ID A0A086AZI2_9FLAO Unreviewed; 991 AA.
AC A0A086AZI2;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=IW22_02540 {ECO:0000313|EMBL:KFF22096.1};
OS Chryseobacterium sp. JM1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales; Weeksellaceae;
OC Chryseobacterium group; Chryseobacterium.
OX NCBI_TaxID=1233950 {ECO:0000313|EMBL:KFF22096.1, ECO:0000313|Proteomes:UP000028731};
RN [1] {ECO:0000313|EMBL:KFF22096.1, ECO:0000313|Proteomes:UP000028731}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JM1 {ECO:0000313|EMBL:KFF22096.1,
RC ECO:0000313|Proteomes:UP000028731};
RA Stropko S.J., Pipes S.E., Newman J.D.;
RT "Genome of Chryseobacterium sp. JM1.";
RL Submitted (JUL-2014) 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 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:KFF22096.1}.
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DR EMBL; JPRN01000002; KFF22096.1; -; Genomic_DNA.
DR RefSeq; WP_034723919.1; NZ_JPRN01000002.1.
DR AlphaFoldDB; A0A086AZI2; -.
DR eggNOG; COG0532; Bacteria.
DR Proteomes; UP000028731; 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 489..659
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 127..358
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 370..404
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 127..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 262..292
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 390..404
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 498..505
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 545..549
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 599..602
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 991 AA; 108353 MW; 005ED56FBAEA5F3B CRC64;
MPKIRLNKAV KEFNISMSRL VEFLQSKDFE VENNPNAQLE EAAYSALEAE FAKDGEQRKA
SHEVVITKVP EEKLEIEEKK TPEVIRAKAN KPETKILGKI DLEPKAPEVE EVPVAPVAAP
VPVAAPVEEK KKEEVVAEPE VKAAPEKQEF KVLDKIDLSQ IESRNRPVKK DKPKMEEKKE
EEKPAEPVKE TPKQPEPAAE KKAEPQKPAE PESQEPQKIE TVYQKLDGPK IVGEKIDLTQ
FAPKPGSGAK KKRKRIEKPG GPNQQGQGNN QNSGNNNNNQ GGQGNNRPQG QGGPGGNRPP
GQGGPGGNRP PGQGGPGGNR FGNNQGNRPP GQGGGFKKGP GGGNNNRPGQ RTMPVELTDE
QVKNQIKETL EKLTNKGGKS KSAKHRKDKR TYRREQDERQ QEIDAQDRTL KVTEFITVGE
LASLMNVSPT EVISACFSLG VMVTMNQRLE ADTLLLVADE FGFKIEFSDA DLEEVESEED
MDTEEDLSSR APIVTVMGHV DHGKTSLLDY IRKTNVIAGE SGGITQHIGA YNVKLENGQR
ITFLDTPGHE AFTAMRARGA QITDIAIIVI AADDDVMPQT REAISHAQAA GVPMIIALNK
VDRPSANPDN IRQQLSGMNI LVEEWGGNVQ AQEISAKFGN NMDVLLEKVL LQAEMLDLKA
NPDRAAQGVV IEASLDKGRG YVATMLVQTG TLRVGDYVVA GKNHGKVKAM LDERGRNLKE
AGPSIPVTIL GLDGAPTAGD KFKVYADESE AKTIANKREQ LQRELSIRTK KHTTLEELGR
RIALGEFKEL NIILKGDVDG SVEALSDQLQ RLSTAEINVN ILHKGVGQIT ESDVNLATAS
DAIIIGFNVR AGANAKELAD KEEIEIRTYS VIYAAIDEVK EAMEGMLSPE IKEQVMGNVE
IREVFKISKV GTIAGCMVLS GKVTRSSKVR VLRDGIVKFD GELESLKRFK DDVREVTKGY
ECGLNLKGYN DIEVGDILEV YEQVAVKKKL K
//
