IF2_CHLCV
ID IF2_CHLCV Reviewed; 887 AA.
AC Q823F2;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=CCA_00465;
OS Chlamydia caviae (strain ATCC VR-813 / DSM 19441 / 03DC25 / GPIC)
OS (Chlamydophila caviae).
OC Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=227941;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC VR-813 / DSM 19441 / 03DC25 / GPIC;
RX PubMed=12682364; DOI=10.1093/nar/gkg321;
RA Read T.D., Myers G.S.A., Brunham R.C., Nelson W.C., Paulsen I.T.,
RA Heidelberg J.F., Holtzapple E.K., Khouri H.M., Federova N.B., Carty H.A.,
RA Umayam L.A., Haft D.H., Peterson J.D., Beanan M.J., White O.,
RA Salzberg S.L., Hsia R.-C., McClarty G., Rank R.G., Bavoil P.M.,
RA Fraser C.M.;
RT "Genome sequence of Chlamydophila caviae (Chlamydia psittaci GPIC):
RT examining the role of niche-specific genes in the evolution of the
RT Chlamydiaceae.";
RL Nucleic Acids Res. 31:2134-2147(2003).
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; AE015925; AAP05210.1; -; Genomic_DNA.
DR AlphaFoldDB; Q823F2; -.
DR SMR; Q823F2; -.
DR STRING; 227941.CCA_00465; -.
DR EnsemblBacteria; AAP05210; AAP05210; CCA_00465.
DR KEGG; cca:CCA_00465; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_3_2_0; -.
DR OMA; NRDNRTG; -.
DR Proteomes; UP000002193; 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..887
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000137187"
FT DOMAIN 393..562
FT /note="tr-type G"
FT REGION 31..87
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 94..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 129..285
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 402..409
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 427..431
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 448..451
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 502..505
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 538..540
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 46..65
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..168
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 195..211
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 212..240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..285
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 402..409
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 448..452
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 502..505
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 887 AA; 96938 MW; F13EECD1700CF6B7 CRC64;
MEKAKLTKNL KLKIKNAQLT KAAGLDKLKQ KLAQAGSSET KSSSEKPSTK VPEKIAKEKV
VKKKSVVDPG VPTMTEPVSA ENSPRRIRAK NHSSFVSEDL NSPQPPVPVD SDASAFSDSA
VVEEVDSFVE TEQEISVSTP PPPVTEETEV VAKEPPAPKK EPEVVVKKEP PKSVVSIKSN
FGPTGKHINH LLAKTFKAPK KEDKPAPKEK TKTTQTKPQQ SSDASNDKHH SPTNRTSQPF
YRRDVSKKSG SDFRDRAKKD DNPKAFTGRD RYGLNDSSDD DKWRKKRVQK TKKHYEEHAI
QRPTHIKVPL PITIKDLAAE MKLKASELIQ KMFIHGMTYV VNDVLDNETT VQFIGLEFGC
TIDIDSSEQD KLCIESNTVK EEIQETDPSK LITRPPIVAF MGHVDHGKTT LIDSLRKTNV
AAVEAGAITQ HMGAFCCSTP VGNLTILDTP GHEAFSAMRA RGAEVCDIVV LVVAGDEGIK
EQTLEAVKHA RAANITIVVA INKCDKPNFN ADTIYRQLAE IELLPEAWGG TTVTINTSAK
TGEGLSELLE MLALQAEVLE LKANPSARAR GLVIESELHK GLGAVATILV QNGTLHLGEA
LVFNDCYGKV KTMHNEHNQL MKSASPSIPA LITGLSSMPK AGDPFVVVKN EKTAKEIVGA
RLAGQQKFAL QKKRPNFDAM LQNKKILKLI IKADVQGSIE ALANSILKIT SDKVSAEILA
NSVGEISESD IRLAAASKAV IIGFHTGIES HAESLIKNLG VKVQLFNIIY HAVDAVKEMM
TALLDPIAEE KNLGSAEIKE TFKSSQLGTI YGCLVSEGTM TRNQKVRVVR GNEIVWKGNL
SSLKRIKEDV KEVKKGFECG ILLEGCQHAQ VGDILQCYEV IYHPQKL
