IF2_CUTAK
ID IF2_CUTAK Reviewed; 964 AA.
AC Q6A7M5;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2004, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000255|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000255|HAMAP-Rule:MF_00100}; OrderedLocusNames=PPA1493;
OS Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS acnes).
OC Bacteria; Actinobacteria; Propionibacteriales; Propionibacteriaceae;
OC Cutibacterium.
OX NCBI_TaxID=267747;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16379 / KPA171202;
RX PubMed=15286373; DOI=10.1126/science.1100330;
RA Brueggemann H., Henne A., Hoster F., Liesegang H., Wiezer A.,
RA Strittmatter A., Hujer S., Duerre P., Gottschalk G.;
RT "The complete genome sequence of Propionibacterium acnes, a commensal of
RT human skin.";
RL Science 305:671-673(2004).
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; AE017283; AAT83240.1; -; Genomic_DNA.
DR RefSeq; WP_002516995.1; NZ_CP025935.1.
DR AlphaFoldDB; Q6A7M5; -.
DR SMR; Q6A7M5; -.
DR STRING; 267747.PPA1493; -.
DR EnsemblBacteria; AAT83240; AAT83240; PPA1493.
DR GeneID; 66620670; -.
DR KEGG; pac:PPA1493; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_9_0_11; -.
DR OMA; QVRPEMI; -.
DR Proteomes; UP000000603; 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.
PE 3: Inferred from homology;
KW Cytoplasm; GTP-binding; Initiation factor; Nucleotide-binding;
KW Protein biosynthesis.
FT CHAIN 1..964
FT /note="Translation initiation factor IF-2"
FT /id="PRO_0000228227"
FT DOMAIN 458..629
FT /note="tr-type G"
FT REGION 49..357
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 467..474
FT /note="G1"
FT /evidence="ECO:0000250"
FT REGION 492..496
FT /note="G2"
FT /evidence="ECO:0000250"
FT REGION 517..520
FT /note="G3"
FT /evidence="ECO:0000250"
FT REGION 571..574
FT /note="G4"
FT /evidence="ECO:0000250"
FT REGION 607..609
FT /note="G5"
FT /evidence="ECO:0000250"
FT COMPBIAS 50..64
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..83
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 86..106
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 108..142
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 143..182
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 213..241
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 467..474
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 517..521
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
FT BINDING 571..574
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00100"
SQ SEQUENCE 964 AA; 101394 MW; 9552FDDDAB499C4B CRC64;
MAKVRVYELA KELGLSSKQL LGKLNDMGEF VRSASSTIEA PVVRRLRDQI GSAEPADDAK
AAKPAARKSQ TSSKKTSKET TTAKPAPGPK PGPGPKPTPG PRPGSSSGPK PGRSSAARTS
ATPRPGLIKS SGASSQQEPP AAKPESKPTP KPGQNVPKPH APAPKPKPGA PSKSPKPGAR
PGPRPGGSAG LPSAARPGPR PGAGRRTGAP RPGNNPFASS QGMGQSRHRS EGGQRSGGSR
SGQGERMPRP GGSQGSRGGS GMPRPNPAMM PKHQSSQIGQ ATTGRGGRGG GRGRGGSRGS
GFGGGFGGGP RGPIGGGRGG RGGRGTQGAF GRGGGGRRGR KSRKQRRQEF DEMQAPLVGG
VRVRKGNGET VRLRRGASLT DLAEKINAEP AQLVQVLFNL GEMVTATQSV SDDTLEILGG
ELNYQIQVVS PEDEDRELLE SFDLEFGEDE GDDSDLVARP PVVTVMGHVD HGKTKLLDAL
RHTDVVKGEA GGITQAIGAY QVQTEVDDAE RAITFIDTPG HEAFTAMRAR GAQSTDIAVL
VVAADDGVMP QTVEALNHAK AADVPIVVAV NKIDKPEADP DKVRGQLTEY GLVPEEYGGD
TMFVNVSART HEGLDDLLEA IVLTADAALD LRANPDMAAQ GVAIEAHLDK GRGPVATALI
QRGTLHIGDS IVAGSSYGRV RAMINDQGES VDEAAPATPV QVLGLTSVPG AGDNFLVVDD
DRKARQIAEK REARMRAAQQ ARSSRRKTLD QLFEQLEKGE TEELLLILKG DGAGSVEALE
DALAKIDVGD EVDLRVIDRG VGAITETNVS LAAASNAVIV GFNVRPTAHA QRMADEENVD
IRYYSVIYDA IDEIEAALRG MLKPIYEEKA MGTAEIRQIF RSSKVGTIAG CMITDGTIRR
HAKARLVRDG VVVQETEINT LQREKDAVTE VREGYECGLT LTNYSDIHVG DEVQCYEMVE
KPRD
