ID A0A291GQV3_9MICO Unreviewed; 946 AA.
AC A0A291GQV3;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 27.
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=CFK38_14330 {ECO:0000313|EMBL:ATG52567.1};
OS Brachybacterium vulturis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Dermabacteraceae;
OC Brachybacterium.
OX NCBI_TaxID=2017484 {ECO:0000313|EMBL:ATG52567.1, ECO:0000313|Proteomes:UP000218165};
RN [1] {ECO:0000313|Proteomes:UP000218165}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VM2412 {ECO:0000313|Proteomes:UP000218165};
RA Tak E.J., Bae J.-W.;
RT "Brachybacterium sp. VM2412.";
RL Submitted (SEP-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 -!- 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; CP023563; ATG52567.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A291GQV3; -.
DR KEGG; brz:CFK38_14330; -.
DR OrthoDB; 9811804at2; -.
DR Proteomes; UP000218165; 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; PR00315; ELONGATNFCT.
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.
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:UP000218165}.
FT DOMAIN 439..613
FT /note="Tr-type G"
FT /evidence="ECO:0000259|PROSITE:PS51722"
FT REGION 33..347
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 121..161
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 448..455
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 498..502
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
FT BINDING 552..555
FT /ligand="GTP"
FT /ligand_id="ChEBI:CHEBI:37565"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00100"
SQ SEQUENCE 946 AA; 99150 MW; 05BFFE20A466EBAC CRC64;
MAKVRVHELA KELGHPSKAV LQKLQDMGEF VRSASSTIEA PVARRLREEL PAKSGADAPA
AKSGTGAPSK TPGAPQPGGA SAPKPGMKPA AKQPAESAPQ EPAAPAPTAE KAEKSAPAPT
PGAERPAPAP KPGAEKPAPA PKPGAEKPVP APKPGGERPS PRPGSARPGN NPFASSQGMP
RPGSRKPGQG GGRPPRGEGA PRPGNNPFAS AQGMPRPGQR PRPAAGDQAS GRPPREGAPR
PAGGRPGMPT PGIMRQHSSG GLTEANQGGG GRGRGGRPGP GGPGGPSRPG GGGGGPRGRG
GRGSTQGAFG RGGKPARSRK SKRAKRQEFE QQQAPAPGGV SIPRGNGQTV RLRRGASLSD
FADRIDVNPA SLITVMFAMG EMATATQSLD EVTFGLLGEE LGYKIEIVSP EDEERELLEQ
FDIDLDAELA EEDDADRLPR PPVVTVMGHV DHGKTRLLDT IRKAKVGAGE AGGITQHIGA
YQVEVEHEEQ DRALTFIDTP GHEAFTAMRA RGADVTDIAI LVVAADDGVM PQTIEALNHA
QAAHVPIVVA VNKVDKPDAN PEKIRQQLTE YNLIAEEYGG DTMFVDVSAR ENLNIEALLE
AVLLTADAAL ELTANPDKDA RGVSIEANLD KGRGPVATVL VQQGTLRVGD AIVCGSGHGR
VRAMLDENGD TVTEAGPSRP VQVLGLTSVP GAGDSFLVAQ DERTARQIAE KREAAKRAAS
LSKVRKRISL EDINQHMADG KVETLNLILK GDAAGAVEAL EESLLGIEVG EGVDLRIIDR
GVGAITMNNI NLAVASNAVI IGYNVRAEGL NADYADREGV EIKYYSVIYN AIDEVESALK
GMLKPEYEEV ELGSAEIREI FRSSKFGNIA GSIVRSGIIK RGAKARITRN GVVVAENIEV
AGLRRFKDDV TEVRDGYECG INLGSYNDLQ LEDHITTYEM QEKPRI
//
