ID A0A0D0SI65_STAGA Unreviewed; 688 AA.
AC A0A0D0SI65;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
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 ORFNames=BUZ01_01155 {ECO:0000313|EMBL:RIL44611.1};
OS Staphylococcus gallinarum.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1293 {ECO:0000313|EMBL:RIL44611.1, ECO:0000313|Proteomes:UP000283576};
RN [1] {ECO:0000313|EMBL:RIL44611.1, ECO:0000313|Proteomes:UP000283576}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SNUC 1388 {ECO:0000313|EMBL:RIL44611.1,
RC ECO:0000313|Proteomes:UP000283576};
RX PubMed=28066335; DOI=.3389/fmicb.2016.01990;
RA Naushad S., Barkema H.W., Luby C., Condas L.A., Nobrega D.B., Carson D.A.,
RA De Buck J.;
RT "Comprehensive Phylogenetic Analysis of Bovine Non-aureus Staphylococci
RT Species Based on Whole-Genome Sequencing.";
RL Front. Microbiol. 7:1990-1990(2016).
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|ARBA:ARBA00025162, ECO:0000256|HAMAP-
CC Rule:MF_00100, ECO:0000256|RuleBase:RU000644}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {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: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:RIL44611.1}.
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; QXRZ01000001; RIL44611.1; -; Genomic_DNA.
DR RefSeq; WP_042738843.1; NZ_RXWT01000329.1.
DR AlphaFoldDB; A0A0D0SI65; -.
DR GeneID; 69851253; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000283576; Unassembled WGS sequence.
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; 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; PF11987; IF-2; 1.
DR Pfam; PF04760; IF2_N; 2.
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.
DR PROSITE; PS01176; IF2; 1.
PE 3: Inferred from homology;
KW Cytoplasm {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}.
FT REGION 193..341
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 199..206
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 245..249
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 299..302
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 688 AA; 75516 MW; 1862CBD7D03F77B6 CRC64;
MSKQRIYEYA KELNIKSKDI IDELKKMNVE VSNHMQALEA DQIKELDKKF KASQSTDSKK
SQPKSNQKPA PKNNNKKNNK GNNKNNKGNN KNNKKQPKQE EPKETPSKIT YQDGITVGEL
ADKLNVDSSG IIKKLFLLGI MANINQSLDD ETLELIVDDY GVEIEKEVVI DEEDLSVYFD
DPSEDEQAVE RPAVVTIMGH VDHGKTTLLD SIRNTKVTAG EAGGITQHIG AYQIVNDGKK
ITFLDTPGHA AFTTMRARGA QVTDITILVV AADDGVMPQT IEAINHAKEA DVPTIVAVNK
IDKPTSNPDR VMQELTEYGL IPEDWGGDTI FVPLSALSGE GIDDLLEMIV LTSEVQELKA
NPSQRAVGTV IEAELDKSRG PAASLLVQNG TLNVGDPVVV GNTYGRIRAM VNDLGQRIKT
AGPSTPVEIT GINDVPQAGD RFVVFKDEKQ ARRIGEARHE SNVLQQRQES KSVSLDNLFE
QMKQGEMKDL NVIIKGDVQG SVEALAASLM KIDVEGVNVR IIHTAVGAIN ESDVTLANAS
NGIIIGFNVR PDTGAKRAAE AEGVDMRLHR VIYNVIEEIE SAMKGMLDPE YEEQVIGQAE
VRQTFKVSKV GTIAGSYVID GKITRNAGVR VIRDGIVQFE GELDTLKRFK DDAKEVAQGY
ECGITIEKYN DLKEGDIIEA FEMVEIKR
//
