IF2_LACLM
ID IF2_LACLM Reviewed; 950 AA.
AC A2RM37;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, 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=llmg_1792;
OS Lactococcus lactis subsp. cremoris (strain MG1363).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus; Lactococcus cremoris subsp. cremoris.
OX NCBI_TaxID=416870;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MG1363;
RX PubMed=17307855; DOI=10.1128/jb.01768-06;
RA Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA van Sinderen D., Kok J.;
RT "The complete genome sequence of the lactic acid bacterial paradigm
RT Lactococcus lactis subsp. cremoris MG1363.";
RL J. Bacteriol. 189:3256-3270(2007).
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; AM406671; CAL98364.1; -; Genomic_DNA.
DR RefSeq; WP_011835571.1; NZ_WJVF01000003.1.
DR AlphaFoldDB; A2RM37; -.
DR SMR; A2RM37; -.
DR STRING; 416870.llmg_1792; -.
DR EnsemblBacteria; CAL98364; CAL98364; llmg_1792.
DR KEGG; llm:llmg_1792; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_0_9; -.
DR OMA; NRDNRTG; -.
DR PhylomeDB; A2RM37; -.
DR BioCyc; LLAC416870:LLMG_RS08985-MON; -.
DR Proteomes; UP000000364; 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..950
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335482"
FT DOMAIN 448..619
FT /note="tr-type G"
FT REGION 128..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 457..464
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 482..486
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 503..506
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 557..560
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 595..597
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 128..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..249
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..288
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 289..316
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 321..354
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 457..464
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 503..507
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 557..560
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 950 AA; 104581 MW; B33801D053BA19A5 CRC64;
MSDKKRINQI AKETGLSNTE LVATAQSLGF EVKSHSSSVT AEQAEKIIQG VKTGTDTIVK
PAEKTVKAKI KTVPETAKSK QEDHPRTFAG KAVVEDPAIL ARIKEKEEAK KAAKTEAEPI
EEVITTEKPK VAEPVKKSEP KAAAKAEETK VEKVEAKAKT VTPKAEVKTE NVADKKEPVV
TEEKKKSLTQ KPRIQIKVIK RAEDIKKEQA AARPEKKKFD KNRNDRNNRN DNRRPNQNGN
GQGHSQGGNH YDKNRPAGQG QNQGQKRDKF ASSGSSSTSD TFTPAASGKN NRRDRDRKKT
DSNRDNTKDG NRKGGPLRVN DNRNQVRNAR NSNWNQKGGR GRYQNNQSSS VPATQRKFHE
LPESLEYEVG MNVQDIAKSI KREPAEIIKK LFMMGTMVNQ NQSLDEDTIE LILMDYGVTP
LKKVEEDKSD IERLFVEDGY LNEDKMVERP AVVTIMGHVD HGKTTLLDRF RESRVTEGEA
GGITQHIGAY QIKTNGKKIT FLDTPGHEAF TSMRARGASV TDITILVVAA DDGVMPQTIE
AINHSKAAGV PIIVAINKID KPGANPQRVT QELTEHGVFP VAWDPENGSE FVEISAKFNQ
NLEELLDTVL LVAEVQELKA DPSVRAIGTV VEARLDQGKG AIATLLVQQG TLHIQDPIVV
GNTYGRVRTM TNDLGRRIKE AGPSTPIELT GLSDVPQAGD HFAVFEDEKA ARAAGEERAK
RAQLIKRQNT RRVNLDNLFD TLKEGQTKSV NIIIKADVQG SAEALAASLQ KIEVEGVKVD
IVHSAVGAIS ESDISLAAAS NAIIIGFNVR PTGLAREQAA QEEVDIRLHS IIYKVIEEVE
TAMRGMLDPE FKEEIIGEAI VRETFNVSKV GTIAGFMVIR GKVTRDASVR VIREGVVIHD
GAIASLKHFK DDVKEVGNAQ EGGLMVEDFN DVEIDDTFEV YKMVEIERKK
