IF2_ACIB3
ID IF2_ACIB3 Reviewed; 899 AA.
AC B7H115;
DT 14-APR-2009, integrated into UniProtKB/Swiss-Prot.
DT 10-FEB-2009, sequence version 1.
DT 03-AUG-2022, entry version 75.
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=ABBFA_003199;
OS Acinetobacter baumannii (strain AB307-0294).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Acinetobacter; Acinetobacter calcoaceticus/baumannii complex.
OX NCBI_TaxID=557600;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AB307-0294;
RX PubMed=18931120; DOI=10.1128/jb.00834-08;
RA Adams M.D., Goglin K., Molyneaux N., Hujer K.M., Lavender H., Jamison J.J.,
RA MacDonald I.J., Martin K.M., Russo T., Campagnari A.A., Hujer A.M.,
RA Bonomo R.A., Gill S.R.;
RT "Comparative genome sequence analysis of multidrug-resistant Acinetobacter
RT baumannii.";
RL J. Bacteriol. 190:8053-8064(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; CP001172; ACJ57595.1; -; Genomic_DNA.
DR RefSeq; WP_000130326.1; NZ_CP001172.1.
DR AlphaFoldDB; B7H115; -.
DR SMR; B7H115; -.
DR GeneID; 66398680; -.
DR HOGENOM; CLU_006301_6_2_6; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000006924; 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; 1.
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..899
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000117317"
FT DOMAIN 399..568
FT /note="tr-type G"
FT REGION 116..135
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 170..189
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 262..306
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 408..415
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 433..437
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 454..457
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 508..511
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 544..546
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 279..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 408..415
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 454..458
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 508..511
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 899 AA; 97315 MW; EE17C37682DFCBE1 CRC64;
MTDKSIKELA LSVGRPVEKL LEQAREAGLP QRTADDIITT EQQDTLVNYL KKVHGQESGN
TGKIALKRKT TSTAKVASTS GKAKTINVEV RKKQVFAKPN PEQIAAEAKA RAEAEAKARA
EQQAREAAEQ KARLQTEQKA KATLDAMRAA HQQDSAAQSA PKAAVVVKKR GGGTVKPAPK
PAETLEQKKA REAQTAQLKA TEEAARRKAA EEAQQRTLEQ MRKMASKYSN DDATATIRVI
DDSPLASGLV GQAYEDSFNQ EDREIKRGGA TTNPRAGKKG GRRGQEEQSF VNHNKRGLKS
SQANKHGFEK PVKKQVYDVE IGSSIVVADL AQKMAIKVRE VIKTLMKMGE LVNQNQTIDQ
DTAALVVEEM GHNPVLVSDT QAEDNLLEAA EEARGEQTTR PPVVTIMGHV DHGKTSLLDR
IRRSKVAAGE AGGITQHIGA YHVETDKGII TFLDTPGHAA FTSMRARGAK ATDIVVLVVA
ADDGVMPQTA EAIDHARAAG TPIIVAINKM DKESADPDRV LNELTTKEIV PEEWGGDVPV
AKVSAHTGQG IDELLDLILI QSELMELKAS AEGAAQGVVI EARVDKGRGA VTSILVQNGT
LNIGDLVLAG SSYGRVRAMS DENGKPIKSA GPSIPVEILG LPEAPMAGDE VLVVNDEKKA
REVADARADR EREKRIERQS AMRLENIMAS MGKKDVPTVN VVLRTDVRGT LEALNAALHE
LSTDEVKVRV ISSGVGAITE SDVILAESSE AVLLGFNVRA DTAARQKSDQ DGIDIRYYSI
IYELIDDVKD AMSGKLAPEH RETILGVAQV REVFRSSKFG AAAGCMVMEG VIHRNKPIRV
LRDDVVIFQG ELESLRRYKD VVDEVRAGME CGLAVKGYND IKPLDKIEVY DVQMVKRSL
