ID   A0A3M8ATE3_9BACL        Unreviewed;       688 AA.
AC   A0A3M8ATE3;
DT   13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT   13-FEB-2019, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=PRD domain-containing protein {ECO:0000313|EMBL:RNB54293.1};
GN   ORFNames=EDM57_17790 {ECO:0000313|EMBL:RNB54293.1};
OS   Brevibacillus gelatini.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Brevibacillus.
OX   NCBI_TaxID=1655277 {ECO:0000313|EMBL:RNB54293.1, ECO:0000313|Proteomes:UP000268829};
RN   [1] {ECO:0000313|EMBL:RNB54293.1, ECO:0000313|Proteomes:UP000268829}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 100115 {ECO:0000313|EMBL:RNB54293.1,
RC   ECO:0000313|Proteomes:UP000268829};
RA   Dunlap C.;
RT   "Phylogenomics of Brevibacillus.";
RL   Submitted (OCT-2018) 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:RNB54293.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; RHHS01000041; RNB54293.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3M8ATE3; -.
DR   OrthoDB; 9776005at2; -.
DR   Proteomes; UP000268829; 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; 1.
DR   Gene3D; 1.10.10.10; Winged helix-like DNA-binding domain superfamily/Winged helix DNA-binding domain; 1.
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:SF18; TRANSCRIPTIONAL REGULATOR MTLR; 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; 1.
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   Transcription {ECO:0000256|ARBA:ARBA00023163};
KW   Transcription regulation {ECO:0000256|ARBA:ARBA00023015};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          185..286
FT                   /note="PRD"
FT                   /evidence="ECO:0000259|PROSITE:PS51372"
FT   DOMAIN          291..398
FT                   /note="PRD"
FT                   /evidence="ECO:0000259|PROSITE:PS51372"
FT   DOMAIN          403..491
FT                   /note="PTS EIIB type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51099"
FT   DOMAIN          539..682
FT                   /note="PTS EIIA type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51094"
SQ   SEQUENCE   688 AA;  78550 MW;  38FA58E72CFA2811 CRC64;
     MLDKRAMQML QLFVQSHHTL SVKELMEQFS ISRRTLYYDI QKINDWLKQA GLQQIQHIYA
     KGFYLDAASR QAAGRIIGEN KPDVLVLRAA DRQVYLLLYV LLADERITTQ VCMDKTGVSR
     NTILHDLKSV KEDVEKHGLQ LAYSYADGYE ITGDELTIRN LLSHHVHSLV HEGQESLLKD
     LLGGEKVVPN PDAILQWLSD CEKQLEVQFA EDATKPLSYL FPCYIKRIGN GHTVAFPQRQ
     ISPIMETRHY EAVQALVRTL PLELPHDEAC YLTTLLLSAK VNEFGQAAKS NEIPALRQAI
     AEMVDLFEVR ACVVFDQRAQ LEHNLYLHLQ PAYYRFLYDI EVTNPIKEMI QRQYRDIYEL
     TKKSVQPLEK LIGKTISDDE IAYITVHFGG WMRWQGITAT SLRRVLLVCA NGVGTSRILT
     QQLEGLFSNI DLQGPITLRQ YEQFHEDVDL VVSTTKIANP RHRIILVNPI LTDRDKVQLL
     HQMETLSGNT PAHITAQTIL SIVKKYAVVE NEHQLTEEIQ QVLQQQKQLK RERKPMLDEL
     LQDEFIQLKD SVRDWREAIR IASEPLLNSG SITEAYVQAM IANVEEHGPY VVIAPKVALP
     HARPEQGVQR VGMSLLRLKQ PVSFSETEQR EAQLIIVLAA VDNETHLKAL SQLSMMLSEE
     DNIDKLIDAA DKETILGYIT AYSKNRGN
//