ID M7PRF9_9GAMM Unreviewed; 928 AA.
AC M7PRF9;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 54.
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 ECO:0000313|EMBL:EMR13024.1};
GN ORFNames=MPL1_06859 {ECO:0000313|EMBL:EMR13024.1};
OS Methylophaga lonarensis MPL.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=1286106 {ECO:0000313|EMBL:EMR13024.1, ECO:0000313|Proteomes:UP000012019};
RN [1] {ECO:0000313|EMBL:EMR13024.1, ECO:0000313|Proteomes:UP000012019}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MPL {ECO:0000313|EMBL:EMR13024.1,
RC ECO:0000313|Proteomes:UP000012019};
RX PubMed=23661481;
RA Shetty S.A., Marathe N.P., Munot H., Antony C.P., Dhotre D.P.,
RA Murrell J.C., Shouche Y.S.;
RT "Draft Genome Sequence of Methylophaga lonarensis MPLT, a Haloalkaliphilic
RT (Non-Methane-Utilizing) Methylotroph.";
RL Genome Announc. 1:E00202-13(2013).
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:EMR13024.1}.
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DR EMBL; APHR01000035; EMR13024.1; -; Genomic_DNA.
DR RefSeq; WP_009726365.1; NZ_APHR01000035.1.
DR AlphaFoldDB; M7PRF9; -.
DR STRING; 1286106.MPL1_06859; -.
DR PATRIC; fig|1286106.3.peg.1376; -.
DR eggNOG; COG0532; Bacteria.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000012019; 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 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:UP000012019}.
FT DOMAIN 428..597
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 126..340
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 431..579
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 166..193
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 196..210
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 215..312
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 437..444
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 483..487
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 537..540
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 928 AA; 100846 MW; 82A388781273A4FF CRC64;
MSDMKVKDLA GTVGITAERL VDQLNEAGIK VSQPDDLITE EQKQTLLQFL QQRHGKSADG
ASVTPKKITL KRKSVSEIKL AGPTRAGKSV SVEVRKKRTY IKRSETEEAA AAAELLKQKE
AEDAAAEAAK LQQQELEAQQ QRERLMEQEA ADREAAAVAA AIEAEKQAAE EARLAAEEEQ
RALAEEAKAA AEEPPAKTQK SQNQEPALTA SQLAHKKLEE ADAKRRAANL ARIDAEKALE
ARRKAREEEE ALEKAREEAK QAAAEVQAKE QKAERQKEGD ARVHAKDKPA KRGKFQRDDE
FERKELHVSE GKTGRRKKKK GVSQPRGAVR DTAGEHGFSM PTAPVVREVS VPETISVSDL
AQRMSVKAAE VIKALMGLGT MATINQVLDQ DTAVIVVEEM GHVAKPTQDN EVELALTVSD
EDLGELKSRA PVVTVMGHVD HGKTSLLDYI RRTKVTTGEA GGITQHIGAY KVETSRGEIA
FLDTPGHAAF TEMRSRGAKV TDIVVLVVAA DDGVMPQTIE AIQHAKAAES ILIVAVNKMD
KPDANPDRVK QELVNHEVIP EDWGGDVQFV PVSALTGQGI DDLLDAISLQ AEIMELTAPV
EGPANGTVIE ARLDKGRGTV VTVLVQKGTL KKGDIVVVGQ EYGRVRALFD ENGQQLEQAG
PSTPVELLGL SSTPAAGDEL QVAPDERTAR EISYFRQTRA REMKMAQQQA AKLDDMFNKM
EAGDVKTLNV VIKADVHGSA EAVSQGLQKL STDLVQVRVI ASGVGGINET DAQLAAASDA
ILIGFNVRAD NTARKVIAEK GLDVQYFSII YDLLDVVTKA MTGMLEPVYK DEIIGLARVD
DVFRSPKFGD IAGCLVLEGM VKRNNPIRVL RDNVVIFEGE LESLRRFKDD VNEVSAGTEC
GIGVRNYKDV KPGDQIEVFE RVLMKPTL
//
