IF2_STACT
ID IF2_STACT Reviewed; 707 AA.
AC B9DPF5;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Sca_0904;
OS Staphylococcus carnosus (strain TM300).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=396513;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TM300;
RX PubMed=19060169; DOI=10.1128/aem.01982-08;
RA Rosenstein R., Nerz C., Biswas L., Resch A., Raddatz G., Schuster S.C.,
RA Goetz F.;
RT "Genome analysis of the meat starter culture bacterium Staphylococcus
RT carnosus TM300.";
RL Appl. Environ. Microbiol. 75:811-822(2009).
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; AM295250; CAL27813.1; -; Genomic_DNA.
DR RefSeq; WP_015900154.1; NC_012121.1.
DR AlphaFoldDB; B9DPF5; -.
DR SMR; B9DPF5; -.
DR STRING; 396513.SCA_0904; -.
DR GeneID; 60545401; -.
DR KEGG; sca:SCA_0904; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR BioCyc; SCAR396513:SCA_RS04560-MON; -.
DR Proteomes; UP000000444; 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..707
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000190633"
FT DOMAIN 209..378
FT /note="tr-type G"
FT REGION 32..125
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 218..225
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 243..247
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 264..267
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 318..321
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 354..356
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 40..76
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 101..115
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 218..225
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 264..268
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 318..321
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 707 AA; 78174 MW; 4A600F634D5E855D CRC64;
MSKQRIYEYA KDLNLKSKDV IDELKKMNVE VSNHMQALEP NEIKELDKKF KPGSSKDKQD
NKAAQNNHKK HQNNNKDKNN NNNGGNAKKN NKKNHNNKNQ KNNKNNKNNK NQKQAPKQEA
VKEMPEKITY TEGITVGELA EKMNIESSNI VKKLFLLGIM ANINQSLDDE TVELIADDYG
IEIEKEVVID EEDLDIYFDD EEEDPDAIER PAVVTIMGHV DHGKTTLLDS IRNTHVTEGE
AGGITQHIGA YQIENDGKKI TFLDTPGHAA FTTMRARGAQ VTDITILVVA ADDGVMPQTI
EAINHAKEAD VPIIVAVNKV DKPTANPDRV MQELTEYGLF PEDWGGDTIF VPLSALSGDG
IDDLLEMIVL VSEVQELKAN PEKRAVGTVI EAELDKSRGP AASLLVQNGT LNVGDAIVVG
NTYGRVRAMV NDAGKRVKSA GPSTPVEITG INDVPQAGDR FVTFSDEKQA RRIGEARHEE
SIIQQRQESK NVSLDNLFEQ MKQGEMKDLN IIIKGDVQGS VEALAASLMK IDVEGVNVRI
IHTAVGAINE SDVTLANASN GIIIGFNVRP DSGAKRAAEQ ENVDMRLHRV IYNVIEEIEA
AMKGMLDPEY EEKVIGQAEV RQTFKVSKVG TIAGCYVTDG KITRNAGVRV IRDGIVVFEG
QLDTLKRFKD DVKEVAQGYE CGITIEKFND IKVDDIIEAY EMVEIQR
