ID A0A077FMW3_9RICK Unreviewed; 853 AA.
AC A0A077FMW3;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000256|HAMAP-Rule:MF_00100,
GN ECO:0000313|EMBL:AIL64666.1};
GN ORFNames=NOVO_01345 {ECO:0000313|EMBL:AIL64666.1};
OS Rickettsiales bacterium Ac37b.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rickettsiales.
OX NCBI_TaxID=1528098 {ECO:0000313|EMBL:AIL64666.1, ECO:0000313|Proteomes:UP000028936};
RN [1] {ECO:0000313|EMBL:AIL64666.1, ECO:0000313|Proteomes:UP000028936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ac37b {ECO:0000313|EMBL:AIL64666.1,
RC ECO:0000313|Proteomes:UP000028936};
RA Felsheim R.F., Kurtti T.J., Johnson S., Labruna M.B., Munderloh U.G.;
RT "Genome sequence of a novel Rickettsiales species cultured from Amblyomma
RT cajennense.";
RL Submitted (JAN-2015) 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:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000644}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000645}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000256|ARBA:ARBA00007733, ECO:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000644}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00100}.
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DR EMBL; CP009217; AIL64666.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A077FMW3; -.
DR STRING; 1528098.NOVO_01345; -.
DR KEGG; rbt:NOVO_01345; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_10_2_5; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000028936; 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; 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; 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; 1.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00100};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00100}; Reference proteome {ECO:0000313|Proteomes:UP000028936}.
FT DOMAIN 351..521
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 118..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 183..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 122..146
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 360..367
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 407..411
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 461..464
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 853 AA; 94485 MW; 76F56F780DE6A1BD CRC64;
MEDTHNKDKN KTSKLTISTA GKLQLSKGDG AQIKQNIAHG RSKTVTVEVK KNRSVKERSN
DGVVEVPSSV IKNDVLQQED DNISSLTDHE KSARIRALEH ADKKYVFKSL LKVSEKPSLL
DNPSEELGKE PEVTETKNHS IELSNEEVKD PIGIPIIDIP NKVVQDQPST DAVKPSITKA
VVREEEDEDD YDSSKKASKH SVSTKKVIKS EVTRKWTEDR RVYGKVSIAN NDIPEDEEPV
RSRSIASIKR AREKAKRFDL RNKETEKIAR EVILPEVISI QELANRMAEK ASEVLKQLMK
LGVMATINQV IDADTAELII HELGHKVKRV TESDVENILF GEQDPEELMV LRPPVVTVMG
HVDHGKTTLL DALRSTDVVA GEAGGITQHI GAYRVELMNG KSITFLDTPG HEAFTAMRAR
GAKVTDIVVL VVAANDGIMA QTAEAINHAK AAKLPIIVAV NKIDLPGVNS QNIRNELLNY
ELVPEELGGD IIIVEVSAKT KKNIDKLEEA ILLQADFLDL KANPNRMAVG TVIEAKVDKG
RGVVTTLLVQ KGTLKIGDII VAGVSFGKVR AMHNDKGIQV KDAIPSMPVE IIGLNEAPEA
GDLFSVVPTE KQAREISDYR SKRVREIRTA RVHKLSLEEL FSNHESLSQT KELSVIVRAD
VQGSVEAIVN NLLKMSNNEI IVKILHSAAG GITESDIVLA KASNAIILGF NVRANSPARL
LADQERIELR YYSVIYDLID EMKSIIGGML SPIIREQILG TVEIRQVFNV GKFNKIAGCF
VTNGIVRRNC KIRLLRDNVV IHTGKIKGLR RFKEDAREVR EGFECGIVLE NYDDIQEKDI
IEAFEVIEEQ QTF
//
