IF2_CHLAB
ID IF2_CHLAB Reviewed; 874 AA.
AC Q5L627;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 21-JUN-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CAB451;
OS Chlamydia abortus (strain DSM 27085 / S26/3) (Chlamydophila abortus).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=218497;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 27085 / S26/3;
RX PubMed=15837807; DOI=10.1101/gr.3684805;
RA Thomson N.R., Yeats C., Bell K., Holden M.T.G., Bentley S.D.,
RA Livingstone M., Cerdeno-Tarraga A.-M., Harris B., Doggett J., Ormond D.,
RA Mungall K., Clarke K., Feltwell T., Hance Z., Sanders M., Quail M.A.,
RA Price C., Barrell B.G., Parkhill J., Longbottom D.;
RT "The Chlamydophila abortus genome sequence reveals an array of variable
RT proteins that contribute to interspecies variation.";
RL Genome Res. 15:629-640(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; CR848038; CAH63904.1; -; Genomic_DNA.
DR AlphaFoldDB; Q5L627; -.
DR SMR; Q5L627; -.
DR EnsemblBacteria; CAH63904; CAH63904; CAB451.
DR KEGG; cab:CAB451; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_3_2_0; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000001012; 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; 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..874
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228183"
FT DOMAIN 380..549
FT /note="tr-type G"
FT REGION 1..289
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 389..396
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 414..418
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 435..438
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 489..492
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 525..527
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 35..54
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 83..103
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..155
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..197
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..227
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..273
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 389..396
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 435..439
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 489..492
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 874 AA; 95618 MW; 8E510FBB80F4EC68 CRC64;
MKIKNAQLTK AAGLDKLKQK LAQAGSSDTK SSSEKPTTKV PEKVAKEKVV KKKSVLDSSV
PTMAEHVSTE TSPRRIRAKN RSSFASEDST IPSPVSVDTE STAFSPPVVE EVVSPLESAE
PEIVEPTPAS IVDEPETTIQ EPPPPKKEAE LVVKKEPPKN VVSIKSNFGP TGKHINHLLA
KTFKAPKKED KPAPKERTGT VQTKPQQSSE VPSDKQHSSN NRQSQPFYRR DTSKRPGSDF
RDRSKKDDSP KAFTGRDRYG LNDSSDDDKW RKKRVQKTKK HYDEHSVQRP THIKVPLPIT
IKDLAAEMKL KASELIQKMF IHGMTYVVND VLDNETTVQF IGLEFGCTID IDSSEQDKLC
IESNTVKEEI QETDPSQLII RPPIVAFMGH VDHGKTTLID SLRKSNVAAV EAGAITQHMG
AFCCSTPVGN ITILDTPGHE AFSAMRARGA EVCDIVVLVV AGDEGIKEQT LEAVKHARAA
NITIVVAINK CDKPNFNADT VYRQLSEINL LPEAWGGTTV TINTSAKTGE GLSELLEMLA
LQAEVLELKA NPEARARGIV IESELHKGLG AVATILVQNG TLHLGEALVF NDCYGKVKTM
HNEHNQLMTS ASPSVPALIT GLSSMPKAGD PFVVVKNEKT AKEIVNARIA GQQKFALQKK
RPNFDAMLQN KKILKLIIKA DVQGSIEALS SSVLKIVSDK VSAEILSSSV GEISESDIRL
AAASKAVIIG FHTGIESHAE SLIKNLGVKV HLFNIIYHAV DAVKEMMTAL LDPIAEERNL
GSAEIKETFK SSQLGTIYGC LVSEGVMTRN QKVRVVRNNE VLWKGNLSSL KRIKEDVKEV
KKGLECGILL EGYQNAQVGD ILQCYEVIYH PQKL
