ID J2K2Z7_9FLAO Unreviewed; 988 AA.
AC J2K2Z7;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
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=PMI13_04064 {ECO:0000313|EMBL:EJL67628.1};
OS Chryseobacterium populi.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1144316 {ECO:0000313|EMBL:EJL67628.1, ECO:0000313|Proteomes:UP000007509};
RN [1] {ECO:0000313|EMBL:EJL67628.1, ECO:0000313|Proteomes:UP000007509}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF314 {ECO:0000313|EMBL:EJL67628.1,
RC ECO:0000313|Proteomes:UP000007509};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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 ECO:0000256|RuleBase:RU000645}.
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:EJL67628.1}.
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DR EMBL; AKJY01000117; EJL67628.1; -; Genomic_DNA.
DR RefSeq; WP_007847165.1; NZ_AKJY01000117.1.
DR AlphaFoldDB; J2K2Z7; -.
DR PATRIC; fig|1144316.3.peg.4064; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000007509; 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; 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; 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.
DR PROSITE; PS01176; IF2; 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}.
FT DOMAIN 486..656
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 104..355
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 368..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 120..185
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 202..216
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 263..330
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 387..401
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 495..502
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 542..546
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 596..599
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 988 AA; 108635 MW; 94124AE2888CE44B CRC64;
MPKIRLNKAV KEFNISMSRL VEFLQSKGFE VESNPNAQLE EAAYSALDAE FAKDGEQRKA
SHEVVITKVP EEKLEIEEKK TPEVIRAKAN KPETKILGKI DLETKKPEVE EAPVATPVAK
PVEEKKEEAV AQEPEVKATP EKQEFKVLDK IDLSQIESRN RPAKKDKPKV EEKKAEEKPI
EPVKEAPKPV VEQPVAKPVE VKAEPQKTET ETEPQSQEPQ KIETVYQKLD GPKIVGEKID
LTQFAPKPSS GAKKKRKRIE KPGGPNQQNQ GNNQQGGNNN NNQQGGGNRP QGGNQGNRPQ
GQGGQGNRPP GQGGQGGNRF GNNNQGNRPP GQGGGFKKGG QNNRPGQRVM PVELTDEQVK
NQIKETLEKL TNKGGKSKSA KHRKDKRTFR REQDERQQEI DAQDRTLKVT EFITVGELAS
LMNVSPTEVI SACFSLGVMV TMNQRLEADT LLLVADEFGY KIEFSDADLE EVESEEDMDT
EEDLSPRAPI VTVMGHVDHG KTSLLDYIRK TNVIAGESGG ITQHIGAYNV KLENGQRITF
LDTPGHEAFT AMRARGAQIT DIAIIVIAAD DDVMPQTREA ISHAQAAGVP MIIALNKVDR
PNANPDNIRQ QLSGMNILVE EWGGNVQAQE ISAKFGNNMD ILLEKVLLQA EMLDLKANPN
RNAQGVVIEA SLDKGRGYVA TMLVQTGTLR VGDYVVAGKN HGKVKAMLDE RGRNLAEAGP
SIPVTILGLD GAPTAGDKFK VYEDESEAKT IANKREQLQR ELSIRTKKHT TLEELGRRIA
LGEFKELNII LKGDVDGSVE ALSDQLQRLS TAEINVNILH KGVGQITESD VNLATASDAI
IIGFNVRAGA NAKELAEKEE IEIRTYSVIY AAIDEVKEAM EGMLSPEIKE QVIGNVEIRE
IFKISKVGTI AGCMVLSGKV TRNSKVRVLR DGIVKFDGEL ESLKRFKDDV KEVTKGYECG
LNLKGYNDIE VGDILEVYEE VAVKKKLK
//
