IF2_LACAC
ID IF2_LACAC Reviewed; 877 AA.
AC Q5FJN6;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=LBA1255;
OS Lactobacillus acidophilus (strain ATCC 700396 / NCK56 / N2 / NCFM).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lactobacillus.
OX NCBI_TaxID=272621;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700396 / NCK56 / N2 / NCFM;
RX PubMed=15671160; DOI=10.1073/pnas.0409188102;
RA Altermann E., Russell W.M., Azcarate-Peril M.A., Barrangou R., Buck B.L.,
RA McAuliffe O., Souther N., Dobson A., Duong T., Callanan M., Lick S.,
RA Hamrick A., Cano R., Klaenhammer T.R.;
RT "Complete genome sequence of the probiotic lactic acid bacterium
RT Lactobacillus acidophilus NCFM.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:3906-3912(2005).
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; CP000033; AAV43088.1; -; Genomic_DNA.
DR RefSeq; WP_011254396.1; NC_006814.3.
DR RefSeq; YP_194119.1; NC_006814.3.
DR AlphaFoldDB; Q5FJN6; -.
DR SMR; Q5FJN6; -.
DR STRING; 272621.LBA1255; -.
DR PRIDE; Q5FJN6; -.
DR EnsemblBacteria; AAV43088; AAV43088; LBA1255.
DR GeneID; 56942846; -.
DR KEGG; lac:LBA1255; -.
DR PATRIC; fig|272621.13.peg.1190; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_0_9; -.
DR OMA; NRDNRTG; -.
DR BioCyc; LACI272621:G1G49-1238-MON; -.
DR Proteomes; UP000006381; 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..877
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228205"
FT DOMAIN 378..547
FT /note="tr-type G"
FT REGION 48..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..394
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 412..416
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 433..436
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 487..490
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 523..525
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 75..93
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 103..119
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 137..189
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 274..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 387..394
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 433..437
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 487..490
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 877 AA; 98134 MW; 6A846D80C4B6FD32 CRC64;
MAKKRIYEVA KEVGVDNKVV VQKAKDLGFD VKNHMSSIDD SQVAKLKSSF QNSAPAEKKA
EKSATKNNKI KISVSSIRKN EKKPEENNTP KKSNRRRNNK RRSSDRARDN KERDAKSNTG
RPKAAALLQQ FKQKQRAEEG QLNREAQKAK KEYHEHLKHP KKEQSEKDNK KTVKESNNKK
VEQQVEKKVI GPKILKPSPA RLKKNQPADN KEKVTTPRVT IPEAPKEEKR GNGRGRNMGK
PGRKGKNQFV NGHSERSDRS ERKRRKNKKH QQEQQKPRKQ ITKRKERPLP DILVYEEGMN
AQDIGKLIHR EPAEIVKKLF MLGVMTNQNQ SLDKDTIELL AAEYGIDAKQ KVHEDISDID
TLYDKRMEAS KKSKNQIKRP PVVTIMGHVD HGKTTLLDRL RHTHVSAHEA GGITQRIGAY
QVRLDDRLIT FLDTPGHAAF SNMRARGAEI TDIVVLVVAA DDGVMPQTVE AIDHAKSANV
PIIVAINKMD KPGANPQHVT EELMKYNLIP EDYGGDTIFV NISAKTGQNV DDLLQMILLQ
ADVMELKANP DEMAIGTVIE ARLSRGRGPV ADVLIQQGTL NIGDPIVVGD TFGRVRTMTN
DRGRQVKKAT PSEPVEITGL NDVPESADKL VEFKDEKTAR SVGEARAQQS LQKSRENVQH
VTLDNLFDTM KKENMKEVDI VLKADVQGSV EALQQSLEKI EVEGVRVNII HSGVGAINES
DVTLAGASNA FIIGFNVRPT ATAKSQAETD GVDIRLYSII YKAIDDVTAA MKGMLEPTYE
EKVIGNLTVR ETWKVSKVGT IAGSFVDKGI VKNDSKIRVI RDGIVKYDGE IASLKRFKDD
VKEVKQGNDC GLTIKDYNDI KVGDEFEVYE MQQVEPK
