ID A0A1T4RGK7_9BACT Unreviewed; 1201 AA.
AC A0A1T4RGK7;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=SAMN04488128_1021116 {ECO:0000313|EMBL:SKA15039.1};
OS Chitinophaga eiseniae.
OC Bacteria; Bacteroidota; Chitinophagia; Chitinophagales; Chitinophagaceae;
OC Chitinophaga.
OX NCBI_TaxID=634771 {ECO:0000313|EMBL:SKA15039.1, ECO:0000313|Proteomes:UP000190367};
RN [1] {ECO:0000313|EMBL:SKA15039.1, ECO:0000313|Proteomes:UP000190367}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22224 {ECO:0000313|EMBL:SKA15039.1,
RC ECO:0000313|Proteomes:UP000190367};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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}.
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DR EMBL; FUWZ01000002; SKA15039.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T4RGK7; -.
DR STRING; 634771.SAMN04488128_1021116; -.
DR Proteomes; UP000190367; 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.
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 DOMAIN 701..871
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 73..317
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 331..616
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 92..121
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 128..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 170..184
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..231
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..267
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 301..317
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..433
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 448..472
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 473..537
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 556..579
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 599..616
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 710..717
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 757..761
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 811..814
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1201 AA; 130096 MW; 72CB64AC49483DBD CRC64;
MEKTGNRGGP KYDMPETTNN TPRLLAAAKE FNIGKETLID FLSNKGFDMG GFGSPNARLT
AVMYTALQSE FQQDKANKRK SDQIALPKGS VLETKMKKEK EEAEAAAKKN LKDKDEAAPV
AEAPKAEQAP EPKQEPVKET PKKEPQAAAP AQPTPPPVKE KEEAKPKQEP PAVTAPPVAE
VPKAPATPAE PEVVKTESPK INGPKVITTI DLDALNRNKK PAAKKEPEEK PAPQPAAPAP
KEEKPQPVTP PVAAKPEEKP EPTPAPTAPV AKQEDVEKAA PKAEKAETAP APQAEKVAQT
VKTDTTEKTE KAAPVEDKPV VNKVEEVLQE AKPAAIKEPA NIPVKQPVKE EQRNIPPAPA
AENTPTPPQQ PEEPTVISNI QAEKLTGPKV IGKIELPVQS DRRDNNKGNF NRDEKRKRKR
IIVEKKPEPI QPKDFKEGGQ QGQGGGNRPH HENRDNRGDN RGGNRPHGDN RNQGDNRNQG
GGQGHNRPGG QQGQGGGFNR GGQQGGGFNR GQGGGQGGNR QGGQQGGNFN RQGGGQGGNR
PGFNRPGQGG NFRPGGRGAD DKRTVEEKEI DKNEIQNKIK ETMAKLGGGG RGKNVKAKHR
REKREERASQ KAKEGVEDNK LQVTEFVSVS ELANLMDVSF AEVISKCMGL GIMVSINQRL
DAEVIELVAG EFGYEVEFIG LDAVEDSEEE EDVDAPEDLL PRAPIVTIMG HVDHGKTSLL
DYIRSANVVA GEAGGITQHI GAYQVTTANG KKITFLDTPG HEAFTAMRAR GAKAADIAVI
VVAADDAIMP QTREAISHSQ AAGLPMVFAI NKIDKEGANP EKIKEQLAQL NLLVEDWGGK
YQSQEISAKS GLNIDVLLEK ILLEAELLEL KANPNREGSG SIVEASLDKG RGYVASLLVQ
NGTLRQGDTI VSGSFYGKIK AMFNERGQRM EEAGPSMPVQ VLGLNGAPQA GEKFKMYEDE
SEAKETANRR AQIVREQGIR TKKHITLDEI GRRLALGNFK QLNLIIKADF DGSVEALSDS
LQKLSTEEIV ISIVHKAVGQ ITESDVLLAT ASDAIILGFQ VRPSSQAAKL AEKENIEIRN
YSIIYDAIDE IKSAMEGMLE PKIEKKVVCN VQVRETYKFD KVTVAGCFVL DGKLTRNTRI
NVVRDGIVVH TGELGSLKRY KDDVKEVAAN MECGLSIRNY SDLRPDDIIE GFEEVEVKRT
L
//
