ID A0A163VV18_9FLAO Unreviewed; 1002 AA.
AC A0A163VV18;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
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=AV926_01510 {ECO:0000313|EMBL:KZE75438.1};
OS Myroides marinus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Myroides.
OX NCBI_TaxID=703342 {ECO:0000313|EMBL:KZE75438.1, ECO:0000313|Proteomes:UP000076630};
RN [1] {ECO:0000313|EMBL:KZE75438.1, ECO:0000313|Proteomes:UP000076630}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L41 {ECO:0000313|EMBL:KZE75438.1,
RC ECO:0000313|Proteomes:UP000076630};
RA Hong K.W.;
RT "Whole genome sequencing of Myroides marinus L41.";
RL Submitted (JAN-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}.
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:KZE75438.1}.
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DR EMBL; LQNU01000083; KZE75438.1; -; Genomic_DNA.
DR RefSeq; WP_038985967.1; NZ_LQNU01000083.1.
DR AlphaFoldDB; A0A163VV18; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000076630; 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 500..670
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 57..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 119..411
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 119..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 185..232
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 233..257
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..272
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 302..362
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 367..389
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 509..516
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 556..560
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 610..613
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 1002 AA; 109677 MW; 2E28BD3962DA1D17 CRC64;
MSEERAIRIN KVLRELNISL DRAVDFLKGK GFDIDATPNA KISDTEYSVL CKQFSADKGK
KEASIEVSEE KKKEKEALKI ERDKELEEKK KQEEARIKRE QEVIRAKAEE IAAIKTVGKI
DLEPKKTKAS SDDSNKENKS FDKDAQAPAK ENKQKQSTEV IEDKKETVAK PVVEKEASKV
TNSSKQVEAK KEVEKPKQKE SVAGSKDASS KNVDSKKVES KPAEDTAKTG EAVEETIKTN
YQKLSGTTFT GQTIDLSQFD KPKKKKEDPK KGGNNAGNNA KNNGAGAAGN KNKRKRIAKP
GTEGANTTNN NSNTNNNAGG GNNNNNNNRN QGGGQRNNNN NNNNAGGNKF GNRNQRRNQQ
APIVKAEPTE EEVKNQIKET LERLQGKGNK SKSAKYRRDK RDVHRKKTDD EQKALEAGSK
VLKVTEFVTV GEIATMMDVP ITKVIGTCMS LGIMVTMNQR LDAETLSIVA DEFGYEVDFT
TAAIEEAIEE APDNPEDLVS RAPIVTVMGH VDHGKTSLLD YVRKANVIAG ESGGITQHIG
AYGVTLENGQ KITFLDTPGH EAFTAMRARG AQVTDIVIIV IAADDDIMPQ TKEAISHAQA
AGVPIIFAIN KVDKPTANPE KIKEKLAAMN FLVEDWGGTY QSQDISAKQG IGMSELLEKV
LLEAEMLDLK ANPNKLAVGT VVEAFLDKGR GYVSTVLVQA GTLRVGDYLL AGCNHGKVRA
MHDERGKSIK VAGPSTPISV LGLDGAPTAG DKFNVFEEEK EAKQIASKRT QLIREQSVRA
QRHITLAEIG RRIALGDFKE LNIILKGDVD GSVEALSDSF SKLSTEEIQV NIIHKGVGAI
TESDVLLASA SDAIIIGFNV RPMASAKQLA DKEEIDIRNY SIIYAAIDDL KDAMEGMLSP
ELKEEVTGTA EIRELFKISK VGTIAGCMVT DGKIFRSSRI RLIREGVVIY TGELTALKRF
KDDVKEVSKG YDCGIQIKNY NDIKEYDVIE AFQEVEVKKK LK
//
