ID A0A1G8PPY3_9BACI Unreviewed; 720 AA.
AC A0A1G8PPY3;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
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=SAMN04488123_10954 {ECO:0000313|EMBL:SDI94609.1};
OS Natribacillus halophilus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Natribacillus.
OX NCBI_TaxID=549003 {ECO:0000313|EMBL:SDI94609.1, ECO:0000313|Proteomes:UP000198853};
RN [1] {ECO:0000313|EMBL:SDI94609.1, ECO:0000313|Proteomes:UP000198853}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21771 {ECO:0000313|EMBL:SDI94609.1,
RC ECO:0000313|Proteomes:UP000198853};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 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; FNEN01000009; SDI94609.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1G8PPY3; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000198853; 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; IPR004161; EFTu-like_2.
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; 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|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:UP000198853}.
FT DOMAIN 221..390
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 33..140
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 224..372
FT /note="G-domain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT COMPBIAS 65..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 230..237
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 276..280
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 330..333
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 720 AA; 78644 MW; C7816E757B707AAB CRC64;
MPKMRVYEYA RSVNRPSKDV VADLKAKNIA VSNHMSVIDD EQIAQLEQAQ PAKKQEERPG
GNRQTKQSKP KQGNEASRPQ NNNQKTNQGN KAQGNKQRGK KNNAQQRSQQ RGGNHGPGRR
GKSNKNQKRR TKEAPKMPEK ITFAGSLTVA ELAEKLTKST SEIIKKLMGL GVMATKNEEL
DKTSIELIAH DFGVEVEEEE VIDELDIERY EEADDPEDLQ ERAPVVTIMG HVDHGKTTLL
DGIRKTKVTD TEAGGITQHI GAYQVEEDGK RVTFLDTPGH AAFTTMRARG AQATDITILV
VAADDGVMPQ TVEALNHAKA AEVPIIVAVN KTDKENANPD RVMQELTEYE LVPEAWGGDT
IFVNVSAVNG GGIDELLEMI LLVAEIEELK ANPSKRAQGT VVEAELDRGR GPVATLLVQG
GTLKVGDPIV VGYTYGRVRA MMSDVGLRVT EAGPSTPVEV TGLNGVPQAG DQFLVFADEK
KAKQIGEGRA IRAKEAQRKQ TSRVSLDDLY NQIQEGEIKE INLIIKADVQ GSVEAVRGSL
EKIDVAGVKV NVIHTGVGAV TESDVILASA SNAIIIGFNV RPGTNAKQTA ESENVDVRLY
RVIYNAIEEI EAAMKGLLDP EYEEKVIGHV EVRQTFKVSR IGTIAGSYVT DGKITRNANA
RVMRDGVVIY DGTIADLKRF KDDVREVSNN YECGITLAKF NDVQEGDTIE AYVMEEVPRT
//
