ID K2Q1P1_9FLAO Unreviewed; 971 AA.
AC K2Q1P1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
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 ECO:0000313|EMBL:EKF54741.1};
GN ORFNames=I215_11155 {ECO:0000313|EMBL:EKF54741.1};
OS Galbibacter marinus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Galbibacter.
OX NCBI_TaxID=555500 {ECO:0000313|EMBL:EKF54741.1, ECO:0000313|Proteomes:UP000007364};
RN [1] {ECO:0000313|EMBL:EKF54741.1, ECO:0000313|Proteomes:UP000007364}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ck-I2-15 {ECO:0000313|Proteomes:UP000007364};
RX PubMed=23209227; DOI=10.1128/JB.01852-12;
RA Lai Q., Li C., Shao Z.;
RT "Genome Sequence of Galbibacter marinum Type Strain ck-I2-15.";
RL J. Bacteriol. 194:6973-6973(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:EKF54741.1}.
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DR EMBL; AMSG01000016; EKF54741.1; -; Genomic_DNA.
DR RefSeq; WP_008992071.1; NZ_AMSG01000016.1.
DR AlphaFoldDB; K2Q1P1; -.
DR STRING; 555500.I215_11155; -.
DR PATRIC; fig|555500.3.peg.2299; -.
DR eggNOG; COG0532; Bacteria.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000007364; 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 Coiled coil {ECO:0000256|SAM:Coils};
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}; Reference proteome {ECO:0000313|Proteomes:UP000007364}.
FT DOMAIN 470..640
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 104..384
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 65..104
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 116..213
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..240
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..258
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 260..293
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..359
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 479..486
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 526..530
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 580..583
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 971 AA; 107668 MW; 2CB39C3CAE16F606 CRC64;
MAESAKLRLN KVLRELNISL DRAVEHLSSK GFDIEARPTT KITNEVYNVL LDEFQTDRSK
KVASKEVGEE KRKEKEAIRQ ELEKENELKR QKQLEEEQEI IRARATLSGP KTVGKIELSG
KKKDDAAAAD ASKEEKPIDK VEEQSPSLET KPKTETKADP VEKEPIKEEK QAEEKTAKTE
TKKEEKPAEK TPEKSTEPVK DTKPEEVKKP QAPKAVETPK APIKTKKMIV DDEVVDSEQI
KTKYTKLSGP NFTGEKIDLS QFNKPKKKKE TKEDPNKKGA KSTGSADDKK KRRRRISKDN
KDSRPGSGNN SGNRFNKDNN KNRRKGAGQR RPVEKVEPTE EEVQKQVRET LEKLQGKASK
SKGAKYRREK RDFHRQKTEQ EIAQQEAESK TLRVTEFVTV SELATLIDVP VTKIISACMS
LGMMVTMNQR LDAETLTIIA EEFGYEVEFI TVDLEDTEVE KVDAPEDLES RAPVVTVMGH
VDHGKTSLLD YIREENVIAG ESGGITQHIG AYGVTLKNGQ KITFLDTPGH EAFTAMRARG
AQVTDMAIIV IAADDDVMPQ TKEAISHAQA AGIPIVFAIN KVDKPTANPD KIKEGLANMN
LLVEDWGGKI QSQDISAKSG LGVPELLEKV LLEAELLELK ANPNKSAVGA VVEAYLDKGR
GYVSTVLVQG GTLKIGDYLL AGTHSGKVKA MQDERGNNIP EAGPSTPISV LGLDGAPQAG
DKFNVYEDEK EAKQIAAKRT QLQREQSVRT QRHITLDEIG RRIALGEFKE LNIILKGDVD
GSVEALTDSF QKLSTEEIHI NIIHKAVGPI TESDVLLATA SDAIIIGFNV RPMGNARSIA
DKEEIDIRTY SIIYDAINDL RDAMEGMLSP ELKEEITGTA EIRETFKISK VGTIAGCMVT
DGKIYRNSGI RLIRDGVVIF TGELTSLKRF KDDVKEVSKG YDCGLQVKNY NDIQIGDIVE
SFREVEVKKK L
//
