IF2_SULDN
ID IF2_SULDN Reviewed; 874 AA.
AC Q30SS6;
DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Suden_0676;
OS Sulfurimonas denitrificans (strain ATCC 33889 / DSM 1251) (Thiomicrospira
OS denitrificans (strain ATCC 33889 / DSM 1251)).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Campylobacterales;
OC Thiovulaceae; Sulfurimonas.
OX NCBI_TaxID=326298;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33889 / DSM 1251;
RX PubMed=18065616; DOI=10.1128/aem.01844-07;
RA Sievert S.M., Scott K.M., Klotz M.G., Chain P.S.G., Hauser L.J., Hemp J.,
RA Huegler M., Land M., Lapidus A., Larimer F.W., Lucas S., Malfatti S.A.,
RA Meyer F., Paulsen I.T., Ren Q., Simon J., Bailey K., Diaz E.,
RA Fitzpatrick K.A., Glover B., Gwatney N., Korajkic A., Long A.,
RA Mobberley J.M., Pantry S.N., Pazder G., Peterson S., Quintanilla J.D.,
RA Sprinkle R., Stephens J., Thomas P., Vaughn R., Weber M.J., Wooten L.L.;
RT "Genome of the epsilonproteobacterial chemolithoautotroph Sulfurimonas
RT denitrificans.";
RL Appl. Environ. Microbiol. 74:1145-1156(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; CP000153; ABB43955.1; -; Genomic_DNA.
DR RefSeq; WP_011372309.1; NC_007575.1.
DR AlphaFoldDB; Q30SS6; -.
DR SMR; Q30SS6; -.
DR STRING; 326298.Suden_0676; -.
DR EnsemblBacteria; ABB43955; ABB43955; Suden_0676.
DR KEGG; tdn:Suden_0676; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_4_1_7; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000002714; 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; 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; PF04760; IF2_N; 2.
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..874
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000335513"
FT DOMAIN 374..543
FT /note="tr-type G"
FT REGION 55..139
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 245..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 383..390
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 408..412
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 429..432
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 483..486
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 519..521
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 55..69
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 383..390
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 429..433
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 483..486
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 874 AA; 95935 MW; 6B19F540A06F3905 CRC64;
MTEKVRVHEI AKELGITSKD VVKKASDMGI EIKSANSSVS MEEAEGLMNY IMSGELAQSP
TAEQKVQTKA PSHTPKEEDP TQESNKSQTT LSKKASETPI QHVVEKAKEI DVKNSEKEVI
SEVKEIKKEE ESIESSELKK MQIKKSGLKI VKKKQPREEE KIQDDFISSV KQTQASISSY
GKISAEVLEE LANKKKAKQA SSGAKKQEQG VKIDIFGASL SEVSMDMDDQ IVLLDLNSTQ
RQELIAEEPR KPKVVKPAGR NANKKSAPKG RNVSRDKRKK YAKDKPEDLI VTHVEIPEDI
RVYEFAEKLN RPISDVIKVL FSLGLMMTKN DFLGSDEIEI LSEEFGVEVT IVDPKDAFNY
EEDLAEVIDE NATERPPVIT IMGHVDHGKT SLLDAIRKAK VTQDEAGGIT QHIGAYTIEQ
NGKAITFLDT PGHAAFSQMR QRGTDVTDII IIVVAADDGV KPQTEEVIKL AKESKVPVIV
AVNKMDKPTA NPDMVKAQMA ERGLNPIDWG GDIEFIPISA KSGMGIDELL ENILLTAEVL
ELKANENAMA KAAVVESSLE KGRGPVATVI VQNGTLNVGD YVVCGSSYGR VKALINEHKQ
QIKSIKPSHT AVVVGLNEVP SSGEIMMAMS SDKEAREYAL KRHEYDRHKE LSHSTKSTLE
DMTSMIAEGR LKSLKVVLKT DVHGSLEAIR SSLNELRNDE VKINVISSGV GGITENDVEL
VSNSENCVLL GFNVRPTGSV KALAKQKNVD IKTYSIIYQL LDDMTGMLMG MMAPKFSEIN
TGQAEVRNTF KAPKGMVAGC VVVDGKLIRG GLVRVIRDGV VVHEGELTSL KRFKDDVDEI
GNGYECGVMI KGYDDVIVGD VIETFKKVEQ KVSL
