IF2_CORA7
ID IF2_CORA7 Reviewed; 905 AA.
AC C3PH19;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 16-JUN-2009, sequence version 1.
DT 03-AUG-2022, entry version 79.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=cauri_1530;
OS Corynebacterium aurimucosum (strain ATCC 700975 / DSM 44827 / CIP 107346 /
OS CN-1) (Corynebacterium nigricans).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=548476;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700975 / DSM 44827 / CIP 107346 / CN-1;
RX PubMed=20137072; DOI=10.1186/1471-2164-11-91;
RA Trost E., Gotker S., Schneider J., Schneiker-Bekel S., Szczepanowski R.,
RA Tilker A., Viehoever P., Arnold W., Bekel T., Blom J., Gartemann K.H.,
RA Linke B., Goesmann A., Puhler A., Shukla S.K., Tauch A.;
RT "Complete genome sequence and lifestyle of black-pigmented Corynebacterium
RT aurimucosum ATCC 700975 (formerly C. nigricans CN-1) isolated from a
RT vaginal swab of a woman with spontaneous abortion.";
RL BMC Genomics 11:91-91(2010).
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; CP001601; ACP33123.1; -; Genomic_DNA.
DR RefSeq; WP_010190332.1; NZ_ACLH01000084.1.
DR AlphaFoldDB; C3PH19; -.
DR SMR; C3PH19; -.
DR STRING; 548476.cauri_1530; -.
DR EnsemblBacteria; ACP33123; ACP33123; cauri_1530.
DR GeneID; 31924160; -.
DR KEGG; car:cauri_1530; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_0_11; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000002077; 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 PRINTS; PR00315; ELONGATNFCT.
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..905
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000118757"
FT DOMAIN 401..575
FT /note="tr-type G"
FT REGION 50..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 410..417
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 435..439
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 460..463
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 514..517
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 550..552
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 89..123
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 288..302
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 410..417
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 460..464
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 514..517
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 905 AA; 94792 MW; FBE5F5F80691C941 CRC64;
MPGKLRVHEL AKQLGVTSKE LLATLKEQGE FVKTASSTIE PPVIKKMRAH YEAKGGEDKA
AEKNAPAATP ASASKKPTEK KPATAAKPGP KPSAAPKPGA APKPGGAPKP GGAPKPGATP
KPGGAPKPGA QRKNTEKGSE RAVTPRSMPK PGGTRRVANN PFSTGSSSDR PSPGPRPGGT
KGQRSAGKPG DNRGGKGGAR PQGDGNRSGG RRPSPAMMPS HPNPASMPSK AAGSGGGGRG
RGGRGGGPGH GGPGHGGFRG RGGRRGGTAG AFGRPGGAPR RGKKSKRQKR HEFEEQQKHE
VGGVRLPDGG GKVVRLRRGA SLADFAEKIG ADPAALVQAL FNLGEMVTAT ASVSEDTLQL
LGSEINYEVQ VVSPEDEDRE LLESFDLQFG EDEGGEEALE KRPPVVTVMG HVDHGKTRLL
DTIRKTNEGA GEAGGITQGI GAYQTTVDLE DGPRTITFLD TPGHEAFTAM RARGAKSTDL
AILVVAADDG VMPQTIEAIN HAKAADIPVV VAVNKIDKPE ASPDKIRGQL TEYGLVPEEY
GGDTMFVDIS AKNNINIDDL LEAVILTADA ALELTANPDM DAQGSAIEAH LDRGRGPVAT
VIIQRGTLRI GDSIVVGDAH GRVRRMLDEF GNDVEEAGPS RPVQVQGLNG VPGAGDNLLV
VEDDRVARQI AAQRDARKRS ALQAKARKRV SLEDLDAVLK ETSTLNLILK GDNAGSVEAL
EDALLDIEVD DEVQLNIIDR GVGAVTQTNV SLAAASDAII IAFNVRAEGK ATEEANAEGV
DIRYYTVIYR AIEEVEAALK GMLKPIYEER DTGAAEIRAL FKSSAVGTIA GCMVTEGKVK
RNGKVRLVRD GNVITSDAKI ESLRHEKDDA NEINAGYECG MVLSYPDIQV GDIIQAYEEV
EVPRD
