IF2_STRM5
ID IF2_STRM5 Reviewed; 883 AA.
AC B4SQS0;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Smal_2815;
OS Stenotrophomonas maltophilia (strain R551-3).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Stenotrophomonas; Stenotrophomonas maltophilia group.
OX NCBI_TaxID=391008;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=R551-3;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Lang D., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Taghavi S.,
RA Monchy S., Newman L., Vangronsveld J., van der Lelie D., Richardson P.;
RT "Complete sequence of Stenotrophomonas maltophilia R551-3.";
RL Submitted (JUN-2008) 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; CP001111; ACF52515.1; -; Genomic_DNA.
DR RefSeq; WP_012511703.1; NC_011071.1.
DR AlphaFoldDB; B4SQS0; -.
DR SMR; B4SQS0; -.
DR STRING; 391008.Smal_2815; -.
DR EnsemblBacteria; ACF52515; ACF52515; Smal_2815.
DR KEGG; smt:Smal_2815; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_2_6; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR BioCyc; SMAL391008:SMAL_RS14320-MON; -.
DR Proteomes; UP000001867; 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..883
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093829"
FT DOMAIN 382..551
FT /note="tr-type G"
FT REGION 53..90
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 171..294
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 391..398
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 416..420
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 437..440
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 491..494
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 527..529
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 53..77
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..224
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..269
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 391..398
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 437..441
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 491..494
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 883 AA; 94815 MW; A47393E84CBD060B CRC64;
MSQQTTIRKL AELVNTPVEK LLEQLAGAGM KFSGPDQVVT SSEKVKLLGF LRRSHGKPEQ
APEETDQSAK KITLNRRKQQ EVTVNSGRSK TTVNVEVRQK RTYVKDGARA MTPDEERADI
LRKLEESRAR NLAEQQALAE KDRLRDEAIV RAREEEVAAK ERAEAEKKAA EEAAAAAKAA
EALAASKPKV RAPIDETAPR PPRAPAAAPA APRGAPPPPP RSDDRNNRSA PRNERGPGDR
FAGQMHLSAA DRARRGNSNN SNNRGRPGGR NQSGGRRDMS RGGNNAGPHA FERPTAPVVR
EVAIGETITV ADLAQKLALK GGEVVKALFK MGVMATITQS IDHDTAALVT EELGHKAIRA
NDNDAEDALL ASAGENQGEA VQRPPVVTIM GHVDHGKTSL LDYIRRTKVA TGEAGGITQH
IGAYHVDTPK GVISFLDTPG HAAFTSMRAR GAKLTDIVVL VVAADDGVMP QTKEAIQHAR
SAGVPLIVAI NKIDKSGADP MRVKNELLSE QVVAEDFGGD IQMVEISAKT GLGIDDLLDA
VSVQAELLEL KAVDEGRANG VVIESSLDKG RGPVATVLVQ QGRLKKGDYL VCGIQYGRVR
ALFDETGKQP EFAGPSIPVQ VLGLSGVPEA GDDFVVVDDE RLAKDVAQQR ETKRRESRLV
ATAGSRMEDI MATLGKGEGQ QVLNLVIKAD VQGSVQALSQ ALVALSNEDI RINVIHSGVG
GITESDANSA AASKATVIGF NVRADASARR IIESNGVDLR YFSIIYDVID QVKQVASGLL
GVEIREEIIG IAEVRDVFRS SKLGAVAGSM VIEGVVKRNK PIRVLRDSVV IFEGELESLR
RFKENVEEVR NGTECGIAVK AYNDVKPGDQ IECFERIEVP RTL
