ID A0A1I7HB63_9FLAO Unreviewed; 961 AA.
AC A0A1I7HB63;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
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=SAMN05216480_10847 {ECO:0000313|EMBL:SFU57746.1};
OS Pustulibacterium marinum.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Pustulibacterium.
OX NCBI_TaxID=1224947 {ECO:0000313|EMBL:SFU57746.1, ECO:0000313|Proteomes:UP000199138};
RN [1] {ECO:0000313|EMBL:SFU57746.1, ECO:0000313|Proteomes:UP000199138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.12333 {ECO:0000313|EMBL:SFU57746.1,
RC ECO:0000313|Proteomes:UP000199138};
RA de Groot N.N.;
RL Submitted (OCT-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; FPBK01000008; SFU57746.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I7HB63; -.
DR STRING; 1224947.SAMN05216480_10847; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000199138; 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}; Reference proteome {ECO:0000313|Proteomes:UP000199138}.
FT DOMAIN 460..628
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 58..376
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 58..97
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..223
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 244..267
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 278..306
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 320..349
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 469..476
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 516..520
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 570..573
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 961 AA; 105996 MW; 8C19B1276F08A55A CRC64;
MSEHKTIRLN RVLRELNISL DRAVEYLAAK GHDVEARPTT KISNEVYGVL LAEFQTDKSK
KVASKEVGEE KRKEKEAIRL ELEKEQEKKR KAEESSVVKA RASLSGPKTV GKIDLNPKKE
TVEKQPVQED KKEEQQPVKV EEKAAEVKQV PEVKKETPVK KEAPKEEVAP EVKQKPVETP
KNEPVQKPKP QEFKKENKPV GKPVAKQEKP KQEVKEESGE PEVIQTQYKK LSGPKVVGEK
IDLSQFQKPK KKKEDNKSKG NNNSNRDNNK KKRKRITSNN NSGGNNANPN SGGGNRSNNN
RGGNRPNPNA GKGKKGGSKF RTVKREEPSE EDVQKQVRET LEKLQGKSSK NKGAKYRREK
RDTHRQKTQD EIAQQEADSK VLKVTEFVTV DEVATMMDVP INKVIGACMS LGIMVTMNQR
LDAETLSIVA DEFGYEVEFV TADIEEAIQD APDAEEDLKA RAPIVTVMGH VDHGKTSLLD
YIREENVIAG ESGGITQHIG AYGVKLESGQ RIAFLDTPGH EAFTAMRARG AQVTDIAIIV
IAADDDIMPQ TKEAISHAQA AGVPMIFAIN KIDKPTANPD RIKERLAGMN LLVEDWGGSI
QSHDISAKKG TGVKELLEKV LLEAEILDLK ANPDKAASGT IVEAYLDKGR GYVATVLVQA
GTLKVGDYVL AGKHSGKVKA LHDERGNVVK EAGPSTPVSV LGLDGAPQAG DKFNVFEDER
EAKQIAAKRT QLQREQSVRT QRHITLDEIG RRIALGDFKE LNVILKGDVD GSVEALTDSF
QKLSTEEIQI NIIHKAVGPI TESDVLLASA SDAIIIGFNV RPMGNARSIA DKEEIDIRTY
SIIYDAINDL KDAMEGMLSP EMKEEITGSA EIRETFKISK IGTIAGCMVT DGKIYRSSGI
RLIRDGVVIY TGELASLKRF KDDVKEVSKG YDCGMQVKNY NDIKEGDIIE AFQEVAVKKK
L
//
