IF2_PSECP
ID IF2_PSECP Reviewed; 954 AA.
AC B8HG54;
DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-2009, sequence version 1.
DT 03-AUG-2022, entry version 84.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=Achl_1426;
OS Pseudarthrobacter chlorophenolicus (strain ATCC 700700 / DSM 12829 / CIP
OS 107037 / JCM 12360 / KCTC 9906 / NCIMB 13794 / A6) (Arthrobacter
OS chlorophenolicus).
OC Bacteria; Actinobacteria; Micrococcales; Micrococcaceae; Pseudarthrobacter.
OX NCBI_TaxID=452863;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700700 / DSM 12829 / CIP 107037 / JCM 12360 / KCTC 9906 / NCIMB
RC 13794 / A6;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D.,
RA Goodwin L., Pitluck S., Goltsman E., Clum A., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Mikhailova N., Jansson J., Richardson P.;
RT "Complete sequence of chromosome of Arthrobacter chlorophenolicus A6.";
RL Submitted (JAN-2009) 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; CP001341; ACL39416.1; -; Genomic_DNA.
DR RefSeq; WP_015936639.1; NC_011886.1.
DR AlphaFoldDB; B8HG54; -.
DR SMR; B8HG54; -.
DR STRING; 452863.Achl_1426; -.
DR PRIDE; B8HG54; -.
DR EnsemblBacteria; ACL39416; ACL39416; Achl_1426.
DR KEGG; ach:Achl_1426; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_1_11; -.
DR OMA; QVRPEMI; -.
DR OrthoDB; 347113at2; -.
DR Proteomes; UP000002505; 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; 2.
DR PRINTS; PR00315; ELONGATNFCT.
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..954
FT /note="Translation initiation factor IF-2"
FT /id="PRO_1000118745"
FT DOMAIN 447..618
FT /note="tr-type G"
FT REGION 56..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 456..463
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 481..485
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 506..509
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 560..563
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 596..598
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 70..94
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..228
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 237..258
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 456..463
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 506..510
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 560..563
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 954 AA; 98635 MW; 56B69690CC8101E2 CRC64;
MAKVRVHELA KELGITSKDA VTKLQELGEF VRSASSTIEA PVVRKLRNAF PDAANKAAAP
AAPKAPAPAA ESRPAAPAPG PAAPKAPAPK VEAPAPAAPA ASAPAAPQAS SAAPAAPSTG
AKPGARPGPK AETPAPAPRQ GGSSQGSSAP RPGGPRPGNN PFATSQGMPR GRGGDGDRAP
RPGNNPFATS QGMPRPGRSD GERPGGPRPA AGAGGPRPGG PRPAPGAGGP RPAAGAGGPR
PGAPRPGGPR PTPGMMPNRT ERPAPAGAGR PGGGGRGPGR PGAPGTGGPG GGGGAPAGGG
FGKGGRGRGG TQGAFGKGGA GRGKQRKSKR AKRQELEQMS APSLGGVSVP RGDGNTVIRL
RRGSSITDFA DKIEANPAAL VTVLFHLGEM ATATQSLDED TFALLGEELG YKLQVVSPED
EERELLSTFD IDVEAELEAE GDEELEPRAP VVTVMGHVDH GKTRLLDAIR NSDVVAGEHG
GITQHIGAYQ ISHEHEGVER DITFIDTPGH EAFTAMRARG AKVTDIAILV VAADDGVMPQ
TVEALNHAQA ANVPIVVAVN KIDKEGANPD KVKGQLTEYG LVPEEYGGDT MFVEVSARQN
LNINELIDAV LLTADAALDL RANPDKAARG IAIEANLDKG RGAVATVLVQ SGTLAVGDTI
VAGTAHGRVR AMFDEDGQAL DVALPSRPVQ VLGLSNVPRA GDTFLVTSDE RTARQIAEKR
EAADRNAQLA KRRKRISLED FDQAVADGKI DTLNLILKGD VSGAVEALED ALLKIDVGEG
VQLRVIHRGV GAITQNDVNL ATVDSAVIIG FNVKPAERVA DLADREGVDM RFYSVIYAAI
DDIEAALKGM LKPEYEEFQL GTAEVREVFR SSKFGNIAGS IVRSGIIRRN TKARISRDGK
IIGDNLTIET LKRFKDDATE VRTDFECGIG LGSYNDITEG DIIETFEMRE KPRV
