ID A0A078LWJ6_9STAP Unreviewed; 698 AA.
AC A0A078LWJ6;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 45.
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:CDZ99578.1};
GN ORFNames=BN1048_00541 {ECO:0000313|EMBL:CDZ99578.1};
OS Jeotgalicoccus saudimassiliensis.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Jeotgalicoccus.
OX NCBI_TaxID=1461582 {ECO:0000313|EMBL:CDZ99578.1, ECO:0000313|Proteomes:UP000044136};
RN [1] {ECO:0000313|EMBL:CDZ99578.1, ECO:0000313|Proteomes:UP000044136}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13MG44_air {ECO:0000313|EMBL:CDZ99578.1,
RC ECO:0000313|Proteomes:UP000044136};
RA Urmite Genomes Urmite Genomes;
RL Submitted (JUL-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|ARBA:ARBA00025162, ECO:0000256|HAMAP-
CC Rule:MF_00100, 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}.
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DR EMBL; CCSE01000001; CDZ99578.1; -; Genomic_DNA.
DR RefSeq; WP_035808168.1; NZ_CCSE01000001.1.
DR AlphaFoldDB; A0A078LWJ6; -.
DR STRING; 1461582.BN1048_00541; -.
DR eggNOG; COG0532; Bacteria.
DR HOGENOM; CLU_006301_5_1_9; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000044136; 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; 1.10.10.2480; -; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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; 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; 2.
DR SUPFAM; SSF52156; Initiation factor IF2/eIF5b, domain 3; 1.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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|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:UP000044136}.
FT DOMAIN 199..368
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 53..120
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 202..350
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 65..95
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 96..120
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 208..215
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 254..258
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 308..311
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 698 AA; 76399 MW; 8A0537F051CA00C6 CRC64;
MSKIRIHEYA KEKGLTSKEI IDFLESKNIE VKSHMSSLED DVLKVLDAEF NKAAKKADSK
PAGNKPAAKQ NSKPNQQKNN KNKNQKNNKN QKNQKNSAPK KPEAKKEAPK QEKPAEKHFT
YEEGITVGEL AEKIGVDSSV IVKDLFMLGI VTNINQSLDQ DSVEVVAENY GFTSELEVFV
DDTDLTNFFN LEEQNLDEER PSVVTIMGHV DHGKTTLLDS IRNTKVTAGE AGGITQHVGA
YQIEHGDKKI TFLDTPGHAA FTTMRARGAQ VTDITILVVA ADDGVMPQTI EAINHAKAAE
VPIIVAVNKT DKPTANPDRV MTELGEHGLY PEDWGGDTIF VPLSALTGDG IDELLEMITL
VGEMAELKTT SDMPAIGTVI DAELDKSRGP AASLLVQHGT LNVGDSIVVG STFGKVRAMV
SDTGQRIKSA GPSVPVEITG INDVPEAGDR FVVFADDKKA RQIGEARHED KVMRDREVNQ
KVSLDNLFEQ MKEGEMKDLN VIIKGDAQGS VEALAASLMK IDVEGVNVRI IHTGVGAINE
SDVTLANASS AIIIGFNVRP DVNAKRAAEQ NQIDMRLHRI IYKVIEEIES AMKGMLDPEY
EEQVIGNVEV REIFKVSKVG TIAGAYVTDG KITRDSGVRV IRDGIVVFEG ELDTLKRFKD
DAKEVTTGYE CGLTIKNFND IKEGDQIEPF IMVEIERK
//
