ID IF2_BAUCH Reviewed; 880 AA.
AC Q1LSK8;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2006, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=BCI_0631;
OS Baumannia cicadellinicola subsp. Homalodisca coagulata.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Baumannia.
OX NCBI_TaxID=374463;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16729848; DOI=10.1371/journal.pbio.0040188;
RA Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H.,
RA Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.;
RT "Metabolic complementarity and genomics of the dual bacterial symbiosis of
RT sharpshooters.";
RL PLoS Biol. 4:1079-1092(2006).
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; CP000238; ABF14122.1; -; Genomic_DNA.
DR RefSeq; WP_011520789.1; NC_007984.1.
DR AlphaFoldDB; Q1LSK8; -.
DR SMR; Q1LSK8; -.
DR STRING; 374463.BCI_0631; -.
DR KEGG; bci:BCI_0631; -.
DR HOGENOM; CLU_006301_6_3_6; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000002427; 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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-UniRule.
DR CDD; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR CDD; cd03692; mtIF2_IVc; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.30.56.50; Putative DNA-binding domain, N-terminal subdomain of bacterial translation initiation factor IF2; 1.
DR Gene3D; 2.40.30.10; Translation factors; 2.
DR Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR HAMAP; MF_00100_B; IF_2_B; 1.
DR InterPro; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR004161; EFTu-like_2.
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 NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF03144; GTP_EFTU_D2; 1.
DR Pfam; PF11987; IF-2; 1.
DR Pfam; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 2.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46955; Putative DNA-binding domain; 1.
DR SUPFAM; SSF50447; Translation proteins; 2.
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..880
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000008202"
FT DOMAIN 379..548
FT /note="tr-type G"
FT REGION 259..281
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 388..395
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 413..417
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 434..437
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 488..491
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 524..526
FT /note="G5"
FT /evidence="ECO:0000250"
FT BINDING 388..395
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 434..438
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 488..491
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 880 AA; 97834 MW; FBD996774F5A663E CRC64;
MKNVTVKSLA VEMQISVDHL VQQFSNVGFH KTARDYVTQQ EKETLLAYLK YELSNTPLTL
QRKTRSTLNI ASTSGRSKSV QVEVRKKHIY IQPVAHDSIL TIKENILPNN TQEVKNNAEA
SPKTKFILTP KQQSKIAKNN IVNNQNNLIK KSRQISEKAI LEAKAAELKH QAEEETRRKV
EEKARQIAEE ARQFAEHNDS IWMTTPELAE DDTIDDNLSN YHYASIVEDE NNRKIENERR
TRGNKVSKQK TYRLSEFKKN REEARAVGRS SKSQSKRKSS TLMQVFNKPS QVINRDIVIG
EMITVAELAN KMAVKGSQII KKLIQLGVMA TINQIIDRET AQLVAEDMGH KVILLRENEL
EESIMKDRKI DSSVDNAESR APVVTIMGHV DHGKTSLLDY IRSTKVVASE AGGITQHIGA
YHVETDRGMI TFLDTPGHAA FTAMRARGAR TTDIVVLVVA ADNGAMPQTI EAIQHAKAAK
VPIVVAVNKI DKKEANPENI KNELTKHGII PEEWGGQNQF VNISAKYGTG INNLLDAILL
QAEVLELKAI RNGIASGIVI ESFLDKGRGP VATILVREGT LHHGDMILCG LEYGRVRAMR
DEQGRHLSTA GPSVPVEILG LSGVPIAGDE AMVVRDEKKA REVALYRQGK FREGKLARKH
SAKLENMFTN ISEGGILELN IILKTDVQGS VEAINDALEQ LSTEKAKVKI IGSGVGGITE
TDATLAAASN AILIGFNVRA DASARRIIDK ENLNIHYYSV IYHLINEVTQ AMNGMLTPEY
KQDIIGLAEV RNVFSVPKFG LIAGCMVIEG IVKRHNNIRV IRNNIIIYEG ELYSLRRFKD
DVNEVRNGME CGIGVKNYTD IRTGDIIEVF KLIPIIKSSN
//
