IF2_XANOP
ID IF2_XANOP Reviewed; 904 AA.
AC B2SVK3;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=PXO_01303;
OS Xanthomonas oryzae pv. oryzae (strain PXO99A).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Xanthomonas.
OX NCBI_TaxID=360094;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PXO99A;
RX PubMed=18452608; DOI=10.1186/1471-2164-9-204;
RA Salzberg S.L., Sommer D.D., Schatz M.C., Phillippy A.M., Rabinowicz P.D.,
RA Tsuge S., Furutani A., Ochiai H., Delcher A.L., Kelley D., Madupu R.,
RA Puiu D., Radune D., Shumway M., Trapnell C., Aparna G., Jha G., Pandey A.,
RA Patil P.B., Ishihara H., Meyer D.F., Szurek B., Verdier V., Koebnik R.,
RA Dow J.M., Ryan R.P., Hirata H., Tsuyumu S., Won Lee S., Seo Y.-S.,
RA Sriariyanum M., Ronald P.C., Sonti R.V., Van Sluys M.-A., Leach J.E.,
RA White F.F., Bogdanove A.J.;
RT "Genome sequence and rapid evolution of the rice pathogen Xanthomonas
RT oryzae pv. oryzae PXO99A.";
RL BMC Genomics 9:204-204(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; CP000967; ACD60077.1; -; Genomic_DNA.
DR RefSeq; WP_012445526.1; NC_010717.2.
DR AlphaFoldDB; B2SVK3; -.
DR SMR; B2SVK3; -.
DR STRING; 360094.PXO_01303; -.
DR PRIDE; B2SVK3; -.
DR EnsemblBacteria; ACD60077; ACD60077; PXO_01303.
DR KEGG; xop:PXO_01303; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_6_1_6; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000001740; 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..904
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093844"
FT DOMAIN 403..572
FT /note="tr-type G"
FT REGION 134..248
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 267..315
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 412..419
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 437..441
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 458..461
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 512..515
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 548..550
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 139..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 234..248
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 283..310
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 412..419
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 458..462
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 512..515
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 904 AA; 96198 MW; BDACF0B42FF87046 CRC64;
MSQQTTIRKL AELVNTPVDK LLVQLAEAGM KFSGPDQVVT STEKMKLLGF LRRTHGKAET
PAEAASEAAK KITLNRRKLQ EVTVSAGRTK TTVNVEVRQK RTYVKSENEG SGRATPMTPD
EERADILAKL AASRQRNLDE QQRLAESDRV RDEEIQRKRD EEQAAKDRAE AERKAAEEAA
AAASAPAPVA AAPTPSAAAP AARAPSSPSS APRPSRPGGA SPASRPSTPA RPDDRNNAAK
HKTRGSHVMV AGVEDDDATK RFAGQLHLSA ADRARRSNVR GKPTGRPGSS SSRRGNDNGR
GSNQANSGPH GFERPTAPVV REVAIGETIT VADLAQKLAL KGGDVVKALF KMGVMATITQ
SIDHDTAALV TEELGHKAVR ADNADFEDAL LAHAEDAQGD TTTRPPVVTI MGHVDHGKTS
LLDYIRRTKI ASGEAGGITQ HIGAYHVETD RGVISFLDTP GHAAFTSMRA RGAKITDIVV
LVVAADDGVM PQTKEAVAHA KAAGVPLIVA VNKIDKAGAD PLRVKNELLA ENVVAEDFGG
DTQFIEVSAK VGTGVDTLLD AISLQAEVLE LKAVAEGRAS GTVIESSLDK GRGPVATVLV
QQGALKRGDY LVCGIQYGRV RALFDETGHQ PGSAGPSIPV QVLGLSGVPE AGDDFVVVDD
ERLAKDVAQQ RETKRRESRL VASATNRMED ILAQMGKGEG QQVLNLVIKA DVQGSVEALK
QSLVALSNED IRINVIHSGV GGITESDANS AAASKATIIG FNVRADASAR KIVESNGVDL
RYFSIIYDVI DQVKQVASGL LGVEIREEIM GIAQVRDVFR SSKFGAVAGC MIIEGVVKRS
KPIRVLRDSV VVFEGELESL RRFKENVDEV RNGNECGIGV KAYNDVKAGD QIECFERIEV
ARTL
