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IF2_CHLTA
ID   IF2_CHLTA               Reviewed;         892 AA.
AC   Q3KMS4;
DT   21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN   Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CTA_0102;
OS   Chlamydia trachomatis serovar A (strain ATCC VR-571B / DSM 19440 / HAR-13).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=315277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-571B / DSM 19440 / HAR-13;
RX   PubMed=16177312; DOI=10.1128/iai.73.10.6407-6418.2005;
RA   Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D.;
RT   "Comparative genomic analysis of Chlamydia trachomatis oculotropic and
RT   genitotropic strains.";
RL   Infect. Immun. 73:6407-6418(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; CP000051; AAX50348.1; -; Genomic_DNA.
DR   RefSeq; WP_009871444.1; NC_007429.1.
DR   AlphaFoldDB; Q3KMS4; -.
DR   SMR; Q3KMS4; -.
DR   EnsemblBacteria; AAX50348; AAX50348; CTA_0102.
DR   KEGG; cta:CTA_0102; -.
DR   HOGENOM; CLU_006301_3_1_0; -.
DR   OMA; NRDNRTG; -.
DR   Proteomes; UP000002532; 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..892
FT                   /note="Translation initiation factor IF-2"
FT                   /id="PRO_0000228182"
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:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         452..456
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT   BINDING         506..509
FT                   /ligand="GTP"
FT                   /ligand_id="ChEBI:CHEBI:37565"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
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
 
 
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