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Database: UniProt
Entry: A0A6I1F5P9_9BACI
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ID   A0A6I1F5P9_9BACI        Unreviewed;       643 AA.
AC   A0A6I1F5P9;
DT   12-AUG-2020, integrated into UniProtKB/TrEMBL.
DT   12-AUG-2020, sequence version 1.
DT   05-FEB-2025, entry version 15.
DE   SubName: Full=Transcription antiterminator {ECO:0000313|EMBL:KAB7670751.1};
GN   ORFNames=F9279_08000 {ECO:0000313|EMBL:KAB7670751.1};
OS   Bacillus sp. B1-b2.
OC   Bacteria; Bacillati; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2653201 {ECO:0000313|EMBL:KAB7670751.1, ECO:0000313|Proteomes:UP000437773};
RN   [1] {ECO:0000313|EMBL:KAB7670751.1, ECO:0000313|Proteomes:UP000437773}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B1-b2 {ECO:0000313|EMBL:KAB7670751.1,
RC   ECO:0000313|Proteomes:UP000437773};
RA   Park S.-J.;
RT   "Draft genome sequence of Bacillus sp. B1-b2.";
RL   Submitted (OCT-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KAB7670751.1}.
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DR   EMBL; WEHU01000006; KAB7670751.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A6I1F5P9; -.
DR   Proteomes; UP000437773; Unassembled WGS sequence.
DR   GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
DR   GO; GO:0006355; P:regulation of DNA-templated transcription; IEA:InterPro.
DR   CDD; cd00211; PTS_IIA_fru; 1.
DR   CDD; cd05568; PTS_IIB_bgl_like; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.40.930.10; Mannitol-specific EII, Chain A; 1.
DR   Gene3D; 1.10.1790.10; PRD domain; 2.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 2.
DR   InterPro; IPR050661; BglG_antiterminators.
DR   InterPro; IPR013196; HTH_11.
DR   InterPro; IPR007737; Mga_HTH.
DR   InterPro; IPR011608; PRD.
DR   InterPro; IPR036634; PRD_sf.
DR   InterPro; IPR016152; PTrfase/Anion_transptr.
DR   InterPro; IPR002178; PTS_EIIA_type-2_dom.
DR   InterPro; IPR036095; PTS_EIIB-like_sf.
DR   InterPro; IPR013011; PTS_EIIB_2.
DR   InterPro; IPR036388; WH-like_DNA-bd_sf.
DR   InterPro; IPR036390; WH_DNA-bd_sf.
DR   PANTHER; PTHR30185; CRYPTIC BETA-GLUCOSIDE BGL OPERON ANTITERMINATOR; 1.
DR   PANTHER; PTHR30185:SF13; LICABCH OPERON REGULATOR-RELATED; 1.
DR   Pfam; PF08279; HTH_11; 1.
DR   Pfam; PF05043; Mga; 1.
DR   Pfam; PF00874; PRD; 2.
DR   Pfam; PF00359; PTS_EIIA_2; 1.
DR   SUPFAM; SSF55804; Phoshotransferase/anion transport protein; 1.
DR   SUPFAM; SSF52794; PTS system IIB component-like; 1.
DR   SUPFAM; SSF63520; PTS-regulatory domain, PRD; 2.
DR   SUPFAM; SSF46785; Winged helix' DNA-binding domain; 1.
DR   PROSITE; PS51372; PRD_2; 2.
DR   PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
DR   PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
PE   4: Predicted;
KW   Activator {ECO:0000256|ARBA:ARBA00023159};
KW   Reference proteome {ECO:0000313|Proteomes:UP000437773};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          189..294
FT                   /note="PRD"
FT                   /evidence="ECO:0000259|PROSITE:PS51372"
FT   DOMAIN          300..407
FT                   /note="PRD"
FT                   /evidence="ECO:0000259|PROSITE:PS51372"
FT   DOMAIN          411..502
FT                   /note="PTS EIIB type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51099"
FT   DOMAIN          505..643
FT                   /note="PTS EIIA type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51094"
SQ   SEQUENCE   643 AA;  73970 MW;  8EA62B6F18FBA549 CRC64;
     MLSSRMKEIL RELMTADTPI TGSYLATENE VTSRTIREDI KNLDYILNSN GARIIAVISK
     GYKLEIRDKQ LFQAFLQSIS VENSFYNKAI PKTPEDRVTY LITRFLLSDH YIKLDDLAEE
     LYISKSTIQL DIKSVKEILQ KYDITLEAKP NYGLKVLGEE IKVRFCLSEY VLNRNQQTSS
     ALDVPLPSFF SDTNKEKIQT IILRQIEKHD ITLSDIAINN LLIHIIIAHK RIVSGHYAAL
     IHADLDEMQQ QKEYHVASQM VKEVEALYEV TFPQEEIAYI AMHLLGTKMV SQKRGEIDHV
     IEKDIFELVT FTLSKIEEQL DLGIEKDEEL IFGMSLHLKP AVNRIKYGMN IRNPMLREIK
     NNYPLAYEAG IIAGLAITEY TGIEMDENEV GYLALHIGAA MERKKLNSGS KRCLVVCASG
     LGTAQLIYYR LKSYFGSNLE VVETTEYYKL EQYNLNDIDL IVSSIPISEN FNVPVIQVNA
     ILKESDLKAI EKFIMHQSNN QTTPSFFLEE LAFFRKKFDS QEQVLQFLYE QLIEKELVDQ
     TFLEAVYARE KVASTSYGNL VAIPHPITPQ TEKTFLSICT LEKPISWNNN SVQLILLLCV
     KKNSQEDLQE MYEMLGQIIE DKARVQKMVR VSDYEEFMEL MKE
//
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