IF2_CHLTR
ID IF2_CHLTR Reviewed; 892 AA.
AC O84098;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
DE RecName: Full=Translation initiation factor IF-2;
GN Name=infB; OrderedLocusNames=CT_096;
OS Chlamydia trachomatis (strain D/UW-3/Cx).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=272561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D/UW-3/Cx;
RX PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT trachomatis.";
RL Science 282:754-759(1998).
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 (By similarity). {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000305}.
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DR EMBL; AE001273; AAC67687.1; -; Genomic_DNA.
DR PIR; H71558; H71558.
DR RefSeq; NP_219599.1; NC_000117.1.
DR RefSeq; WP_009871444.1; NC_000117.1.
DR AlphaFoldDB; O84098; -.
DR SMR; O84098; -.
DR STRING; 813.O172_00520; -.
DR EnsemblBacteria; AAC67687; AAC67687; CT_096.
DR GeneID; 884165; -.
DR KEGG; ctr:CT_096; -.
DR PATRIC; fig|272561.5.peg.105; -.
DR HOGENOM; CLU_006301_3_1_0; -.
DR InParanoid; O84098; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000000431; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
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; IBA:GO_Central.
DR GO; GO:0006413; P:translational initiation; IBA:GO_Central.
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; Reference proteome.
FT CHAIN 1..892
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137191"
FT DOMAIN 397..566
FT /note="tr-type G"
FT REGION 32..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 114..300
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 406..413
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 431..435
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 452..455
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 506..509
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 542..544
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 33..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..135
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..162
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 200..250
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 251..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 406..413
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 452..456
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
FT BINDING 506..509
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000250"
SQ SEQUENCE 892 AA; 97010 MW; 9D401C079D6B1A51 CRC64;
MEKVKLTKNL KLKIKNAQLT KAAGLDKLKQ KLAQAGSSDT KNSPASKAQT KEKSSKKTAG
TPAPAPEVDS GATESTARRI RAKDRSSFAA EPTVTTALPG DASHLTLDAI PAMKAPEITS
VTQKEQTLGE CTDTSSVQQE EKKESSEETS PERVEETLII RTRTEPKSVV SIKPKFGPTG
KHINHLLAKT FKAPAKETKA ASTEETTQQQ PRQNDAASYN NKQQPSGTSS RPASSAPSYR
RESTNNNNNA KRGSERDRSK RSDESVKAFT GRDRYGLNEG SSEEDKWRKK RVHKTKKQAE
EHVVQCPAHI KIALPITVKD LAAEMKLKAS ELIQKLFIHG MTYVVNDVLD SQTVVEYIGL
EFGCTIEIDS SAKEKLCLLE NAVRDEVNAT DPEKLIIRSP IVAFMGHVDH GKTTIIDALR
QSNMAASEAG AITQHTGAFK CTTPVGEITV LDTPGHEAFS AMRARGAEVC DIVVLVVAGD
EGIKEQTIEA IEHAKGANIT IVVAINKCDK PNFNVETVYR QLAELDLLPE AWGGSIATIN
TSAKTGEGLQ DLLEMLALQA EVLELKADPS ARARGLVIES ELHKGLGAVA TVLVQNGTLH
LGEALVFNDC YGKVKTMHDE HNQLLQSATP STPVLITGLS AIPKAGDPFI VVKNEKVAKE
IISARLAGQQ RSAALQKKRP NFDAVLQNKK TLKLIIKADV QGSIEALAHS ILNIRSEKVD
VEILSSEVGD ISESDIRLAS ASKATVIGFH TSVESHAEPL IKNLNVKVCL FDIIYHAVDA
IKEIMTGLLD PIAEEKNLGA AEIKATFKSS QLGTIYGCLV TEGTIVRNQK IRIIRDKEVL
WKGSLSSLKR LKEDVKEVKK GMECGILLDN YQQAQVGDIL QCYEVIYHPQ KL
