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Database: UniProt
Entry: A0A150LG06_9BACI
LinkDB: A0A150LG06_9BACI
Original site: A0A150LG06_9BACI 
ID   A0A150LG06_9BACI        Unreviewed;       695 AA.
AC   A0A150LG06;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KYD11258.1};
GN   ORFNames=B4102_2223 {ECO:0000313|EMBL:KYD11258.1};
OS   Heyndrickxia sporothermodurans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Heyndrickxia.
OX   NCBI_TaxID=46224 {ECO:0000313|EMBL:KYD11258.1, ECO:0000313|Proteomes:UP000075666};
RN   [1] {ECO:0000313|EMBL:KYD11258.1, ECO:0000313|Proteomes:UP000075666}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B4102 {ECO:0000313|EMBL:KYD11258.1,
RC   ECO:0000313|Proteomes:UP000075666};
RA   Berendsen E.M., Wells-Bennik M.H., Krawcyk A.O., De Jong A., Holsappel S.,
RA   Eijlander R.T., Kuipers O.P.;
RT   "Genome Sequences of Twelve Sporeforming Bacillus Species Isolated from
RT   Foods.";
RL   Submitted (JAN-2016) 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:KYD11258.1}.
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DR   EMBL; LQYN01000008; KYD11258.1; -; Genomic_DNA.
DR   RefSeq; WP_066226512.1; NZ_NAZD01000105.1.
DR   AlphaFoldDB; A0A150LG06; -.
DR   STRING; 46224.B4102_2223; -.
DR   PATRIC; fig|46224.3.peg.20; -.
DR   OrthoDB; 9776005at2; -.
DR   Proteomes; UP000075666; 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; 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; 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; IPR003501; PTS_EIIB_2/3.
DR   InterPro; IPR036388; WH-like_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; 1.
DR   Pfam; PF00359; PTS_EIIA_2; 1.
DR   Pfam; PF02302; PTS_IIB; 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   PROSITE; PS51372; PRD_2; 1.
DR   PROSITE; PS51094; PTS_EIIA_TYPE_2; 1.
DR   PROSITE; PS51099; PTS_EIIB_TYPE_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000075666};
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          299..405
FT                   /note="PRD"
FT                   /evidence="ECO:0000259|PROSITE:PS51372"
FT   DOMAIN          408..498
FT                   /note="PTS EIIB type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51099"
FT   DOMAIN          536..683
FT                   /note="PTS EIIA type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51094"
SQ   SEQUENCE   695 AA;  79625 MW;  80E4DB8952E6F131 CRC64;
     MFITSREKAI IELIIKTSGK HTAFSIATFL NVSVRTIQRD LKAIEKILEQ FQLQLVRNPN
     KGLSIEGKNE QVFRLVQHLA SSQPIDQPPQ EKKLQLLLSL FQTAESFKIQ VLAHELGVSI
     TTLSAYLDEL AEWLTNFQLV LSRKRGVGVE LTGEEVNKRK ALANYFLLYF NEELIESLFL
     LEQGQAENNQ ILHFFRSDYL LTIERLVNDI VNKRQTRLAD SDYIGLVIEI CITMQRAMNG
     FRIEEDENLV EDSDEYRQIE NICNCLEEGF PVQFNRGDIH YLSTVLKGSK LHEAGFVPYD
     SVILGQLIKN IIQSVSTQLH IDLTNDFSLF QGLLAHMLPS LFRMKQNMSL YNPLTEEIKK
     KYPVLFLAVK NSVEKEFKEF VTFPDEEIAY IVLHFGSALV LKEEQLPIKA LVICPTGIGT
     SKMLASRIKK EITEIDSVEI KSIKDVQKQK SLNQFDVILS TVRLPFMNNE YILVNPLLSK
     EDIKTIRSFL QKNIEQLTRN KLYTGLSTNE DSSSTRQQPL MDVLQELKDT HTSIEAIIQH
     FHVVQITNKT DYQQVMKNML ITAEKDNLIS NVESVFEALI DRERKGGLGI PGTGMGLFHC
     RNPHVDKLIF QIAHLEEPCV IKGMDGNDMY MKSLLLMLAP EELSPREQEM ISLLSTSLIE
     NNEAIMIFSS SDEKIIRSKM ETIFLDYLYT NVIKE
//
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