ID F0RZ13_SPHGB Unreviewed; 982 AA.
AC F0RZ13;
DT 03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2011, sequence version 1.
DT 02-APR-2025, entry version 75.
DE RecName: Full=Translation initiation factor IF-2 {ECO:0000256|ARBA:ARBA00020675, ECO:0000256|HAMAP-Rule:MF_00100};
GN Name=infB {ECO:0000256|HAMAP-Rule:MF_00100};
GN OrderedLocusNames=SpiBuddy_1395 {ECO:0000313|EMBL:ADY13220.1};
OS Sphaerochaeta globosa (strain ATCC BAA-1886 / DSM 22777 / Buddy)
OS (Spirochaeta sp. (strain Buddy)).
OC Bacteria; Pseudomonadati; Spirochaetota; Spirochaetia; Spirochaetales;
OC Sphaerochaetaceae; Sphaerochaeta.
OX NCBI_TaxID=158189 {ECO:0000313|EMBL:ADY13220.1, ECO:0000313|Proteomes:UP000008466};
RN [1] {ECO:0000313|Proteomes:UP000008466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1886 / DSM 22777 / Buddy
RC {ECO:0000313|Proteomes:UP000008466};
RA Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Zeytun A., Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N.,
RA Ivanova N., Mikhailova N., Pagani I., Ritalahti K.M., Loeffler F.E.,
RA Woyke T.;
RT "Complete sequence of Spirochaeta sp. Buddy.";
RL Submitted (FEB-2011) 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|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000644}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|ARBA:ARBA00004496,
CC ECO:0000256|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:0000256|ARBA:ARBA00007733, ECO:0000256|HAMAP-Rule:MF_00100,
CC ECO:0000256|RuleBase:RU000644}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00100}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP002541; ADY13220.1; -; Genomic_DNA.
DR RefSeq; WP_013607070.1; NC_015152.1.
DR AlphaFoldDB; F0RZ13; -.
DR STRING; 158189.SpiBuddy_1395; -.
DR KEGG; sbu:SpiBuddy_1395; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_12; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000008466; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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 FunFam; 2.40.30.10:FF:000007; Translation initiation factor IF-2; 1.
DR FunFam; 2.40.30.10:FF:000008; Translation initiation factor IF-2; 1.
DR FunFam; 3.40.50.10050:FF:000001; Translation initiation factor IF-2; 1.
DR FunFam; 3.40.50.300:FF:000019; Translation initiation factor IF-2; 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; IPR053905; EF-G-like_DII.
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.
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; PF22042; EF-G_D2; 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; 1.
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 {ECO:0000256|ARBA:ARBA00022490, ECO:0000256|HAMAP-Rule:MF_00100};
KW GTP-binding {ECO:0000256|ARBA:ARBA00023134, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Initiation factor {ECO:0000256|ARBA:ARBA00022540, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00100};
KW Protein biosynthesis {ECO:0000256|ARBA:ARBA00022917, ECO:0000256|HAMAP-
KW Rule:MF_00100}; Reference proteome {ECO:0000313|Proteomes:UP000008466}.
FT DOMAIN 473..643
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 1..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 21..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 75..88
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 180..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..211
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..229
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..267
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..281
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 296..338
FT /note="Gly residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..370
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 482..489
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 529..533
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 583..586
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 982 AA; 106574 MW; 3FA9870E3CE65AB8 CRC64;
MTEENNKPKA TLIKHVVTPS EQKEEPKSPA KEQDTKPKAP EKRRVVVVKK KVVVVKPQPK
SETELSTSDN AVEAPKSEEN TKSHDKQGAQ HRLGGVRRTP RPSTDKLTAS PLHNGPVVIR
PTNLPPVPNQ GLTVKDHAEL QNRAPDASAV QTPVPSSGPR IAGTVGGRPA PGTRPAYQGT
RPTSGYQGQN PRPQGQGAPV SQGYQGQNPR PQGQGYPASQ GYQGQNPRPQ GQGYQGQNPR
PQGQGYQGQN PRPQGQGYPS SQGYQGQNPR PSTPYQGTQP PRQGGFQSRP PYQGRPAGGA
PGQRPSGPGG FRPQGGGGGR PPFGQRPGGV GQRPGGAPGS QDMDTLNQRT PKKTFTKKKD
QASYKKRNAE EEKEFLIQRR KEQAAAKLAS VPKTVDMMEV ISVSDLAKKM NLKASEIIAK
LFKMGMMVTI NQQIDYETAE IICGEYNCQV HLVSLYDETL IASDPDSEDN LVDRAPIVTV
MGHVDHGKTK LLDAIRSTKV AEGEFGGITQ HIGAYKVNLP GKGEVVFLDT PGHAAFSMMR
ARGAQVTDIV ILVVAANDGV MPQTREAIDH ARAANVPIIV AINKCDLPEA KPERVMQQLS
DLGLMPEEWG GQTLYCQISA LKKIGIDELL DTVLLQAEML ELKANAGCRA EGKVIESRID
QGRGIVASVL IERGTLRQGD YYVAGIYPGR VRAMFDDKGR KIDIAGPSTP VEIIGLSDIP
GAGDPFQVTE DERQARQVGT KRQELERLGD SRNVKKVTLD NLYTKIKEGA IQEFNVIIKG
DVQGSVEALQ GSLEKLSNNE IHLNVIRASA GAIIESDVTL ASASDALVIG FNVRPTPRAQ
ALADQEKIEI RKYNIIYDVV DDIRLAMEGM LSPELREVEI GTVEVRDTFK VPRVGTIAGC
MVTKGKIKRN SLVRVIRDSI QLNSTMVKIT SLKRFKDDAK EVAEGFECGV GLENFNDLHV
GDILEVVETE EIARKLESSE KI
//
