ID   PTXBC_STAA8             Reviewed;         484 AA.
AC   Q2G1G5;
DT   23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   03-AUG-2022, entry version 98.
DE   RecName: Full=PTS system MurNAc-GlcNAc-specific EIIBC component {ECO:0000250|UniProtKB:Q2FK70};
DE   Includes:
DE     RecName: Full=MurNAc-GlcNAc-specific phosphotransferase enzyme IIB component;
DE              EC=2.7.1.- {ECO:0000250|UniProtKB:Q2FK70};
DE     AltName: Full=PTS system MurNAc-GlcNAc-specific EIIB component;
DE   Includes:
DE     RecName: Full=MurNAc-GlcNAc permease IIC component;
DE     AltName: Full=PTS system MurNAc-GlcNAc-specific EIIC component;
GN   OrderedLocusNames=SAOUHSC_00158;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
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. This
CC       system is involved in the uptake and phosphorylation of MurNAc-GlcNAc,
CC       the principle peptidoglycan turnover product of S.aureus, yielding
CC       cytoplasmic MurNAc 6P-GlcNAc. {ECO:0000250|UniProtKB:Q2FK70}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=N(pros)-phospho-L-histidyl-[protein] + N-acetyl-beta-D-
CC         muramate-(1->4)-N-acetyl-D-glucosamine(out) = 6-phospho-N-acetyl-
CC         beta-D-muramate-(1->4)-N-acetyl-D-glucosamine(in) + L-histidyl-
CC         [protein]; Xref=Rhea:RHEA:66784, Rhea:RHEA-COMP:9745, Rhea:RHEA-
CC         COMP:9746, ChEBI:CHEBI:29979, ChEBI:CHEBI:64837, ChEBI:CHEBI:167476,
CC         ChEBI:CHEBI:167477; Evidence={ECO:0000250|UniProtKB:Q2FK70};
CC       PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:66785;
CC         Evidence={ECO:0000250|UniProtKB:Q2FK70};
CC   -!- PATHWAY: Cell wall biogenesis; peptidoglycan recycling.
CC       {ECO:0000250|UniProtKB:Q2FK70}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00426}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC       ProRule:PRU00426}.
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   -!- DOMAIN: The EIIC domain forms the PTS system translocation channel and
CC       contains the specific substrate-binding site.
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DR   EMBL; CP000253; ABD29338.1; -; Genomic_DNA.
DR   RefSeq; WP_000159750.1; NZ_LS483365.1.
DR   RefSeq; YP_498757.1; NC_007795.1.
DR   AlphaFoldDB; Q2G1G5; -.
DR   SMR; Q2G1G5; -.
DR   STRING; 1280.SAXN108_0178; -.
DR   EnsemblBacteria; ABD29338; ABD29338; SAOUHSC_00158.
DR   GeneID; 3919866; -.
DR   KEGG; sao:SAOUHSC_00158; -.
DR   PATRIC; fig|93061.5.peg.148; -.
DR   eggNOG; COG1263; Bacteria.
DR   eggNOG; COG1264; Bacteria.
DR   HOGENOM; CLU_012312_2_0_9; -.
DR   OMA; VAHCMTR; -.
DR   UniPathway; UPA00544; -.
DR   PRO; PR:Q2G1G5; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
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:0090588; F:protein-phosphocysteine-N-acetylmuramate phosphotransferase system transporter activity; IBA:GO_Central.
DR   GO; GO:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IBA:GO_Central.
DR   GO; GO:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IBA:GO_Central.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   CDD; cd00212; PTS_IIB_glc; 1.
DR   Gene3D; 3.30.1360.60; -; 1.
DR   InterPro; IPR036878; Glu_permease_IIB.
DR   InterPro; IPR018113; PTrfase_EIIB_Cys.
DR   InterPro; IPR003352; PTS_EIIC.
DR   InterPro; IPR013013; PTS_EIIC_1.
DR   InterPro; IPR001996; PTS_IIB_1.
DR   Pfam; PF00367; PTS_EIIB; 1.
DR   Pfam; PF02378; PTS_EIIC; 1.
DR   SUPFAM; SSF55604; SSF55604; 1.
DR   PROSITE; PS51098; PTS_EIIB_TYPE_1; 1.
DR   PROSITE; PS01035; PTS_EIIB_TYPE_1_CYS; 1.
DR   PROSITE; PS51103; PTS_EIIC_TYPE_1; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Kinase; Membrane; Phosphotransferase system;
KW   Reference proteome; Sugar transport; Transferase; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..484
FT                   /note="PTS system MurNAc-GlcNAc-specific EIIBC component"
FT                   /id="PRO_0000272173"
FT   TRANSMEM        135..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        160..180
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        200..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        234..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        274..294
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        305..325
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        349..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        384..404
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        408..428
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   TRANSMEM        450..470
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   DOMAIN          5..87
FT                   /note="PTS EIIB type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT   DOMAIN          130..484
FT                   /note="PTS EIIC type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT   ACT_SITE        27
FT                   /note="Phosphocysteine intermediate; for EIIB activity"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
SQ   SEQUENCE   484 AA;  50665 MW;  3DB68A1088038706 CRC64;
     MTKEQQLAER IIAAVGGMDN IDSVMNCMTR VRIKVLDENK VDDQELRHID GVMGVIHDER
     IQVVVGPGTV NKVANHMAEL SGVKLGDPIP HHHNDSEKMD YKSYAADKAK ANKEAHKAKQ
     KNGKLNKVLK SIANIFIPLI PAFIGAGLIG GIAAVLSNLM VAGYISGAWI TQLITVFNVI
     KDGMLAYLAI FTGINAAKEF GATPGLGGVI GGTTLLTGIA GKNILMNVFT GEPLQPGQGG
     IIGVIFAVWI LSIVEKRLHK IVPNAIDIIV TPTIALLIVG LLTIFIFMPL AGFVSDSLVS
     VVNGIISIGG VFSGFIIGAS FLPLVMLGLH HIFTPIHIEM INQSGATYLL PIAAMAGAGQ
     VGAALALWVR CKRNTTLRNT LKGALPVGFL GIGEPLIYGV TLPLGRPFLT ACIGGGIGGA
     VIGGIGHIGA KAIGPSGVSL LPLISDNMYL GYIAGLLAAY AGGFVCTYLF GTTKAMRQTD
     LLGD