ID A0A161LCH9_9BACT Unreviewed; 998 AA.
AC A0A161LCH9;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 36.
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=PJIAN_184 {ECO:0000313|EMBL:GAT61505.1};
OS Paludibacter jiangxiensis.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Paludibacteraceae;
OC Paludibacter.
OX NCBI_TaxID=681398 {ECO:0000313|EMBL:GAT61505.1, ECO:0000313|Proteomes:UP000076586};
RN [1] {ECO:0000313|Proteomes:UP000076586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NM7 {ECO:0000313|Proteomes:UP000076586};
RA Qiu Y., Matsuura N., Ohashi A., Tourlousse M.D., Sekiguchi Y.;
RT "Draft genome sequence of Paludibacter jiangxiensis strain NM7.";
RL Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000076586}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NM7 {ECO:0000313|Proteomes:UP000076586};
RA Qiu Y.-L., Tourlousse D.M., Matsuura N., Ohashi A., Sekiguchi Y.;
RT "Draft genome sequence of Paludibacter jiangxiensis NM7(T), a propionate-
RT producing fermentative bacterium.";
RL Genome Announc. 0:0-0(2017).
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:GAT61505.1}.
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DR EMBL; BDCR01000001; GAT61505.1; -; Genomic_DNA.
DR RefSeq; WP_068701063.1; NZ_BDCR01000001.1.
DR AlphaFoldDB; A0A161LCH9; -.
DR STRING; 681398.PJIAN_184; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000076586; 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 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:UP000076586}.
FT DOMAIN 497..667
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 65..101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 134..191
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..370
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 387..413
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..101
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..162
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..235
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 269..286
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 287..313
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 314..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 334..348
FT /note="Polar 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 998 AA; 110287 MW; 6022046BF1964C16 CRC64;
MSSIRLNKVV KDLNVGLSTA VEFLRKKGHV VEENPNFKIS EDQYTILVKE FSNDKDLKIK
SERETQMRQE KEKAQTITAA GYEASVSKDK PKVEAKPEPK PVTHEIKVVV SDEIRPHITT
VGKIDLDALD KKVAPAPATP APEKQPEPTP EPEPVPAPKP EPVVEQKPEK IEEPAPEPVV
VPEPESPKAE PVVVEKKIEV EAVKEVVKEP VAVVEKVIEK PSEDNSSKEN AEPEVQNEGE
VFQLRPTVIE QNIKVVDKID LSALNQQTRP KKKSKEEKRK ERVQREQQNT PNNQQRPANP
SAASPATQQG SANADQRKEK RKRIHKEKVD LSKPNVPQGN NPARPNDNRH KGQGNMPKRP
FKPEVNEEDV QKQIKETLAR LTEKKIKGSK YRKEKRDSVS ARQQEREEME RDSENVLKLT
EFVTVAELAT MMDVPVTKVI GTCMNLGVMV SINQRLDAET INIVADEFGY KTEYVSSEVI
DAIAQDQEED RAEDMEARPP IVTVMGHVDH GKTSLLDHIR KANVIAGEAG GITQHIGAYH
VTLESGREIT FLDTPGHEAF TAMRARGAAV TDIAIIIVAA DDSVMPQTIE AINHASAANV
PMVFAINKID KPGANPEKIK EALANMNYLV EDWGGKYQSQ EISAKKGVGV HELLEKVLLE
ADLLELKANP NKRATGSIIE SSLDKGRGYV ATVLVKDGTL NIGDVVLAGT HFGRVKAMFN
ERNQRVTSVG PSEPVLILGL DGAPQAGDTF NVMPTEQEAR DIANKREQLQ REQGLRTSRH
ITLDEIGRRI AIGNFQELNV IVKGDVDGSI EALSDSLIKL STEEIQVNVI HKAVGQISES
DVMLAAASNA IIIGFQVRPS MSARKLAEKE EIDIRLYSII YNAIEELKAA MEGMLSPEIK
EEVVATLEVQ EVFKITKVGS VAGCIVREGK IKRGSKIRLI RDGIVVFSGE LGSLKRFKDD
VKEVGNGYEC GLNIANYNDI KTGDLIEGYE EVEVKKTL
//
