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   27-MAR-2024, entry version 130.
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=PPA1493;
OS   Cutibacterium acnes (strain DSM 16379 / KPA171202) (Propionibacterium
OS   acnes).
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Propionibacteriaceae; 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   AlphaFoldDB; Q6A7M5; -.
DR   SMR; Q6A7M5; -.
DR   EnsemblBacteria; AAT83240; AAT83240; PPA1493.
DR   KEGG; pac:PPA1493; -.
DR   eggNOG; COG0532; Bacteria.
DR   HOGENOM; CLU_006301_9_0_11; -.
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; cd01887; IF2_eIF5B; 1.
DR   CDD; cd03702; IF2_mtIF2_II; 1.
DR   CDD; cd03692; mtIF2_IVc; 1.
DR   Gene3D; 1.10.10.2480; -; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   Gene3D; 2.40.30.10; Translation factors; 2.
DR   Gene3D; 3.40.50.10050; Translation initiation factor IF- 2, domain 3; 1.
DR   HAMAP; MF_00100_B; IF_2_B; 1.
DR   InterPro; IPR004161; EFTu-like_2.
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   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; PF03144; GTP_EFTU_D2; 1.
DR   Pfam; PF11987; IF-2; 1.
DR   Pfam; PF04760; IF2_N; 2.
DR   PRINTS; PR00315; ELONGATNFCT.
DR   SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR   SUPFAM; SSF50447; Translation proteins; 2.
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
//