IF2_PSEU2
ID IF2_PSEU2 Reviewed; 841 AA.
AC Q4ZNR2;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-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=Psyr_4180;
OS Pseudomonas syringae pv. syringae (strain B728a).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas; Pseudomonas syringae.
OX NCBI_TaxID=205918;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B728a;
RX PubMed=16043691; DOI=10.1073/pnas.0504930102;
RA Feil H., Feil W.S., Chain P., Larimer F., Dibartolo G., Copeland A.,
RA Lykidis A., Trong S., Nolan M., Goltsman E., Thiel J., Malfatti S.,
RA Loper J.E., Lapidus A., Detter J.C., Land M., Richardson P.M.,
RA Kyrpides N.C., Ivanova N., Lindow S.E.;
RT "Comparison of the complete genome sequences of Pseudomonas syringae pv.
RT syringae B728a and pv. tomato DC3000.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:11064-11069(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; CP000075; AAY39210.1; -; Genomic_DNA.
DR RefSeq; WP_011268881.1; NC_007005.1.
DR RefSeq; YP_237248.1; NC_007005.1.
DR AlphaFoldDB; Q4ZNR2; -.
DR SMR; Q4ZNR2; -.
DR STRING; 205918.Psyr_4180; -.
DR EnsemblBacteria; AAY39210; AAY39210; Psyr_4180.
DR KEGG; psb:Psyr_4180; -.
DR PATRIC; fig|205918.7.peg.4307; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_1_6; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000000426; 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..841
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228232"
FT DOMAIN 341..510
FT /note="tr-type G"
FT REGION 87..254
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..357
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 375..379
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 396..399
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 450..453
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 486..488
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 87..135
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 175..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 350..357
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 396..400
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 450..453
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 841 AA; 90539 MW; 5F7D2C7A492B68AC CRC64;
MTQVTVKELA KVVDTPVERL LQQMREAGLS HTAAEQVVTD NEKQALLTHL KSGHKAKVEE
PRKITLQRKT TSTLRVAGSK SISVEVRKKK VFVQRSPEEI EAERKREMDE RRAVENAARQ
KAEEEAKRRA EEDARSQPAA SQSAPAAAEP VAAAEPVREA APAAAPAPAS AAPSADARKR
DEQRRPDKPR ADDRNARGGD GERKNAPHRA SVKEKAPAPR VAPRTTDEES DSFRRGGRGK
GKLKKRNAHG FQSPTGPVIR DVAIGETITV GELSAQMSVK AAEVIKFMFK MGTPVTINQV
LDQETAQLIA EELGHKVTLV SDNALEDSLA ESLKFEGESF SRAPVVTVMG HVDHGKTSLL
DYIRRAKVAA GEAGGITQHI GAYHVETERG MVTFLDTPGH AAFTAMRARG AKATDIVILV
VAADDGVMPQ TIEAVQHAVA AGVPLVVAVN KIDKPGADLD RIRSELSVHG VTSEEWGGDT
PFVSVSAKMG TGVDELLEAV LLQAEVLELK ATPSAPGRGV VVESRLDKGR GPVATVLVQD
GTLRQGDMVL VGSNFGRIRA MLDENGKPVK EAGPSIPVEI LGLDGTPDAG DEMSVLSDEK
KAREVALFRQ GKFREVKLAR AHAGKLENIF ENMGQAEKKT LNIVLKSDVR GSLEALNGAL
NGLGNDEVQV RVVGGGVGGI TESDANLALA SNAVLFGFNV RADAGARKIV EQEGLDMRYY
NVIYDIIEDV KKALTGMLGS DVRENILGIA EVRDVFRSPK FGAIAGCMVL EGTVYRNRPI
RVLREDIVIF EGELESLRRF KDDAAEVRAG MECGIGVKSY NDVKVGDKIE VFEKVQVARS
L
