ID A0A1M6GLN9_9FLAO Unreviewed; 999 AA.
AC A0A1M6GLN9;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 27-MAR-2024, entry version 29.
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=SAMN04487911_11159 {ECO:0000313|EMBL:SHJ10869.1};
OS Arenibacter nanhaiticus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Arenibacter.
OX NCBI_TaxID=558155 {ECO:0000313|EMBL:SHJ10869.1, ECO:0000313|Proteomes:UP000184231};
RN [1] {ECO:0000313|EMBL:SHJ10869.1, ECO:0000313|Proteomes:UP000184231}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.8863 {ECO:0000313|EMBL:SHJ10869.1,
RC ECO:0000313|Proteomes:UP000184231};
RA Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL Submitted (NOV-2016) 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; FQYX01000011; SHJ10869.1; -; Genomic_DNA.
DR RefSeq; WP_072764366.1; NZ_FQYX01000011.1.
DR AlphaFoldDB; A0A1M6GLN9; -.
DR STRING; 558155.SAMN04487911_11159; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000184231; 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 Coiled coil {ECO:0000256|SAM:Coils};
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:UP000184231}.
FT DOMAIN 497..667
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 118..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 303..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 65..97
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 127..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 156..177
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 303..321
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..411
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 506..513
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 553..557
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 607..610
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 999 AA; 109582 MW; 1DBA16DCA334E1F8 CRC64;
MADNATIRLN KVLRELNISL DRAVDYLGSK GHDIEARPTT KISNEVYQVL LDGFQTDMSK
KVASKEVGEE KRKEKEAIRL QLEQEQEEKK LAREKRAKEG IVKARVELAG PKTVGKIDLD
QPKKAATPVA PKEEEKTVKE PETAPEVTVG KASEPVVEKT VDKVDAPVEK EEVAPKVEAA
APESQKAEPV KPAPVKEESV KEEPVKAAPV KAEPKKTGPV KKEEVKDVPV VKETEKKTDE
VKQAPVKEVT EKKEAEKVET DKKEAIVGED GRAIETEVIT TKYQKLSGPK IMGAKIDLTQ
FEKPKKKKEV AKAGDAADKK KRRKRIVTKP GAGGDANKPA AARPRGPVVR RAPGQRFTPA
AKVEPTEEDV QKQVRETLEK LQGKSKKGKG AKYRRDKRDQ HRQQTEKDLE KQELESKILK
VTEFVTASEV ATMMDVPTTK IISACMSLGI MVTMNQRLDA ETLSIVADEF GYEVEFVTAD
LEESIVEEPD AEEDLVARAP IVTVMGHVDH GKTSLLDYIR KENVIAGESG GITQHIGAYG
VTLEGGQKIS FLDTPGHEAF TVMRARGAQV TDIAIIVVAA DDAIMPQTKE AISHAQAAGV
PIIFAINKID KPHANPDKIK EGLAQMNLLV EDWGGKVQSH DISAKIGTGV KELLEKVLLE
AELLELKANP KKLASGTVVE AFLDKGRGYV STILVQAGTL KVGDYVLAGT CSGKVKAMHD
ERGKIVKEAG PSRPVSILGL DGAPQAGDKF NVLLDEREAK QIATKRSQLL REQSVRTQRH
ITLDEIGRRI ALGDFKELNI ILKGDVDGSV EALTDSFQKL STAEIQVNII HKAVGPITES
DVLLASASDA VIIGFNVRPM GNARMLADKE EIDIRMYSII YDAINDLKDA MEGMLSPEMK
EEITGTAEIR ETFKISKVGT IAGCMVTTGK IYRNSNIRLI RDGVVIYTGE LSSLKRFKDD
VKEVAKGYDC GLQVKNYNDI RELDIVEAFQ EVEVKKKLK
//
