IF2_KLEP7
ID IF2_KLEP7 Reviewed; 896 AA.
AC A6TEI7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 89.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN OrderedLocusNames=KPN78578_35470; ORFNames=KPN_03576;
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578;
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000647; ABR78971.1; -; Genomic_DNA.
DR RefSeq; WP_002918250.1; NC_009648.1.
DR AlphaFoldDB; A6TEI7; -.
DR SMR; A6TEI7; -.
DR STRING; 272620.KPN_03576; -.
DR jPOST; A6TEI7; -.
DR EnsemblBacteria; ABR78971; ABR78971; KPN_03576.
DR KEGG; kpn:KPN_03576; -.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000000265; 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; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR013575; IF2_assoc_dom_bac.
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; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 2.
DR SUPFAM; SSF46955; SSF46955; 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..896
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008257"
FT DOMAIN 395..564
FT /note="tr-type G"
FT REGION 93..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 404..411
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 429..433
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 450..453
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 504..507
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 540..542
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 93..228
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 238..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 404..411
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 450..454
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 504..507
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 896 AA; 98076 MW; 5CA2C8AA3149A001 CRC64;
MTDVTIKALA SEIQTSVDRL IQQFADAGIR KSADDSVTSQ EKQTLLTHLN REHGSAPDKL
TLQRKTRSTL NIPGTGGKSK SVQIEVRKKR TFVKRDPQEA ERLAAEEQAQ REAEEQARRE
AEEAAKREAQ LKAEREAAEQ AKREVADKAK REAAEKDKVS NQHTDEMTKT AQAEKIRREN
EAAELKRKSE EEARRKLEEE ARRVAEEARR MAEENEKNWS ETSDSPEDSS DYHVTTSQHA
RQAEDDNDRE VEGGRGRSRS SKAARPAKKG NKHAESKADR EEARAAVRGG KGGKHRKGSA
LQQGFQKPAQ AVNRDVVIGE TITVGELANK MAVKGSQVIK AMMKLGAMAT INQVIDQETA
QLVAEEMGHK VILRRENELE EAVMSDRDTG AAAEPRAPVV TIMGHVDHGK TSLLDYIRST
KVASGEAGGI TQHIGAYHVE TDNGMITFLD TPGHAAFTSM RARGAQATDI VVLVVAADDG
VMPQTIEAIQ HAKAAQVPVV VAVNKIDKPE ADPDRVKNEL SQYGILPEEW GGESQFVHVS
AKAGTGIDDL LDAILLQAEV LELKAVRNGM ASGAVIESFL DKGRGPVATV LVREGTLHKG
DIVLCGFEYG RVRAMRDELG REVLEAGPSI PVEILGLSGV PAAGDEVTVV RDEKKAREVA
LYRQGKFREV KLARQQKSKL ENMFANMTEG EVHEVNIVLK ADVQGSVEAI SDSLLKLSTD
EVKVKIIGSG VGGITETDAT LAAASNAILV GFNVRADASA RKVIEAESLD LRYYSVIYNL
IDEVKAAMSG MLSPELKQQI IGLAEVRDVF KSPKFGAIAG CMVTEGTIKR HNPIRVLRDN
VVIYEGELES LRRFKDDVNE VRNGMECGIG VKNYNDVRVG DMIEVFEIIE IQRSID
