IF2_MYCPA
ID IF2_MYCPA Reviewed; 925 AA.
AC Q73VV4;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=MAP_2907c;
OS Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS (Mycobacterium paratuberculosis).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium avium complex (MAC).
OX NCBI_TaxID=262316;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-968 / K-10;
RX PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA Kanjilal S., Kapur V.;
RT "The complete genome sequence of Mycobacterium avium subspecies
RT paratuberculosis.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(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; AE016958; AAS05224.1; -; Genomic_DNA.
DR RefSeq; WP_010949773.1; NC_002944.2.
DR AlphaFoldDB; Q73VV4; -.
DR SMR; Q73VV4; -.
DR STRING; 262316.MAP_2907c; -.
DR EnsemblBacteria; AAS05224; AAS05224; MAP_2907c.
DR KEGG; mpa:MAP_2907c; -.
DR PATRIC; fig|262316.17.peg.3082; -.
DR eggNOG; COG0481; Bacteria.
DR HOGENOM; CLU_006301_9_3_11; -.
DR OMA; QVRPEMI; -.
DR Proteomes; UP000000580; 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.
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..925
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228214"
FT DOMAIN 421..592
FT /note="tr-type G"
FT REGION 52..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 98..326
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 430..437
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 455..459
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 480..483
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 534..537
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 570..572
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 130..171
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 188..239
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 430..437
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 480..484
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 534..537
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 925 AA; 96526 MW; 84B6E78A51B3A852 CRC64;
MAGKARVHEL AKELGVTSKE VLARLNEQGE FVKSASSTVE APVARRLRES FGGGKAAEGA
AKAPAKAAAK GDAKTAAKGD VKAPDKALDA ALDNAIKAGG NGEAAAPPAQ PGGTATTPAA
QATPEAPARP GPAAARPSAP APGQPKPPAP GQPPRPGATP GPRPGPAPKP AARTPRVGNN
PFSSAQPVDR PIPRPVPRPG APRPGAPRPG ASPGNMPPRP GGVGGPGRPA RPGAPRPGGG
RPGGPGGRDG GGGNYRGGGV GASPGGGGGF RGRPGGGGGG RPGQRGGAAG AFGRPGGAPR
RGRKSKRQKR QEYDSMQAPV VGGVRLPHGN GETIRLARGA SLSDFAEKID ANPASLVQAL
FNLGEMVTAT QSVGDETLEL LGSEMNYNVQ VVSPEDEDRE LLESFDLTYG EDEGTEEDLQ
TRPPVVTVMG HVDHGKTRLL DTIRKANVRE AEAGGITQHI GAYQVTVEHD GVERPITFID
TPGHEAFTAM RARGAKATDI AILVVAADDG VMPQTVEAIN HAQAADVPIV VAVNKIDVEG
ADPQKIRGQL TEYGLVPEEF GGDTMFVDIS AKQGTNIDQL LEAVLLTADA ALDLRANPDM
EAQGVAIEAH LDRGRGPVAT VLIQRGTLRV GDSIVAGDAY GRVRRMVDEH GDDVEEALPS
RPVQVIGFTS VPGAGDNLLV VDEDRIARQI ADKRSARKRN ALAARSRKRI SLEDLDSALK
ETSQLNLILK GDNAGTVEAL EEALMGIQID DEVALRVIDR GVGGITETNV NLASASDAVI
IGFNVRAEGK ATELANREGV EIRYYSVIYQ AIDEIEKALR GMLKPIYEEN QLGRAEIRAI
FRSSKVGIIA GCMITSGVVR RNAKARLLRD NVVVSENLTI NSLRREKDDV TEVREGFECG
MTLGYSDIKE GDVIESYELV QKERT
