IF2_BACTN
ID IF2_BACTN Reviewed; 1040 AA.
AC Q8A2A1;
DT 15-DEC-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=BT_3404;
OS Bacteroides thetaiotaomicron (strain ATCC 29148 / DSM 2079 / JCM 5827 /
OS CCUG 10774 / NCTC 10582 / VPI-5482 / E50).
OC Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Bacteroidaceae;
OC Bacteroides.
OX NCBI_TaxID=226186;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29148 / DSM 2079 / JCM 5827 / CCUG 10774 / NCTC 10582 /
RC VPI-5482 / E50;
RX PubMed=12663928; DOI=10.1126/science.1080029;
RA Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C.,
RA Hooper L.V., Gordon J.I.;
RT "A genomic view of the human-Bacteroides thetaiotaomicron symbiosis.";
RL Science 299:2074-2076(2003).
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; AE015928; AAO78510.1; -; Genomic_DNA.
DR RefSeq; NP_812316.1; NC_004663.1.
DR RefSeq; WP_011108813.1; NC_004663.1.
DR AlphaFoldDB; Q8A2A1; -.
DR SMR; Q8A2A1; -.
DR STRING; 226186.BT_3404; -.
DR PaxDb; Q8A2A1; -.
DR PRIDE; Q8A2A1; -.
DR EnsemblBacteria; AAO78510; AAO78510; BT_3404.
DR GeneID; 60924583; -.
DR KEGG; bth:BT_3404; -.
DR PATRIC; fig|226186.12.peg.3472; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_0_1_10; -.
DR InParanoid; Q8A2A1; -.
DR OMA; KPGANTE; -.
DR Proteomes; UP000001414; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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; 1.
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..1040
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137171"
FT DOMAIN 539..709
FT /note="tr-type G"
FT REGION 67..92
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 272..402
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..451
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 548..555
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 573..577
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 595..598
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 649..652
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 685..687
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 214..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 280..346
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 347..392
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 435..451
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 548..555
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 595..599
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 649..652
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1040 AA; 114866 MW; E1D997868E3B3DB8 CRC64;
MTIRLNKVTR DLNVGIATVV EFLQKKGYTV EANPNTKISE EQYAVLVKEF STDKNLRLES
ERFIQERQNK ERNKASVSIE GFEKQQEKPK SEDVIKTVVP EDARPKFKPV GKIDLDKFSG
RRTDKVEKAP EKKVEPVVEQ PVVEQPVAEK TVVEKPVVES EVKKEEPKVE KVEVIAPKPA
PVEQPVVAPK PAVETKPVEV EKVVVEEVKK EEPKVVETAP VKAEERKVER TAEVTATVTT
PTEENASKEN EVFKIRQPEL GAKINVIGQI DLAALNQSTR PKKKSKEEKR REREEKEKVR
QDQKKLMKEA IIKEIRKEDS KQAKPGVKDN NADAARKKRN RINKEKVDVN NVATSNFAAP
RPNTQTGKGG GNHPRPQGQG QGQGNNNNNN KKNNNKDRFK KPVIKQEVSE EDVAKQVKET
LARLTTKGKN KTSKYRKEKR EMASNRMQEL EDQEMAESKV LKLTEFVTAN ELATMMDVSV
NQVIATCMSI GMMVSINQRL DAETINLVAE EFGFKTEYVS AEVAQAIVEE EDAPEDLQPR
APIVTVMGHV DHGKTSLLDY IRKANVIAGE AGGITQHIGA YNVQLEDGRR ITFLDTPGHE
AFTAMRARGA KVTDIAIIIV AADDNVMPQT KEAINHAMAA GVPIVFAINK VDKPTANPDK
IKEELAAMNY LVEEWGGKYQ SQDISAKKGM GVEDLMEKVL LEAEMLDLKA NPNRNATGSI
IESSLDKGRG YVATVLVSNG TLKVGDIVLA GTSYGRVKAM FNERNQRVKE AGPAEPALIL
GLNGAPAAGD TFHVVESDQE AREITNKREQ LAREQGLRTQ KILTLDELGR RIALGNFQEL
NIIVKGDVDG SVEALSDSLI KLSTEQIQVN VIHKGVGAIS ESDVSLAAAS DAIIVGFQVR
PSGAAAKMAE QEGVDIRKYS VIYDAIEEVK AAMEGMLAPE LKEQITATIE IREVFNITKV
GLVAGAVVKT GKVKRSDKAR LIRDGIVIFT GNINALKRFK DDVKEVGTNF ECGISLVNCN
DMKVGDMIET FEEIEVKQTL
