ID O07365_CHLTH Unreviewed; 676 AA.
AC O07365;
DT 01-JUL-1997, integrated into UniProtKB/TrEMBL.
DT 01-JUL-1997, sequence version 1.
DT 27-MAR-2024, entry version 104.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|RuleBase:RU000644};
DE Flags: Fragment;
OS Chlamydia trachomatis.
OC Bacteria; Chlamydiota; Chlamydiia; Chlamydiales; Chlamydiaceae;
OC Chlamydia/Chlamydophila group; Chlamydia.
OX NCBI_TaxID=813 {ECO:0000313|EMBL:AAB58905.1};
RN [1] {ECO:0000313|EMBL:AAB58905.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=L2/434/Bu {ECO:0000313|EMBL:AAB58905.1};
RA Raggiaschi R., Ratti G.;
RT "The nusA gene of Chlamydia trachomatis.";
RL Submitted (OCT-1996) to the EMBL/GenBank/DDBJ databases.
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:0000256|RuleBase:RU000644}.
CC -!- SIMILARITY: Belongs to the TRAFAC class translation factor GTPase
CC superfamily. Classic translation factor GTPase family. IF-2 subfamily.
CC {ECO:0000256|ARBA:ARBA00007733, ECO:0000256|RuleBase:RU000644}.
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DR EMBL; U74759; AAB58905.1; -; Genomic_DNA.
DR AlphaFoldDB; O07365; -.
DR GO; GO:0005525; F:GTP binding; IEA:UniProtKB-KW.
DR GO; GO:0003924; F:GTPase activity; IEA:InterPro.
DR GO; GO:0003743; F:translation initiation factor activity; IEA:UniProtKB-KW.
DR CDD; cd01887; IF2_eIF5B; 1.
DR CDD; cd03702; IF2_mtIF2_II; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 2.40.30.10; Translation factors; 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; IPR009000; Transl_B-barrel_sf.
DR NCBIfam; TIGR00487; IF-2; 1.
DR NCBIfam; TIGR00231; small_GTP; 1.
DR PANTHER; PTHR43381:SF5; TR-TYPE G DOMAIN-CONTAINING PROTEIN; 1.
DR PANTHER; PTHR43381; TRANSLATION INITIATION FACTOR IF-2-RELATED; 1.
DR Pfam; PF00009; GTP_EFTU; 1.
DR Pfam; PF04760; IF2_N; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF50447; Translation proteins; 1.
DR PROSITE; PS51722; G_TR_2; 1.
PE 3: Inferred from homology;
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540,
KW ECO:0000256|RuleBase:RU000644};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917,
KW ECO:0000256|RuleBase:RU000644}.
FT DOMAIN 401..570
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 32..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..304
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 33..49
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..134
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 135..165
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 203..254
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 255..274
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 676
FT /evidence="ECO:0000313|EMBL:AAB58905.1"
SQ SEQUENCE 676 AA; 73125 MW; F3D8E2637A68865B CRC64;
MEKAKLTKNL KLKIKNAQLT KAAGLDKLKQ KLAQAGSSDT KNSPASKAQT KEKSSKKTAG
TPAPAPEVDL GATESTARRI RAKDRSSFAA EPTVTTALPG DASHLTLDAI PAIKAPEITS
VTQKEQTLRE CTDTSSVQQE EKKESSEETS PETPERIEET PIIRTRTEPK SVVSIKPKFG
PTGKHINHLL AKTFKAPAKE TKAASTEETT QQQPRQNDAA SHNNKQQPSG TSSRPASSAP
SYRRESTSNN NNNAKRGSER DRSKRSDESV KAFTGRDRYG LNEGSSEEDK WRKKRVHKTK
KQAEEHVVQC PAHIKIALPI TVKDLAAEMK LKASELIQKL FIHGMTYVVN DVLDSQTVVE
YIGLEFGCTI EIDSSAKEKL CLVENTVRDE VNATDPEKLI IRSPIVAFMG HVDHGKTTII
DALRQSNMAA SEAGAITQHT GAFKCTTPVG EITVLDTPGH EAFSAMRARG AEVCDIVVLV
VAGDEGIKKQ TIEAIEHAKG ANITIVVAIN KCDKPNFNVK TVYRQLAKLD LLPEAWGGSI
ATINTSAKTG EGLQDLLEML ALQAEVLELK ADPSARARGL VIESELHKGL GAVATVLVQN
GTLHLGEALV FNDCYGKVKT MHDEHNQLLQ SATPSTPVLI TGLSAIPKAG DPFIVVKNEK
VAKEIISARL AGQQRS
//