PTXBC_STAAS
ID PTXBC_STAAS Reviewed; 484 AA.
AC Q6GCT4;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 105.
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=SAS0167;
OS Staphylococcus aureus (strain MSSA476).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=282459;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MSSA476;
RX PubMed=15213324; DOI=10.1073/pnas.0402521101;
RA Holden M.T.G., Feil E.J., Lindsay J.A., Peacock S.J., Day N.P.J.,
RA Enright M.C., Foster T.J., Moore C.E., Hurst L., Atkin R., Barron A.,
RA Bason N., Bentley S.D., Chillingworth C., Chillingworth T., Churcher C.,
RA Clark L., Corton C., Cronin A., Doggett J., Dowd L., Feltwell T., Hance Z.,
RA Harris B., Hauser H., Holroyd S., Jagels K., James K.D., Lennard N.,
RA Line A., Mayes R., Moule S., Mungall K., Ormond D., Quail M.A.,
RA Rabbinowitsch E., Rutherford K.M., Sanders M., Sharp S., Simmonds M.,
RA Stevens K., Whitehead S., Barrell B.G., Spratt B.G., Parkhill J.;
RT "Complete genomes of two clinical Staphylococcus aureus strains: evidence
RT for the rapid evolution of virulence and drug resistance.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9786-9791(2004).
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; BX571857; CAG41935.1; -; Genomic_DNA.
DR RefSeq; WP_000159750.1; NC_002953.3.
DR AlphaFoldDB; Q6GCT4; -.
DR SMR; Q6GCT4; -.
DR KEGG; sas:SAS0167; -.
DR HOGENOM; CLU_012312_2_0_9; -.
DR OMA; VAHCMTR; -.
DR UniPathway; UPA00544; -.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; 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:0009254; P:peptidoglycan turnover; IEA:UniProtKB-UniPathway.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
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 Sugar transport; Transferase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..484
FT /note="PTS system MurNAc-GlcNAc-specific EIIBC component"
FT /id="PRO_0000272179"
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
