IF2_LEVBA
ID IF2_LEVBA Reviewed; 780 AA.
AC Q03QT5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=LVIS_1335;
OS Levilactobacillus brevis (strain ATCC 367 / BCRC 12310 / CIP 105137 / JCM
OS 1170 / LMG 11437 / NCIMB 947 / NCTC 947) (Lactobacillus brevis).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Levilactobacillus.
OX NCBI_TaxID=387344;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 367 / BCRC 12310 / CIP 105137 / JCM 1170 / LMG 11437 / NCIMB
RC 947 / NCTC 947;
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}.
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; CP000416; ABJ64437.1; -; Genomic_DNA.
DR RefSeq; WP_011668010.1; NC_008497.1.
DR AlphaFoldDB; Q03QT5; -.
DR SMR; Q03QT5; -.
DR STRING; 387344.LVIS_1335; -.
DR PRIDE; Q03QT5; -.
DR EnsemblBacteria; ABJ64437; ABJ64437; LVIS_1335.
DR KEGG; lbr:LVIS_1335; -.
DR PATRIC; fig|387344.15.peg.1269; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001652; 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.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis; Reference proteome.
FT CHAIN 1..780
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008258"
FT DOMAIN 281..450
FT /note="tr-type G"
FT REGION 24..194
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..297
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 315..319
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 336..339
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 390..393
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 426..428
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 54..70
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 78..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..170
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 173..192
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 290..297
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 336..340
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 390..393
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 780 AA; 85858 MW; 2D0B157D5EB853B2 CRC64;
MGKKRIYELA KEINVSSKQI IAKAEEKGFP VKNHMSTLGE NEERQLRAAF KPQAKTSHEQ
SAASAQPQRK VQQPRREKSQ GTARTQTTAQ KPAGKPANQT QRNNNNKNNG QTGNRQHEQQ
HSGTGRFGGS LNNNTNNSNG RRNSNNSNSR GGRNSRNNRN NRRRNNNNNN RYKKNQRIKD
TNQHKGAPER KNKALPEVLV YTDGMNAQDL AKILHRSSAE IVKKLFMLGV MVNQNQSLDK
DTIEILADDY GIQAQEKVEV DVTDIDKFFD AEMANKDFEA PRAPVVTIMG HVDHGKTTLL
DHLRHSHITD GEAGGITQAI GAYQVHYNDK VITFLDTPGH AAFTEMRARG AEITDITVLV
VAADDGVMPQ TIEAIHHAKA AGTPIIVAVN KIDKPGANPN HVMEQLTEYE LIPEDWGGDT
IFVEISAKFG KNIDELLDMI LLQSDVLELK ANPKQNGVGS VIEARLDQGK GSVATLLVQQ
GTLHVGDPIV VGNTFGRVRT MVNERGRRIK DATPSTPVEI TGLNDVPEAG DRFVVFDDEK
TARAAGEERA KEALVKERRN TSHVTLDNLF DSLKEGEMKE VDVIIKADVQ GSVEALAGSL
KKIDVSGVRV NIIHSAVGAI NESDVTLAEA SDAIIIGFNV RPTPQARAQA DSDKVDIRLH
NVIYNAIDEI ETAMKGLLEP TYEEEIIGEV EVKDIFHASK VGTIVGGMVT EGYVTSESDV
RLIRDGVVIY EGKLGSLKRF KDDVKQVKMG YELGLTIENY NDVKVGDVIE AYVMKEVPVK
