
     KSAGVPIIVA VNKIDKPGAN PDHVMEQLMK YGLVPEDWGG DTIFVKISAK TGKNVEELLQ
     MILLQADVME LKADPDQKAI GTVIEARLDK GRGSVADVLV QQGTLKVGDP IVVGDTFGRV
     RVMTNDKGRR VKKATPSAPV EITGLNDVPE AADKLVVFED EKTARSVGEQ RAKNALEKQR
     ENVQHVTLDN LFDTMKKENM KEVDIVLKAD VQGSAEALQQ SLEKIEVEGV RVNIIHSGVG
     AINESDVTLA GASNAFIVGF NVRPTNTAKS QADAEGVDIR LYNIIYKVMD DVEAAMKGML
     EPTYEEKVTG NLTVRETWKV SKIGTIAGAF VDNGYVTRDS GIRVIRDGIV KYDGKVASLK
     RFKDDVKEVK QGFDCGITIE NFNDIKVDDQ LEAYEMQEVP VK
//
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