ID   IF2_ANAMM               Reviewed;         832 AA.
AC   Q5PAJ5;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 1.
DT   03-AUG-2022, entry version 101.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=AM735;
OS   Anaplasma marginale (strain St. Maries).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rickettsiales;
OC   Anaplasmataceae; Anaplasma.
OX   NCBI_TaxID=234826;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=St. Maries;
RX   PubMed=15618402; DOI=10.1073/pnas.0406656102;
RA   Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L.,
RA   Palmer G.H., McGuire T.C., Knowles D.P. Jr.;
RT   "Complete genome sequencing of Anaplasma marginale reveals that the surface
RT   is skewed to two superfamilies of outer membrane proteins.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:844-849(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; CP000030; AAV86685.1; -; Genomic_DNA.
DR   RefSeq; WP_011114409.1; NC_004842.2.
DR   AlphaFoldDB; Q5PAJ5; -.
DR   SMR; Q5PAJ5; -.
DR   KEGG; ama:AM735; -.
DR   HOGENOM; CLU_006301_10_2_5; -.
DR   OMA; VIFAMNK; -.
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; 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   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..832
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000228161"
FT   DOMAIN          331..500
FT                   /note="tr-type G"
FT   REGION          1..87
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          120..148
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          163..201
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          340..347
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          365..369
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          386..389
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          440..443
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          476..478
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        21..46
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        71..87
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         340..347
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         386..390
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         440..443
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   832 AA;  88755 MW;  27D0E71FD56CF213 CRC64;
     MLMSDVEKFG GDCGSSGGSG RPTLKLGTRA STLAKTPTST GGRTFMTVEV RSRKRKASGA
     SPAEGVGYGT SPYTSDDNRQ GQISRSATCS LTAREQLSRI NAIHTADSIS AQKEAAKKLR
     DEEEVEVAPP EGESVIDEPD SVKEPAAAAD AVADVATPVL GDIAPGAAGT RPGRGGHDDK
     GKRYSYQGAG GKIKEKEGGG GVKKAAASRA SSKHIKLDIE NALSGTEERY VLMASSRRRG
     GSKSDRRISR DVVIPDEIEV KALAAAMAEK VGDVLRVLSH MGVEARQNTA IGSDVASEVA
     ERFSHRPKVV SKIQMERELS DISDSGLALE PRPPVVTVMG HVDHGKTSLL DVLRKSNVAE
     KEFRGITQHI GAYQIDVDGK KITFLDTPGH EAFSDMRARG TNVTDIVVLV VAADDGVMPQ
     TVESINHVKT AGVSMVVAVN KIDRSDANVD KITNDLLQHG VVPEKLGGDV MIVPVSAKTG
     ENLDKLKSSI LLLAEMLELR APVEGRAQGV VIESKIERNC GVVATVIVQR GTLRKGNVVV
     AGDGSYGKVR NMFDDSDNSV EEALPSMPVR VLGLDKVPKA GDVFLVMPSE KHARDLLEHR
     AGINLSRGRD SGRNDSVFTG PLFSMDRPEG VNMILKADVA GSLEAISRSV AQIEHEEVKF
     NILHKDIGDV TKSDILLAEA ASAVVLAFNV KVDAQARDLV RQKDVDIRHH RVIYDLIDDV
     KGVVCGKLKP IIREVQVGLL VVREVFSSGK GGTVIGCYVS EGAVSRGALV KIYRNDAVTC
     EGKVKVLRRF KDDVKEVGHG LECGVLVEGA KDVAVGDVIK VLEVVEHARV VE