ID A0A3S8Z5X2_9ACTO Unreviewed; 949 AA.
AC A0A3S8Z5X2;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 27-MAR-2024, entry version 19.
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=EJO69_00255 {ECO:0000313|EMBL:AZN28902.1};
OS Flaviflexus salsibiostraticola.
OC Bacteria; Actinomycetota; Actinomycetes; Actinomycetales; Actinomycetaceae;
OC Flaviflexus.
OX NCBI_TaxID=1282737 {ECO:0000313|EMBL:AZN28902.1, ECO:0000313|Proteomes:UP000270021};
RN [1] {ECO:0000313|EMBL:AZN28902.1, ECO:0000313|Proteomes:UP000270021}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 33148 {ECO:0000313|EMBL:AZN28902.1,
RC ECO:0000313|Proteomes:UP000270021};
RA Bae J.-W.;
RT "Complete genome sequence of Flaviflexus salsibiostraticola KCTC 33148.";
RL Submitted (DEC-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|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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_00100}.
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DR EMBL; CP034438; AZN28902.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3S8Z5X2; -.
DR KEGG; fsl:EJO69_00255; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000270021; 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: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 PRINTS; PR01217; PRICHEXTENSN.
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:UP000270021}.
FT DOMAIN 443..617
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 33..336
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..125
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 141..168
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 452..459
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 502..506
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 556..559
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 949 AA; 98900 MW; D5462C64257B35FB CRC64;
MAKVRVHQLA KEFGIQSKEV LAYLSEAGEF VKSASSTLEP PVERRAREHF AALTKSTAKT
TQQADAPARP APKPGPKADK PASAKPASPQ APKPGPKPTP KPEAPAAEAP KPAAPEAPVA
PKPAAPETPA AEAKPEAPAQ EAPKPEAPKP TPASSAKPGP PAPKPGPKPG GARGQGQRTG
GKGGPRPGNN PFAPNQGMPR PGGGKGGPRP GNNPFAPNQG MPRPGGGKKT EGQGAARPRP
GGAKGGPRPS PAMMPNQSAL AQPKAGGRGG RGGARPGQTR GPGTGAPGAA AGGGAPGRGG
RPMRGGTAGA FGRGGGRAGR GRKSKRAKRQ EYEQQHAPMV GGVRVPRGDG STVIRVRAGA
SLADFAEKIN VDPAALVTVM FSMGEMVTAN QSLDEDTFQL LGAELGYDIQ IRSVEDEDRE
ILEAFNIDLE AEEAAEGEDD LVARPPVVTV MGHVDHGKTK LLDAIRSDDV AGAEAGGITQ
RIGAYQVTVE HDGQDRAITF IDTPGHEAFT QMRARGAEVT DIAILVVAAN DGVMPQTIEA
LNHAQAAGVP IVVAVNKIDV EGASPDKVRG QLTEYGLVAE EYGGDTMFVD VSAKQRINID
ELLEAVLLTA DAALELTANP NKAARGVAIE AKLDPGRGSV ITALIESGTL RVGDAIVAGS
AHGTVRALFD DHGLPVDEAG PSFPVQVLGL QSVPSAGDSL LVAEDSRQAR QIADKREAAR
RAATLAKRRK RMSLEDFNEA LRAGQVETLN LIIKGDSSGT VEALESSLLE LEVSEEVALN
IIHRGVGAIT QNDVNLATVD SAVIIGFNVR PAERVADYAD AEGVEMKFYS VIYDAIDDVE
AALKGMLKPI YEEVELGRAE IRQIFRSGKF GNIAGSMVLS GVIKRGTNAR LVRNGVVVTP
NLEIVSLRRE KDDVTEVREG FECGITLGHK DIAEGDIIET FEMREKPRD
//