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Database: UniProt
Entry: A0A0B3VXF9_9FIRM
LinkDB: A0A0B3VXF9_9FIRM
Original site: A0A0B3VXF9_9FIRM 
ID   A0A0B3VXF9_9FIRM        Unreviewed;       644 AA.
AC   A0A0B3VXF9;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   27-MAR-2024, entry version 31.
DE   SubName: Full=Uncharacterized protein {ECO:0000313|EMBL:KHS57503.1};
GN   ORFNames=QX51_07875 {ECO:0000313|EMBL:KHS57503.1};
OS   Terrisporobacter othiniensis.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC   Terrisporobacter.
OX   NCBI_TaxID=1577792 {ECO:0000313|EMBL:KHS57503.1, ECO:0000313|Proteomes:UP000031189};
RN   [1] {ECO:0000313|EMBL:KHS57503.1, ECO:0000313|Proteomes:UP000031189}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=08-306576 {ECO:0000313|EMBL:KHS57503.1,
RC   ECO:0000313|Proteomes:UP000031189};
RA   Lund L.C., Sydenham T.V., Hogh S.V., Skov M.N., Kemp M., Justesen U.S.;
RT   "Draft genome sequence of Terrisporobacter sp. 08-306576, isolated from the
RT   blood culture of a bacteremia patient.";
RL   Submitted (DEC-2014) 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:KHS57503.1}.
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DR   EMBL; JWHR01000072; KHS57503.1; -; Genomic_DNA.
DR   RefSeq; WP_039679364.1; NZ_JWHR01000072.1.
DR   AlphaFoldDB; A0A0B3VXF9; -.
DR   STRING; 1577792.QX51_07875; -.
DR   OrthoDB; 3175596at2; -.
DR   Proteomes; UP000031189; 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: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   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; 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   Reference proteome {ECO:0000313|Proteomes:UP000031189};
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          190..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          413..503
FT                   /note="PTS EIIB type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51099"
FT   DOMAIN          508..644
FT                   /note="PTS EIIA type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51094"
SQ   SEQUENCE   644 AA;  74626 MW;  9C2EB3DCAB098ACF CRC64;
     MIKATGRQRG IINAIISADG YISGNDLAKI NQISAKTVQR EIKDINEFLQ PYNCEILSKR
     SYGYKIRYDN YDDYKILKSV VGEIDCNCVY TLEENRVEWL IRKLAFLYAD SETESIKQDE
     LCDELFISLS TLKNDLKVVK EILHNYDLKL SRKGNSGVYI SGNEAKFRYF LSDYIVHKTG
     QEKSGTILEM IDTKSSESIR SIIIDVINKY DLNITDLGFD NLFNHIVITI TRIKNDKIIN
     EEESRHIPVG DIEYEAAINL CRQICELTGI EFPTAEVVYI YQHLKSQNRL FKDDNYSIDE
     EDNNNLDTIR KSLKEIYLQI GIDFTHDEIL ENGLLIHLKS VLHRIQYKMK IRNNLLDQIK
     KNYVLAYELA NFLAKAIEED MNVEVDENEV GFLALHFGGA LERMNIKGRK DRLRVILICA
     SGMGTSILLR SKLSNRFGSR IQICGVYPSY KLEELDFKDI DLIISTINLQ YKNLPIINIS
     PILSDADMNK INHFISKGNE NYKLDIKSYF KDEIFSPNLE INNYLDVVEY MSSKMYELGY
     IDEVMKNSFV EREKLSSTEI GNMVAIPHAL VGDVKKPGIY VAILKEPIKW VYSEVQLVMM
     IAIDKDVFLE HENLFLDIYN PVDEMYKVEK IINKKDLNYI KKLY
//
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