IF2_SERP5
ID IF2_SERP5 Reviewed; 895 AA.
AC A8G907;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 13-NOV-2007, sequence version 1.
DT 03-AUG-2022, entry version 86.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Spro_0489;
OS Serratia proteamaculans (strain 568).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Serratia.
OX NCBI_TaxID=399741;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=568;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Taghavi S., Newman L.,
RA Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of chromosome of Serratia proteamaculans 568.";
RL Submitted (SEP-2007) 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; CP000826; ABV39597.1; -; Genomic_DNA.
DR RefSeq; WP_012004947.1; NC_009832.1.
DR AlphaFoldDB; A8G907; -.
DR SMR; A8G907; -.
DR STRING; 399741.Spro_0489; -.
DR PRIDE; A8G907; -.
DR EnsemblBacteria; ABV39597; ABV39597; Spro_0489.
DR KEGG; spe:Spro_0489; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
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..895
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335512"
FT DOMAIN 394..563
FT /note="tr-type G"
FT REGION 50..217
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 232..302
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 403..410
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 428..432
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 449..452
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 503..506
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 539..541
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 62..82
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 109..217
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 239..261
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..290
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 403..410
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 449..453
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 503..506
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 895 AA; 97586 MW; AEDAE66A36889A14 CRC64;
MTTDVTVKSL AAEIQTPVDR LVQQFADAGI NKSETDSVTQ HEKEALLAHL NREHGSAPGK
LTLQRKTRST LNIPSTGGKS KSVQIEVRKK RTYVNRDTPE AQQAEAAEQA QREAEEQAQR
AAEELAKREA EAKRAAEEQA KREAAEIAKR NSAEKEKVTN QHTDEMTKPA QAEKARREAE
AAELKRKAEE EVRRKVEEDA KRVAEEARRM AEEKGEEWAA AEKASAAVET ADYHVTTSQH
ARAAEDENDA KVEGERRTRT RGGKATKQKK GNKLSESKAD REEARAVTRG GKGKRKPSTL
QQGFNKPAQV VNRDVVIGET ITVAELANKM AVKGSQVIKA MMKLGAMATI NQVIDQETAQ
LVAEEMGHKV ILRRENELEE ALMSDRDTGA AAEPRAPVVT IMGHVDHGKT SLLDYIRSTK
VAAGEAGGIT QHIGAYHVET DNGMITFLDT PGHAAFTSMR ARGAQATDIV VLVVAADDGV
MPQTIEAIQH AKAAQVPLVV AVNKIDKPEA DPDRVKQELS QYGVMPEEWG GEAQFVHVSA
KAGTGIDELL NAILLQSEVL ELKAVRSGMA SGVVIESFLD KGRGPVATVL VQEGTLNKGD
IVLCGFEYGR VRAMRDELGR EVTSAGPSIP VEILGLSSVP AAGDEATVVR DEKKAREVAL
YRQGKFREVK LARQQKSKLE NMFANMTDGE VSELNIVLKS DVQGSCEAIC ESLLKLSTDE
VKVKIVGSGV GGITETDATL AAASNAIILG FNVRADASAR RVIEAESLDL RYYSVIYNLI
DEVKQAMSGM LAPEYKQQII GLAAVRDVFK SPKFGAIAGC MVTEGNIKRH NPIRVLRDNV
VIYEGELESL RRFKDDVNEV RNGMECGIGV KNYNDVRVGD MIEVFEIIEI QRTIA
