ID A0A7V7KSY6_9GAMM Unreviewed; 851 AA.
AC A0A7V7KSY6;
DT 02-JUN-2021, integrated into UniProtKB/TrEMBL.
DT 02-JUN-2021, sequence version 1.
DT 28-JAN-2026, entry version 15.
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=DT594_17315 {ECO:0000313|EMBL:KAA0691335.1};
OS Halopseudomonas laoshanensis.
OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria;
OC Pseudomonadales; Pseudomonadaceae; Halopseudomonas.
OX NCBI_TaxID=2268758 {ECO:0000313|EMBL:KAA0691335.1, ECO:0000313|Proteomes:UP000463138};
RN [1] {ECO:0000313|EMBL:KAA0691335.1, ECO:0000313|Proteomes:UP000463138}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Y22 {ECO:0000313|EMBL:KAA0691335.1,
RC ECO:0000313|Proteomes:UP000463138};
RA Sun J., Yu L., Wang M., Zhang C.;
RT "Pseudomonas laoshanensis sp. nov., isolated from soil.";
RL Submitted (JUL-2018) 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|ARBA:ARBA00004496,
CC ECO:0000256|HAMAP-Rule:MF_00100, 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:KAA0691335.1}.
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DR EMBL; QOVF01000008; KAA0691335.1; -; Genomic_DNA.
DR RefSeq; WP_149334215.1; NZ_QOVF01000008.1.
DR AlphaFoldDB; A0A7V7KSY6; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000463138; Unassembled WGS sequence.
DR GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
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 FunFam; 2.40.30.10:FF:000007; Translation initiation factor IF-2; 1.
DR FunFam; 2.40.30.10:FF:000008; Translation initiation factor IF-2; 1.
DR FunFam; 3.40.50.10050:FF:000001; Translation initiation factor IF-2; 1.
DR FunFam; 3.40.50.300:FF:000019; Translation initiation factor IF-2; 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; IPR053905; EF-G-like_DII.
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.
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; PF22042; EF-G_D2; 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:UP000463138}.
FT DOMAIN 351..518
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 99..263
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 354..502
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 99..138
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 139..163
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..175
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 194..204
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 241..257
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 360..367
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 406..410
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 460..463
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 851 AA; 91684 MW; 31E75AC0D95DAC40 CRC64;
MAEVTVKDLA QVVGTPLERL LQQMQEAGLP QTSAEQRVSD DEKQKLLAFL KNSHGGDSAP
SEPRKITLKR KTVSTLKVAG SKTVNVEVRK KKTYVKRDPA ELEAERVREV DEQQAAEDVR
KAAVEAQRKA EEETRKAAEA AAAAKAETPA AAVTEAPAAA EAPAPAPAAP APAPAPEVQA
APTVIAPPAD KPDHSKKKDA HRKPTRAEEE EERSRKRAGG HAGKGRNATR SGSDDDEAMA
RRRGGGGKLK ANKKRNQHGF EKPTGPLVRE VVIGETITVS ELAQKMSIKA AEVIKYMFKS
GNMVTINQVL DQDTASIIAE DMGHKVKQIS DNDLEDALVS ASQAHEGELV NRAPVVTVMG
HVDHGKTSLL DYIRRAKVAS GEAGGITQHI GAYHVETERG MVTFLDTPGH AAFTAMRARG
AKATDIVILV VAADDGVMPQ TEEAVAHSKA AGVPLVVAIN KIDKEDADLD RIKNALAALD
VIPEEWGGDT MFMPVSAKAG TGIDELLEAV LLQAEVLELQ AQPSVPGRGV VVESRLDKGR
GPVATVLVQN GTLRQGDIVL AGVNYGRVRA MYDENGKPIK EAGPSIPVEI LGLDGTPDAG
DELTVVTDEK KAREVALFRQ GKFREIKLAR QQSSKLENMF DNLGQDEKKT LNIVLKSDVR
GSLEALQSSL SELGNEEVQV KIISGGVGGI TETDVNLALA SNAVVFGFNV RADATARKIV
ETEGLDLRYY SVIYEIIDDV KKALGGMLGS DVREQILGVA EVRDVFRSPK FGDVAGCMVI
EGTIHRNRPI RVLRQDVVIY EGELESLRRF KDDVAEVRNG MECGVGVKNY NDVKPGDRIE
VFERIQVQRS L
//
