IF2_CHLPB
ID IF2_CHLPB Reviewed; 911 AA.
AC B3ELN8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 22-JUL-2008, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100};
GN OrderedLocusNames=Cphamn1_0402;
OS Chlorobium phaeobacteroides (strain BS1).
OC Bacteria; Chlorobi; Chlorobia; Chlorobiales; Chlorobiaceae;
OC Chlorobium/Pelodictyon group; Chlorobium.
OX NCBI_TaxID=331678;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BS1;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Ovchinnikova G., Li T., Liu Z., Zhao F.,
RA Overmann J., Bryant D.A., Richardson P.;
RT "Complete sequence of Chlorobium phaeobacteroides BS1.";
RL Submitted (JUN-2008) 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: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; CP001101; ACE03367.1; -; Genomic_DNA.
DR RefSeq; WP_012473858.1; NC_010831.1.
DR AlphaFoldDB; B3ELN8; -.
DR SMR; B3ELN8; -.
DR STRING; 331678.Cphamn1_0402; -.
DR KEGG; cpb:Cphamn1_0402; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_0_1_10; -.
DR OMA; NRDNRTG; -.
DR OrthoDB; 79988at2; -.
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..911
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000093769"
FT DOMAIN 408..578
FT /note="tr-type G"
FT REGION 80..142
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 153..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..309
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 417..424
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 442..446
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 464..467
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 518..521
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 554..556
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 80..128
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..262
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 284..301
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 417..424
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 464..468
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 518..521
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 911 AA; 101322 MW; A77303E91842C4F7 CRC64;
MSPEGKEMRY RISDIARELQ VSPQEVLHFV KEAGGKVAST SSMVKGPMRD LILDQFSDEK
KLVDETRKIR EEKQLRLSRL EEQSRKTYEK EQQLKDTISG RPERAAAKPR TEVPSESVEP
EPVKEMPETV AEPEVTGVVS EPDENVAAVA EEVKSPVEET SETVAEKNDV EGQVSYEVPQ
KIGGLTVFGT LDVQSSLGMG GEADKKKQRK KRFKEQADEL KDEFDIKAKE GGKEREAGGE
SRKPVKKGSE ETKKTTVEST SAKKKKGKKK KKPEVDEKTI EKNIRSTISG MDDTSGSGSS
RQKFRKMRKI EREKELEEAE AIKEAERSII RVTEFATAHE LADLMGILPK EIIQHCFTMG
KFVTINQRLD KETIELVAME FGFDAEFVSE VEATEVTEIE DEEEELEIRP PVVTIMGHVD
HGKTSLLDYI RSSNVVAGES GGITQHIGAY EVSLDGDRKI TFLDTPGHEA FTAMRARGAQ
VTDIVILVVS ADDSVMPQTV EAINHSKAAG VPIVVAINKI DKPDANPEKI KTQLSEAGVL
VEDWGGEYQC QEISAKQGTG IDALMEKVLT EAEIRELKAN FSEDVPSRGI IVEAELDKGK
GVVSTVLVQR GFLKVGDPFV AGHTMGKVRA LMDERGKRIR EAGPSQPVSV LGFEDLPQSG
DLFTVMPSDR EAREIAQKRQ IIRREHEFRR STRVKLDSIA RQIKEGLMKE LSVILKADTD
GSIQALADGL MKIHNDEVKV QIIHQGVGQI TETDVLLAAA SDAIIIGFRV RPNVNAKRLA
EKEDLDVRFY SVIYHVIEDI EQALEGMLSP ELHEESIGSL EIRQVFKVPK IGNVAGCYML
EGKIFRDSKV RLLRDGVQIY DGVLDSLKRF KDDVKEVDAG YECGLNLKGY SDIKVGDIVE
GYRIVEKKRK L
