ID U2QNK2_9BACT Unreviewed; 953 AA.
AC U2QNK2;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
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 ECO:0000313|EMBL:ERK40367.1};
GN ORFNames=HMPREF9135_0570 {ECO:0000313|EMBL:ERK40367.1};
OS Segatella baroniae F0067.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC Segatella.
OX NCBI_TaxID=1115809 {ECO:0000313|EMBL:ERK40367.1, ECO:0000313|Proteomes:UP000016648};
RN [1] {ECO:0000313|EMBL:ERK40367.1, ECO:0000313|Proteomes:UP000016648}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0067 {ECO:0000313|EMBL:ERK40367.1,
RC ECO:0000313|Proteomes:UP000016648};
RA Durkin A.S., Haft D.R., McCorrison J., Torralba M., Gillis M., Haft D.H.,
RA Methe B., Sutton G., Nelson K.E.;
RL Submitted (AUG-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Abolishes the inhibitory effect of tetracyclin on protein
CC synthesis by a non-covalent modification of the ribosomes.
CC {ECO:0000256|ARBA:ARBA00003987}.
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|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 -!- 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:ERK40367.1}.
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DR EMBL; AWEY01000007; ERK40367.1; -; Genomic_DNA.
DR RefSeq; WP_021588865.1; NZ_AWEY01000007.1.
DR AlphaFoldDB; U2QNK2; -.
DR PATRIC; fig|1115809.3.peg.388; -.
DR Proteomes; UP000016648; 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; 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; 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|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:UP000016648}.
FT DOMAIN 452..622
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 66..146
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 191..354
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 80..98
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 102..116
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 198..214
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..275
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..304
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..328
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 461..468
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 508..512
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 562..565
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 953 AA; 104421 MW; DA0620032F71C235 CRC64;
MSIRLNKALR ELNIGLQTAV EFLEKRTELG EVKPEPSFKL NDDQYNALVT AFKQDAEVRS
QAEKLFQKKN KEKKSVQASD NRAESLLASS SQQQFKPLGK IDLDQVGKKK PEAVKSVAAG
RPETAGKVTA AVSPKPEPKP VEIPVEKVEQ AAPNVEAKAE PVVEKKVEAV VEPAKEPVGK
EQPVAKPVEE VAAEVETEQT PKQESTTGVF QLKSEKKILN TPKVNVLGKI DLDSINQSTR
PKKKTKEERR KEREEKVASQ HGGERKKRVR INKERVDINA AANQQSDNGG NANSRNNNAK
GNSGGKKKNR NRNQKPLEVD DEAVARQVKE TLARLTSKSN QNKKGAKYRK EKREAVQEKL
QQEAYAERKD SKILKLTEFV TVSELATMMD ISVTQVISTL MSIGIMVSIN QRLDAETINM
VADEFGFKTE YVSAEVQEAV SEEEDDENDL VSRAPIVTVM GHVDHGKTSL LDHIRNTNVI
AGEAGGITQH IGAYGVTLKN GRKVTFLDTP GHEAFTAMRA RGAQVTDIAI IIIAADDSVM
PTTKEAIAHA QAAGVPMVFA INKIDKPGAN PDKIREDLAN MNLLVEEWGG KYQCQEISAK
KGIGVDELME KVLLEADMLD LKANPNRKAT GNIIESSLDK GRGFVSTVLV SNGTLKVGDV
VIAGTSWGHV KAMFNERNQR IESAAPAEPA IILGLNGAPT AGDAFHVLET DQEAREIANK
REQLQREQGL RTQKRLTLGD ISHRIARGEF HEFNIIVKGD TDGSIEALSD SFIKLSTEKV
QINVINKAVG QISENDVMLA SASDAVIVGF QVRPSSDARK LADREGVEIN TYSIIYDAID
DVKSAMVGML DKVKKEIVTG QIEVKQVFKI SKVGTVAGGM VMEGKVHNKD KARVVRDGIV
IRTADIDALK RYKDDVKEVA TGLECGISLV NFNDIEAGDI IETFTEIEVE QKL
//
