ID X7E5P8_9GAMM Unreviewed; 847 AA.
AC X7E5P8;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=MUS1_14655 {ECO:0000313|EMBL:ETX10473.1};
OS Marinomonas ushuaiensis DSM 15871.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=1122207 {ECO:0000313|EMBL:ETX10473.1, ECO:0000313|Proteomes:UP000054058};
RN [1] {ECO:0000313|EMBL:ETX10473.1, ECO:0000313|Proteomes:UP000054058}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15871 {ECO:0000313|EMBL:ETX10473.1,
RC ECO:0000313|Proteomes:UP000054058};
RA Lai Q., Shao Z.S.;
RT "Marinomonas ushuaiensis DSM 15871 Genome Sequencing.";
RL Submitted (JAN-2014) 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:ETX10473.1}.
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DR EMBL; JAMB01000008; ETX10473.1; -; Genomic_DNA.
DR RefSeq; WP_036162142.1; NZ_JAMB01000008.1.
DR AlphaFoldDB; X7E5P8; -.
DR STRING; 1122207.MUS1_14655; -.
DR PATRIC; fig|1122207.3.peg.2081; -.
DR eggNOG; COG0532; Bacteria.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000054058; 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; 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; PF11987; IF-2; 1.
DR Pfam; PF08364; IF2_assoc; 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 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:UP000054058}.
FT DOMAIN 347..516
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 51..79
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 124..262
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 350..498
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 64..79
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 124..139
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 193..254
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 356..363
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 402..406
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 456..459
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 847 AA; 91964 MW; 07CB28CC6F832F4A CRC64;
MTVQTVKILS ELVNTPVDKL LTQMKDAGLP QTSASQEVSE VEKQTLLSFL KRQHGEEGDN
SQRITLQRKT TSTLSRSDGG KAVNVAVKKK RTYVKRDDAD EEAQKQEEKR LAEEVRLEAE
RKLEQEKAAK EKAAAEEKAR QEAVAASSVV GVGAVNETEQ KVSDTGAVEP VESPKQPKAA
KKPQPAVENK KPAAAPKGKK GPARHDNDNN KDKDKPRGRA PENKRGSRVN LNGDDDQRRG
KLGRKNKKSA SKQEHGFQKP TAKIVHEVAL PESITVAELA EKMSVKGAAV IKVMFKMGAM
ATINETIDRD TAILVVEEMG HTVTFIDENA VENDMIEAID YEGEAIKRAP VVTVMGHVDH
GKTSLLDYIR TTRVAAGESG GITQHIGAYH VETPHGMVSF LDTPGHAAFT SMRARGAKAT
DIVILVCAAD DGVMPQTIEA IQHARAAGVP MVVAITKIDK EGADIDRVKN ELVAQEVVPE
EWGGDVQFIG VSAKSGEGIE ELLEAVLLQS EVLELTAVPS SPAKGVVVEA RLDRGRGSVA
TLLIQNGTLK KGDVVLAGLQ MGRVRALLDE NGKPIDSAGP SIPVEILGLD GTPDAGEEFI
VVANERKARE VANFRQGRYR EVRFARQHTA KLENLFSEMG KDEIRTLNVV LKADVRGSLE
ALIKSLIDLN TDEVQVNIVS SGVGGITETD ASLALASDAV IFGFNVRADT SAKQLIEREA
IDLRYYSIIY NIIDDVKSAL SGMLSPDLRE DIQGTAEVRD VFNSPKFGLI AGCMVVEGTV
YRNKQIRVLR EDVVIYEGEL ESLRRFKDAV NEVGRGIECG IGVKNYNDVK VGDKIEVFET
VEVARTL
//
