ID A0A1E8FG57_9ALTE Unreviewed; 870 AA.
AC A0A1E8FG57;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, 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=BFC17_15200 {ECO:0000313|EMBL:OFI34911.1};
OS Alteromonas lipolytica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alteromonas/Salinimonas group; Alteromonas.
OX NCBI_TaxID=1856405 {ECO:0000313|EMBL:OFI34911.1, ECO:0000313|Proteomes:UP000176037};
RN [1] {ECO:0000313|EMBL:OFI34911.1, ECO:0000313|Proteomes:UP000176037}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JW12 {ECO:0000313|EMBL:OFI34911.1,
RC ECO:0000313|Proteomes:UP000176037};
RA Wu Y.-H., Cheng H., Xu X.-W.;
RT "Alteromonas lipolytica, a new species isolated from sea water.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
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: 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:OFI34911.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; MJIC01000010; OFI34911.1; -; Genomic_DNA.
DR RefSeq; WP_070175829.1; NZ_MJIC01000010.1.
DR AlphaFoldDB; A0A1E8FG57; -.
DR STRING; 1856405.BFC17_15200; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000176037; 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:0097216; F:guanosine tetraphosphate binding; IEA:UniProt.
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; 3.30.56.50; Putative DNA-binding domain, N-terminal subdomain of bacterial translation initiation factor IF2; 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; IPR009061; DNA-bd_dom_put_sf.
DR InterPro; IPR004161; EFTu-like_2.
DR InterPro; IPR013575; IF2_assoc_dom_bac.
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; PF08364; IF2_assoc; 1.
DR Pfam; PF04760; IF2_N; 2.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1.
DR SUPFAM; SSF46955; Putative DNA-binding domain; 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:UP000176037}.
FT DOMAIN 370..543
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 30..282
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 373..521
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COILED 638..665
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 33..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..263
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 379..386
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 425..429
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 479..482
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 870 AA; 95680 MW; 7780E81B3F2F320A CRC64;
MADVSIEKLA SDIGTSVDRL VSQFSDAGIK KAAGESVTED EKRKLLDHLS KQHGGTNAGA
EPKKMTLQRK TTSTLSVGKS KEVKVEVRKK KTYVKRTDIE EQRQAEEEAK RREEEARLKR
EAEEKAAEDA RKAAEEKARK AEEARKAAEE EKARRAEKAK QEAAARAEAE SELTEEEKQE
QEAARQEEER LRKQQEEEAQ RKLEEDAKKA AEEARKLAEE NERRWKEEEE RRKQAEAEEV
HMHSNRYAQE AEDEEDMQVE RSSRRRKKPK KNASESLKQG FNKPAAPVER VVKLGETITV
GELASRLAIK VQEVIKAMMK MGEMATINQV LDQDTAVLVV EEMGHKYELV NDNALEDELL
AESGAGEKDT RAPVVTIMGH VDHGKTSLLD YIRRAKVAAG EAGGITQHIG AYSVDTDLGK
ITFLDTPGHA AFTAMRARGA TATDIVVLVV AADDGVMPQT KEAVQHARAA GVPLIIAVNK
MDKESADPDR VKTELSQLEV ISEEWGGEHQ FVNVSAKTGM GVDELLEAIS LQAEVLDLKA
TPTGPGRGIV IESRLDKGRG PIASVLVQEG QVKAGDILLC GEEYGRVRAM RDENGQDVKL
AGPSTPVEIL GLSGVPVAGE DALVVSDERK AREVAGKRHQ KKRELKLARQ QKAKLENMFA
NMEAGDVSEL NIVLKADVQG SVEAISESLM KLSTSEVKVN IVGSGVGGIT ETDASLAAAS
SAIIVGFNVR ADATARRVIE AEEIDLRYYS VIYDLIDEVK AAMSGMLAPE FKQEIMGLAE
VRDVFKSPKL GAIAGCMVTE GTVKRSNPIR VLRDNVVIYE GELESLRRFK DDVQEVRNGM
ECGIGVKNYN DVKVGDQIEV FQVVEVKREI
//
