IF2_KLEP3
ID IF2_KLEP3 Reviewed; 896 AA.
AC B5XSX4;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 25-NOV-2008, 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=KPK_0546;
OS Klebsiella pneumoniae (strain 342).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=507522;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=342;
RX PubMed=18654632; DOI=10.1371/journal.pgen.1000141;
RA Fouts D.E., Tyler H.L., DeBoy R.T., Daugherty S., Ren Q., Badger J.H.,
RA Durkin A.S., Huot H., Shrivastava S., Kothari S., Dodson R.J., Mohamoud Y.,
RA Khouri H., Roesch L.F.W., Krogfelt K.A., Struve C., Triplett E.W.,
RA Methe B.A.;
RT "Complete genome sequence of the N2-fixing broad host range endophyte
RT Klebsiella pneumoniae 342 and virulence predictions verified in mice.";
RL PLoS Genet. 4:E1000141-E1000141(2008).
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; CP000964; ACI07533.1; -; Genomic_DNA.
DR AlphaFoldDB; B5XSX4; -.
DR SMR; B5XSX4; -.
DR PRIDE; B5XSX4; -.
DR EnsemblBacteria; ACI07533; ACI07533; KPK_0546.
DR KEGG; kpe:KPK_0546; -.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001734; 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.
FT CHAIN 1..896
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093794"
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; 98074 MW; C967DEB3C377321B CRC64;
MTDVTIKALA SEIQTSVDRL IQQFADAGIR KSADDSVTAQ 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 AVNRDVIIGE 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
