IF2_LISW6
ID IF2_LISW6 Reviewed; 780 AA.
AC A0AIC6;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 28-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=lwe1340;
OS Listeria welshimeri serovar 6b (strain ATCC 35897 / DSM 20650 / CIP 8149 /
OS NCTC 11857 / SLCC 5334 / V8).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=386043;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35897 / DSM 20650 / CIP 8149 / NCTC 11857 / SLCC 5334 / V8;
RX PubMed=16936040; DOI=10.1128/jb.00758-06;
RA Hain T., Steinweg C., Kuenne C.T., Billion A., Ghai R., Chatterjee S.S.,
RA Domann E., Kaerst U., Goesmann A., Bekel T., Bartels D., Kaiser O.,
RA Meyer F., Puehler A., Weisshaar B., Wehland J., Liang C., Dandekar T.,
RA Lampidis R., Kreft J., Goebel W., Chakraborty T.;
RT "Whole-genome sequence of Listeria welshimeri reveals common steps in
RT genome reduction with Listeria innocua as compared to Listeria
RT monocytogenes.";
RL J. Bacteriol. 188:7405-7415(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; AM263198; CAK20758.1; -; Genomic_DNA.
DR RefSeq; WP_011702142.1; NC_008555.1.
DR AlphaFoldDB; A0AIC6; -.
DR SMR; A0AIC6; -.
DR STRING; 386043.lwe1340; -.
DR EnsemblBacteria; CAK20758; CAK20758; lwe1340.
DR GeneID; 61189217; -.
DR KEGG; lwe:lwe1340; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000000779; 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..780
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008265"
FT DOMAIN 281..450
FT /note="tr-type G"
FT REGION 44..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 64..166
FT /note="Polar 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; 84719 MW; 50457A13380F1006 CRC64;
MSKVRVYEYA KEHQVSSKKV IEALKDLGIE VANHMSTINE NALRQLDNAV DGTNKKAEAP
KKETTSNENG NSKGPNKPNM TNSNEKSNKP NKPAGQATKP ATANKSQGAK PATNKPANTS
NQTQSSGNQQ QAGGQKRNNN SNRPGGGNSN RPGGNNRPNR GGNFNNKGRN TKKKGKLNHS
TVPPTPPKPK ELPEKIVFSE SLTVAELAKK LYREPSELIK KLFMLGVVAT INQSLDKDAI
ELICDDYGVQ VEEEIKVDVT DLDVYFENEL NETVDESKLV ERPPVVTIMG HVDHGKTTLL
DSLRNTKVTL GEAGGITQHI GAYQLEIHDK KITFLDTPGH AAFTAMRARG AQITDITILV
VAADDGVMPQ TIEAINHAKA AGMPIIVAVN KIDKPQANPD RVMQELTEYE LVPEAWGGDT
IFAPISAKFG EGLENLLDMI LLVSEVEELK ANPNRRAIGS VIEAELDKGR GPVATLLVQD
GTLNIGDPIV VGNTFGRVRA MVNDLGRRVK KVGPSTPVEI TGLNDVPQAG DRFVVFEDEK
TARNIGETRA SRALVAQRSA TNRVSLDNLF EHMKAGEMKE VNVIIKADVQ GSVEALAASL
RKIDVEGVNV KIIHTAVGAI NESDITLAAA SNAIVIGFNV RPTAQAREAA ENESVDIRLH
RVIYKAIDEI EAAMKGMLDP EFQEKIIGQA QVRQTINVSK VGTIAGCYVT DGKITRDSGV
RIIRDGIVVF EGEIATLKRF KDDAKEVAKG YECGITVQNF NDIKEDDVIE AYVMEEIERK
