IF2_ZYMMO
ID IF2_ZYMMO Reviewed; 989 AA.
AC Q5NQ27;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=ZMO0554;
OS Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Zymomonadaceae; Zymomonas.
OX NCBI_TaxID=264203;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31821 / ZM4 / CP4;
RX PubMed=15592456; DOI=10.1038/nbt1045;
RA Seo J.-S., Chong H., Park H.S., Yoon K.-O., Jung C., Kim J.J., Hong J.H.,
RA Kim H., Kim J.-H., Kil J.-I., Park C.J., Oh H.-M., Lee J.-S., Jin S.-J.,
RA Um H.-W., Lee H.-J., Oh S.-J., Kim J.Y., Kang H.L., Lee S.Y., Lee K.J.,
RA Kang H.S.;
RT "The genome sequence of the ethanologenic bacterium Zymomonas mobilis
RT ZM4.";
RL Nat. Biotechnol. 23:63-68(2005).
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; AE008692; AAV89178.1; -; Genomic_DNA.
DR RefSeq; WP_011240460.1; NZ_CP035711.1.
DR AlphaFoldDB; Q5NQ27; -.
DR SMR; Q5NQ27; -.
DR STRING; 264203.ZMO0554; -.
DR PRIDE; Q5NQ27; -.
DR EnsemblBacteria; AAV89178; AAV89178; ZMO0554.
DR GeneID; 58026392; -.
DR KEGG; zmo:ZMO0554; -.
DR eggNOG; COG0532; Bacteria.
DR eggNOG; COG3064; Bacteria.
DR HOGENOM; CLU_006301_10_1_5; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000001173; 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; 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; 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..989
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228265"
FT DOMAIN 489..659
FT /note="tr-type G"
FT REGION 43..219
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 234..379
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 498..505
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 523..527
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 545..548
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 599..602
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 635..637
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 68..90
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..200
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..294
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..330
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..364
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 498..505
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 545..549
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 599..602
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 989 AA; 106621 MW; 6E4E9F72CCBA5B74 CRC64;
MSDNDKPKLG MRAPLGIKRT VETSKVKQSF SHGRSNTVIV ETKRRRVINK PGSGDAATAA
ETAKKQAEPV ENTPNKDTAV TQTATKNETV ATPAAAPAPA PAAAPKPVAA EATAQETSKA
APAAAQPVAE KEAAAPASAE AAKSAAIKVT DRGAKKTTEK NGANASGNRP SGNRSQDNRG
RQGGRGSQNK NQTRSGGQPR QPRTLAHRDL ASRQELQARL LREAEESRLQ ALEEARRRED
RLKQEADLEE QRRIEEKRRL EAEAKVEAEK QAALKEKEKA EAKARAKAEK EAKAAQAKTA
GAAEGEEKTR RPAKAAAPKA REERSESPRS PAPRRFTPVS PPRREAPRPA MRDRKGEDRR
QSGKLTVTKA LSGDEGGARA RSLAALRRAR EKDKRANQNR AQQVRQIRDV VVPEAITVQE
LANRMAERGA DLVKALFKMG VAVTLTQTID QDTAELLVTE FGHNIKRVSE SDVEIDSSSD
VDPEETLKSR PPVVTIMGHV DHGKTSLLDA LRGSDVVRGE AGGITQHIGA YQVESPSGEK
ITLLDTPGHE AFSEMRARGA NVTDIVIIVV AADDGLRPQT VEAIDHARAA DVPIIIAINK
MDKPEANPQR IREALLQYNV QVEAMGGDVQ DVEISAAKKT GLDELIEKIL LQAEMLELKA
NPDRAAEGTV VEAKLDRGRG PVATILVRRG TLKVGDIFVV GEFSGRVRAM TDAQGKNQKE
AGPSMPVEVL GLSGVPQAGD TLTVVESEAR AREVAAYRAE IALRKRTTAQ PASLESMFSA
LKDKQAVEYP LLIKADTQGS VEAIAGALNK ISNEDIRVRI LHQGVGGITE SDVSLAAASG
APIIGFHVRP NSKARDIARR DGVALKFYDV IYDLIDEIKA AMAGKLGPEY FETVVGKAEI
REVFSAGKHG RAAGLLVLEG YIRQKLRARV LRNDVIIYNG SIASLRRFKD DVPEVRAGLE
CGITLEGSTD IKAGDIVETF EVEERARTL
