ID A0A167JCW6_9FLAO Unreviewed; 946 AA.
AC A0A167JCW6;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=ULVI_07400 {ECO:0000313|EMBL:OAB80550.1};
OS Cochleicola gelatinilyticus.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Cochleicola.
OX NCBI_TaxID=1763537 {ECO:0000313|EMBL:OAB80550.1, ECO:0000313|Proteomes:UP000077013};
RN [1] {ECO:0000313|EMBL:OAB80550.1, ECO:0000313|Proteomes:UP000077013}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LPB0005 {ECO:0000313|EMBL:OAB80550.1,
RC ECO:0000313|Proteomes:UP000077013};
RA Shin S.-K., Yi H.;
RT "Ulvibacter sp. LPB0005, isolated from Thais luteostoma.";
RL Submitted (FEB-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:OAB80550.1}.
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DR EMBL; LRXL01000026; OAB80550.1; -; Genomic_DNA.
DR RefSeq; WP_068591229.1; NZ_LRXL01000026.1.
DR AlphaFoldDB; A0A167JCW6; -.
DR STRING; 1763537.ULVI_07400; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000077013; 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:UP000077013}.
FT DOMAIN 444..614
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 110..360
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 68..95
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 118..237
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 253..270
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..333
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 453..460
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 500..504
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 554..557
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 946 AA; 104631 MW; 1B702126060DC337 CRC64;
MAEVKSIRLN KVLREFNISL DRAVEFLKDK GHEVDARPTT KISNEEYQVL FEEFQTDKSK
KIESKEVGEE KRKEKEELRL EREREIEEKQ KKEAARVIKA EAKLDGPKQV GKVNLDASGK
VVKEKKAEEI EAKEKTPVEK PAAKEVVPEE KPEPPKAEKP PVKKEKPPVK VETPAAKTEE
KASVETPKEK PETKKEVVKE TSEVKKEPTK EKPAPAASEE TKTESETPEK TIVETKYKKL
DGPNFTGQKI DLTQFKKPEK KKTEKKGDNK ERKGRRRRIS KDTTARSGGG AKDNRARGKT
GGGRSNTPKE EPSEEEVQRQ VRETLEKLQG KSSKGKGAKY RREKRDSHRQ KTEDELAEQE
AGSKILKVTE FVTVSEIATM MDVPVTKIIS ACMSLGMMVT MNQRLDAETL SIVADEFDYE
VEFVNADIEE SIQVEEDAPE DLEDRAPIVT VMGHVDHGKT SLLDFIREEN VIAGESGGIT
QHIGAYGVTL KGGQKIAFLD TPGHEAFTAM RARGAQVTDL AIIVVAADDS IMPQTKEAIS
HAQAAGVPIV FAINKIDKPD ANPEKIKEGL AQMNLLVEDW GGKIQSHDIS AKTGQGVPEL
LEKVLLEAEL LELKANPNKL ANGTVVEAFL DKGRGYVSTI LVQGGTLKIG DYVLAGQHSG
KVKAMHDERG NDIAQAGPST PVSILGLDGA PQAGDKINVF LDEREAKSIA TKRTQLQREQ
SVRTQRHITL DEIGRRIALG DFKELNIILK GDVDGSVEAL TDSFQKLSTE EIQVNIIHKA
VGPITESDVL LASASDAIII GFNVRPMGNA RQIADKEEID IRTYSIIYAA INDLKDAMEG
MLSPVMKEEI LGTAEIRETF KISKVGTIAG CMVLTGKILR NSGIRLIREG VVVFTGELES
LKRFKDDVRE VAKGYDCGIQ IKNYNDIQEN DIIESFHEVA TKKKLK
//
