ID A0A1B8PHZ2_MORNO Unreviewed; 934 AA.
AC A0A1B8PHZ2;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=A9Z60_03995 {ECO:0000313|EMBL:OBX48819.1};
OS Moraxella nonliquefaciens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC Moraxella.
OX NCBI_TaxID=478 {ECO:0000313|EMBL:OBX48819.1, ECO:0000313|Proteomes:UP000092671};
RN [1] {ECO:0000313|EMBL:OBX48819.1, ECO:0000313|Proteomes:UP000092671}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 60284 {ECO:0000313|EMBL:OBX48819.1,
RC ECO:0000313|Proteomes:UP000092671};
RA Salva-Serra F., Engstrom-Jakobsson H., Thorell K., Gonzales-Siles L.,
RA Karlsson R., Boulund F., Engstrand L., Kristiansson E., Moore E.;
RT "Draft genome of Moraxella nonliquefaciens CCUG 60284.";
RL Submitted (JUN-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 -!- 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:OBX48819.1}.
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; LZDN01000040; OBX48819.1; -; Genomic_DNA.
DR RefSeq; WP_066893832.1; NZ_LZDN01000040.1.
DR AlphaFoldDB; A0A1B8PHZ2; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000092671; 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; 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; 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; 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:UP000092671}.
FT DOMAIN 436..605
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 191..227
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 299..342
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 439..587
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COILED 109..140
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 193..227
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 317..332
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 445..452
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 491..495
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 545..548
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 934 AA; 101688 MW; E15BD567B5E9C53D CRC64;
MATKTVKELA KDSKITTDVL LKQLKNAGLP IRGEDDAIST DEQATLVAFL KQSHGQAQKT
RIGMTQKTTT TKKITTTTGK AQNINVVRAK KKQFDIQKPD LVADQAKVQA EHEAKKAKAI
AALEAKQNEE RAKQEATKRQ ETTLAAMRAN SGNTNDSEHK PSASVVVKKV KKDNADTDSI
VSSTVVKKGL AVKSGVKTDK KEGKSDKAKK QSAKPIKSET EKERQARLAR EIEEQKLREI
EAENRRRAAI DAQNRTLEQM KQMANRYSEK DDVPSAVVRK DEPLAAGLVG AALEESFEKE
RREIKRGTGT AASRAKGGKK KGKEELEIRP KSRGLKSSQA SKHKFEMPLE KIIHNVEVGE
QIVVSDLAQK MAVKVREVVK SLMKMGEMVR ESDVIDQTTA ALVIEEFGHN FVAVSDTQLE
DDLQEAAIEK QGNVQIRPPV VTIMGHVDHG KTSLLDKIRE TKVASGEAGG ITQHIGAYHV
ETDRGVITFL DTPGHAAFTA MRSRGAQATD IVVIVVAADD GVMPQTEEAI DHARAAGTPI
IIAMNKMDKD TTDPERVLNE LSVKEVITDA WGGDTSLVKV SAKTGMGIDE LLDTISIQAE
IMELTAPVDG AAQGVVIESR LDKGRGAVAS LLVKKGTLKQ GDLVLAGEFY GKVRAMTDEN
GGRIKSAGPS IPVEILGLPD APMAGSEFLV VSDEKKAREV ADFRIARERE RLIERQNKMR
LENMFANMGS EAKTLNLILK TDVRGSLEAL LGALDDLSTD EVKVRVISSG VGAITESDVI
LAESSEAVLL GFNVRADTAG KRKADEAGLD IRYYSVIYGL IDDVKAAMSG MLAPEHREKI
LGVAEVRDVF RSSKFGAAAG CMVQEGTIYR NKPIRVLRDD KVIFTGQLQS LRRYKDDVNE
VKAGMECGLA VKGYDVVVGD KIEVFEIHEV ARTL
//
