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Database: UniProt
Entry: A0A2C1Z7I1_9BACI
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ID   A0A2C1Z7I1_9BACI        Unreviewed;       642 AA.
AC   A0A2C1Z7I1;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   SubName: Full=Transcriptional antiterminator {ECO:0000313|EMBL:PGV53403.1};
GN   ORFNames=COD92_07375 {ECO:0000313|EMBL:PGV53403.1};
OS   Bacillus sp. AFS037270.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=2033499 {ECO:0000313|EMBL:PGV53403.1, ECO:0000313|Proteomes:UP000225442};
RN   [1] {ECO:0000313|EMBL:PGV53403.1, ECO:0000313|Proteomes:UP000225442}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AFS037270 {ECO:0000313|EMBL:PGV53403.1,
RC   ECO:0000313|Proteomes:UP000225442};
RG   Agbiome Team Llc;
RA   Bleich R.M., Grubbs K.J., Santa Maria K.C., Allen S.E., Farag S.,
RA   Shank E.A., Bowers A.;
RT   "Large-scale bioinformatics analysis of Bacillus genomes uncovers conserved
RT   roles of natural products in bacterial physiology.";
RL   Submitted (SEP-2017) 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:PGV53403.1}.
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DR   EMBL; NUNF01000014; PGV53403.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2C1Z7I1; -.
DR   Proteomes; UP000225442; 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; 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; 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:SF12; TRANSCRIPTIONAL REGULATOR MANR; 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; PS00372; PTS_EIIA_TYPE_2_HIS; 1.
DR   PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
PE   4: Predicted;
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          180..285
FT                   /note="PRD"
FT                   /evidence="ECO:0000259|PROSITE:PS51372"
FT   DOMAIN          290..397
FT                   /note="PRD"
FT                   /evidence="ECO:0000259|PROSITE:PS51372"
FT   DOMAIN          402..492
FT                   /note="PTS EIIB type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51099"
FT   DOMAIN          502..641
FT                   /note="PTS EIIA type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51094"
SQ   SEQUENCE   642 AA;  73744 MW;  F34F05A07DEC29FA CRC64;
     MNNRQKELLR ILLVHKDEVW HIKDLSERLD CAEKTVRNDL DRLEEFLLDY PSARLIRKPG
     FGISIESDEG VRSTILRSLL STEPKTNEER LFEIAFQLLS SSHAITLQYF ADRYYVPKAA
     IKKDIEMITQ WLKRYGLELV SKPRVGNMIE GLELHKRNAL AHLSELISPF AQDKNVVLDL
     FLPYEISIVR KALEDMQERF SIAITDGSLD SLLVHALIMV KRTRQRSPVF VQDSEKKIAG
     ERLEYQYTGW FFDILESAFG ITFPEEERVY FTWHLISSKR TEEGMDQLLK VDEALTNLVI
     ALIRKMGKLT LVPYEADPIL LNGLTVHMHS VINRIKFGFP ITNPLLSNIK KMYPYMFHMV
     MITLEDMKKI FQIEIPEDEA AYIVLHFQAS VERIEKKRDI KKKALIVCHM GIGMSHLLEA
     KIEQQYQDID ILACIGKNEV NNYVKDDQVD FIISTVPLEK INTAHIVLSP LFGHEDKKKL
     SQFVEGLKEK KDKLLEPNIF ATFLEEELIF FDVEKEHRYL VVEMLAAALF QKGYVSNEYI
     HSAVNRERNS ATAIGGGIAI PHGNPSWVYK SAIASAILKE RLEWGNERVS LVFMLAIAKE
     NQSEIRGIIG KIASLSETPL VVHALTAARD YQEILTIIGN NE
//
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