ID   Y801_STRP6              Reviewed;         163 AA.
AC   Q5XCC7; P82567;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Probable phosphotransferase enzyme IIB component M6_Spy0801;
DE            EC=2.7.1.-;
DE   AltName: Full=PTS system EIIB component;
GN   OrderedLocusNames=M6_Spy0801;
OS   Streptococcus pyogenes serotype M6 (strain ATCC BAA-946 / MGAS10394).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Streptococcus.
OX   NCBI_TaxID=286636;
RN   [1] {ECO:0000312|EMBL:AAT86936.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-946 / MGAS10394;
RX   PubMed=15272401; DOI=10.1086/422697;
RA   Banks D.J., Porcella S.F., Barbian K.D., Beres S.B., Philips L.E.,
RA   Voyich J.M., DeLeo F.R., Martin J.M., Somerville G.A., Musser J.M.;
RT   "Progress toward characterization of the group A Streptococcus metagenome:
RT   complete genome sequence of a macrolide-resistant serotype M6 strain.";
RL   J. Infect. Dis. 190:727-738(2004).
RN   [2] {ECO:0000305}
RP   PROTEIN SEQUENCE OF 23-47; 94-108 AND 120-135, AND MASS SPECTROMETRY.
RC   STRAIN=JRS4 / Serotype M6 {ECO:0000269|Ref.2};
RA   Hogan D.A., Du P., Stevenson T.I., Whitton M., Kilby G.W., Rogers J.,
RA   VanBogelen R.A.;
RT   "Two-dimensional gel electrophoresis map of Streptococcus pyogenes
RT   proteins.";
RL   Submitted (MAY-2000) to UniProtKB.
CC   -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC       system (sugar PTS), a major carbohydrate active -transport system,
CC       catalyzes the phosphorylation of incoming sugar substrates
CC       concomitantly with their translocation across the cell membrane.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:P37081}.
CC   -!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a
CC       cysteinyl or histidyl residue, depending on the transported sugar.
CC       Then, it transfers the phosphoryl group to the sugar substrate
CC       concomitantly with the sugar uptake processed by the EIIC domain.
CC       {ECO:0000305}.
CC   -!- MASS SPECTROMETRY: Mass=17933.93; Method=Electrospray;
CC       Evidence={ECO:0000269|Ref.2};
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DR   EMBL; CP000003; AAT86936.1; -; Genomic_DNA.
DR   RefSeq; WP_011184474.1; NC_006086.1.
DR   AlphaFoldDB; Q5XCC7; -.
DR   SMR; Q5XCC7; -.
DR   EnsemblBacteria; AAT86936; AAT86936; M6_Spy0801.
DR   KEGG; spa:M6_Spy0801; -.
DR   HOGENOM; CLU_116175_2_0_9; -.
DR   OMA; VAYGWAT; -.
DR   Proteomes; UP000001167; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
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:UniProtKB-KW.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.35.10; -; 1.
DR   InterPro; IPR004720; PTS_IIB_sorbose-sp.
DR   InterPro; IPR036667; PTS_IIB_sorbose-sp_sf.
DR   Pfam; PF03830; PTSIIB_sorb; 1.
DR   SUPFAM; SSF52728; SSF52728; 1.
DR   PROSITE; PS51101; PTS_EIIB_TYPE_4; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Direct protein sequencing; Kinase; Phosphotransferase system;
KW   Sugar transport; Transferase; Transport.
FT   CHAIN           1..163
FT                   /note="Probable phosphotransferase enzyme IIB component
FT                   M6_Spy0801"
FT                   /id="PRO_0000259702"
FT   DOMAIN          1..163
FT                   /note="PTS EIIB type-4"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00424"
FT   ACT_SITE        13
FT                   /note="Pros-phosphohistidine intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   163 AA;  17893 MW;  787F386ABDD7DD6A CRC64;
     MITQIRVDDR LVHGQVAVVW TKELNAPLLV VANDEAAKNE ITQMTLKMAV PNGMKLLIRS
     VEDSIKLFND PRATDKRIFV IVNSVKDACA IAKEVPDLEA VNVANVGRFD KSDPASKVKV
     TPSLLLNPEE MAAAKELVSL PELDVFNQVL PSNTKVHLSQ LVN