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IF2_BRUA4
ID   IF2_BRUA4               Reviewed;         964 AA.
AC   A6WWW5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   21-AUG-2007, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Oant_0747;
OS   Brucella anthropi (strain ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 /
OS   LMG 3331 / NBRC 15819 / NCTC 12168 / Alc 37) (Ochrobactrum anthropi).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX   NCBI_TaxID=439375;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49188 / DSM 6882 / CCUG 24695 / JCM 21032 / LMG 3331 / NBRC
RC   15819 / NCTC 12168 / Alc 37;
RX   PubMed=21685287; DOI=10.1128/jb.05335-11;
RA   Chain P.S., Lang D.M., Comerci D.J., Malfatti S.A., Vergez L.M., Shin M.,
RA   Ugalde R.A., Garcia E., Tolmasky M.E.;
RT   "Genome of Ochrobactrum anthropi ATCC 49188 T, a versatile opportunistic
RT   pathogen and symbiont of several eukaryotic hosts.";
RL   J. Bacteriol. 193:4274-4275(2011).
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; CP000758; ABS13469.1; -; Genomic_DNA.
DR   RefSeq; WP_012090991.1; NC_009667.1.
DR   AlphaFoldDB; A6WWW5; -.
DR   SMR; A6WWW5; -.
DR   STRING; 439375.Oant_0747; -.
DR   PRIDE; A6WWW5; -.
DR   EnsemblBacteria; ABS13469; ABS13469; Oant_0747.
DR   KEGG; oan:Oant_0747; -.
DR   PATRIC; fig|439375.7.peg.789; -.
DR   eggNOG; COG0532; Bacteria.
DR   eggNOG; COG3064; Bacteria.
DR   HOGENOM; CLU_006301_10_0_5; -.
DR   OMA; QVRPEMI; -.
DR   OrthoDB; 347113at2; -.
DR   PhylomeDB; A6WWW5; -.
DR   Proteomes; UP000002301; Chromosome 1.
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; 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; 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..964
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_1000008291"
FT   DOMAIN          462..629
FT                   /note="tr-type G"
FT   REGION          1..379
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          471..478
FT                   /note="G1"
FT                   /evidence="ECO:0000250"
FT   REGION          496..500
FT                   /note="G2"
FT                   /evidence="ECO:0000250"
FT   REGION          517..520
FT                   /note="G3"
FT                   /evidence="ECO:0000250"
FT   REGION          571..574
FT                   /note="G4"
FT                   /evidence="ECO:0000250"
FT   REGION          607..609
FT                   /note="G5"
FT                   /evidence="ECO:0000250"
FT   COMPBIAS        12..37
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        42..63
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        101..115
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        123..153
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        156..245
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        251..265
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        327..379
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         471..478
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         517..521
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         571..574
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ   SEQUENCE   964 AA;  104399 MW;  9EDC08D809C53DC9 CRC64;
     MSDKTNDDKT LSVNTKKTLT MKRPGVEQST VRQNFSHGRT KAVVVETKKR KFSRPDEKPE
     VEAAAPKPAA PAPAAPAPAA STPAPAQAAQ PAQAAPVVRA PAPATPAPKP AAPAAPVTKP
     HVAQQRPAQQ RPGGQQAQRP RPSDRSGMVL NTLSRSEMDA RRRALEEAQV REVEERARAV
     EEAKRRAEED ARRAKEREES ARRQAEEEAR LKAEADARRK AEEEAAKRMP QPEARTERRD
     DARPAPQGNR PQQAGRPQGN RPPQGGRPQQ GGPRPAAPSL ADAAPIPGKP LPQSQLRKTV
     ASDDDDRRGG GLTAARRGAP AKPEVRAPKV VKTEDDRRRG KLTISSNLED EGRSRSLSAM
     RRRQEKFKRS QMQETREKIS REVTIPETIT LQELAQRMTE RSVDIIKYLM KQGQMMKPGD
     VIDADMAQLI AEEFGHTVKR VAESDVEEGI FGVADNEAAL VSRPPVVTIM GHVDHGKTSL
     LDAIRHANVV SGEAGGITQH IGAYQVEQNG QKITFIDTPG HAAFTAMRAR GAQATDIAIL
     VVAADDSVMP QTIESINHAK AAGVPIIVAI NKIDKPAADP QKVRTALLQH DVFVESMGGE
     VLDVEVSAKN KLNLDKLLEA ILLQAEILDL KADPSRTAEG VVVEAQLDRG RGSVATVLVQ
     TGTLHPGDIL VAGSEWGRVR ALVNDRGEHV KEAGPAMPVE VLGLQGTPQA GDRFAVVANE
     AKAREIAEYR QRLARDKAVA RQSGARGSLE QMMNQLQVSG TKEFPLVIKG DVQGSIEAIT
     NALDKLGTDE VRARIVHSGA GGITESDVSL AEASNAAIIG FNVRANKQAR DAADQQGIEI
     RYYNIIYDLI DDVKAAMSGL LSPERRETFL GNAEILEVFN ITKVGKVAGC RVTEGKVERG
     AGVRLIRDNV VIHEGKLKTL KRFKDEVSEV PAGQECGMAF ENYDDIRAGD VIEAFRVEHV
     SRTL
 
 
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