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Database: UniProt
Entry: F5X6U0_STRPX
LinkDB: F5X6U0_STRPX
Original site: F5X6U0_STRPX 
ID   F5X6U0_STRPX            Unreviewed;       662 AA.
AC   F5X6U0;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 66.
DE   SubName: Full=Lichenan operon transcriptional antiterminator {ECO:0000313|EMBL:BAK30130.1};
GN   Name=celR {ECO:0000313|EMBL:BAK30130.1};
GN   OrderedLocusNames=SGPB_1065 {ECO:0000313|EMBL:BAK30130.1};
OS   Streptococcus pasteurianus (strain ATCC 43144 / JCM 5346 / CDC 1723-81).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=981540 {ECO:0000313|EMBL:BAK30130.1, ECO:0000313|Proteomes:UP000007946};
RN   [1] {ECO:0000313|EMBL:BAK30130.1, ECO:0000313|Proteomes:UP000007946}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43144 / JCM 5346 / CDC 1723-81
RC   {ECO:0000313|Proteomes:UP000007946};
RX   PubMed=21633709; DOI=10.1371/journal.pone.0020519;
RA   Lin I.-H., Liu T.-T., Teng Y.-T., Wu H.-L., Liu Y.-M., Wu K.-M.,
RA   Chang C.-H., Hsu M.-T.;
RT   "Sequencing and comparative genome analysis of two pathogenic Streptococcus
RT   gallolyticus subspecies: genome plasticity, adaptation and virulence.";
RL   PLoS ONE 6:E20519-E20519(2011).
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DR   EMBL; AP012054; BAK30130.1; -; Genomic_DNA.
DR   RefSeq; WP_013851889.1; NC_015600.1.
DR   AlphaFoldDB; F5X6U0; -.
DR   STRING; 981540.SGPB_1065; -.
DR   KEGG; stb:SGPB_1065; -.
DR   HOGENOM; CLU_013442_5_0_9; -.
DR   Proteomes; UP000007946; Chromosome.
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; 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; 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; 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; PS51099; PTS_EIIB_TYPE_2; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000007946};
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..295
FT                   /note="PRD"
FT                   /evidence="ECO:0000259|PROSITE:PS51372"
FT   DOMAIN          296..403
FT                   /note="PRD"
FT                   /evidence="ECO:0000259|PROSITE:PS51372"
FT   DOMAIN          406..498
FT                   /note="PTS EIIB type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51099"
FT   DOMAIN          516..659
FT                   /note="PTS EIIA type-2"
FT                   /evidence="ECO:0000259|PROSITE:PS51094"
SQ   SEQUENCE   662 AA;  76934 MW;  6F054B927E4391E9 CRC64;
     MLNKKEKQII QFLMKDKDTF VTSKELATHL KCSDRTIRTY YKTLVEKLDD YSGIDLISKQ
     GYGYKLGISD DDAYADFLEE NHINDNHFDY HSITDINDRY NYLLNKLLFE QNEIYFDDLV
     DELYVSRSTL SSDFKKIRQK FKPYHLKIES KANKGVYVTG LERDKRRFIM DYFISSGFMD
     MMHSYVDNEL LNQRISFEEL TIIVLDECRE GGLKLSDFVI QNLVIHIALA IRRITEGFKI
     SSLEEDELNL RELPERQIAD SILKRVSVST KIDFPVEEVD YITLHLISKS HGNARCISEK
     MQESMRQELI DGIGKIDPEV KNDFQLIEGL LAHLSTMLIR LEGKVVLENP LTVEIQKNYP
     DMFQLAEQLV TIMPTFQSFS LTPNEIAYIA LHFMAAKERY KEQRKYNVLV ICATGYGSAQ
     MLKSRIENEL GNLILIADVI GYYEINDEKL KGIDFIISSI DLSNLIFNIP VFTVSVFLTD
     EELQDIKHGI SHLETSTSLR KMEDKTSEFS VREVFDGYFS EDSFFILSNI SKNELLKKLV
     KSISKNENEQ FEKRLLDMIK RREEMSSIIF GDRIAVPHPV KAVGCKHHFA VALIKDDLFW
     DEEYPSVKIV FLMSMSIHEN DGLPELTSAI VDLVDEPELQ KQMLACQSFE EFRTLFFKIK
     ER
//
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