ID A0A1W6B2V7_9GAMM Unreviewed; 896 AA.
AC A0A1W6B2V7;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=B1H58_05005 {ECO:0000313|EMBL:ARJ41430.1};
OS Pantoea alhagi.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Pantoea.
OX NCBI_TaxID=1891675 {ECO:0000313|EMBL:ARJ41430.1, ECO:0000313|Proteomes:UP000192900};
RN [1] {ECO:0000313|EMBL:ARJ41430.1, ECO:0000313|Proteomes:UP000192900}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LTYR-11Z {ECO:0000313|EMBL:ARJ41430.1,
RC ECO:0000313|Proteomes:UP000192900};
RA Zhang L.;
RT "Complete genome sequence of the drought resistance-promoting endophyte
RT Pantoea alhagi LTYR-11Z.";
RL Submitted (FEB-2017) 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}.
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DR EMBL; CP019706; ARJ41430.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1W6B2V7; -.
DR STRING; 1891675.B1H58_05005; -.
DR KEGG; palh:B1H58_05005; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000192900; Chromosome.
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:UP000192900}.
FT DOMAIN 395..562
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 46..307
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..546
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 46..78
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 82..160
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 171..259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 268..289
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 404..411
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 450..454
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 504..507
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 896 AA; 97843 MW; 6F83A768DFA3550C CRC64;
MTDVTVKSLA AEIQTSVERL VQQFADAGIR KSENDSVTQQ EKETLLTHLN RDNGSPSGKL
TLQRKTRSTL NIPGTGGKSK SVQIEVRKKR TYVKEDAEAE KAKAEAEAQA QREAEEQARR
EAEEKATREA AEKAKREAEE QAKREAAEKA KREAAESEKV TNQQTDEMTR AGQSDKARRE
AEAAELKRKV EEEARRKLEE DARRVAEEAR KLAEQKAGDW EVKPTESDDA DYHVTTSQHA
RQAEDENDRE VEGGRSRTRT TAKAPRPRKG NKHAEAKTDR EEARAAIRGG KGGKHRKGSA
LQQGFNRPAQ AVNRDVIIGE TITVAELANK MAVKGSQVIK AMMKMGAMAT INQVIDQETA
QLVAEEMGHK VILRRENELE EAVMSDRDTG AAAESRAPVV TIMGHVDHGK TSLLDYIRST
KIASGEAGGI TQHIGAYHVE TDNGMITFLD TPGHAAFTAM RARGAQATDI VVLVVAADDG
VMPQTIEAVQ HAKAAGVPVV VAVNKIDKPD ADPDRVKNEL TQYGIIPEEW GGENMFVNVS
AKAGTGVDDL LNAILLQSEV LELNAVRAGM ASGVVIESFL DKGRGPVATV LVREGTLRKG
DIVLCGFEYG RVRAMRDEMG HEVTEAGPSI PVEILGLSGV PAAGDEATVV RDEKKAREVA
LYRQGKFREV KLARQQKSKL ENMFANMTEG DVSELNIVLK ADVQGSVEAI SDSLLKLSTD
EVKVKIVGSG VGGITETDAT LAAASNAIIL GFNVRADASA RRVIEAESLD LRYYSVIYNL
IDEVKAAMSG MLAPEYKQQI IGLAEVRDVF KSPKFGAIAG CMVTEGVVKR HNPIRVLRDN
VVIYEGELES LRRFKDDVNE VRNGMECGIG VKNYNDVRTG DMIEVFEVIE IQRTIE
//
