PTXBC_STAS1
ID PTXBC_STAS1 Reviewed; 479 AA.
AC Q49ZN7;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 109.
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=SSP0594;
OS Staphylococcus saprophyticus subsp. saprophyticus (strain ATCC 15305 / DSM
OS 20229 / NCIMB 8711 / NCTC 7292 / S-41).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=342451;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15305 / DSM 20229 / NCIMB 8711 / NCTC 7292 / S-41;
RX PubMed=16135568; DOI=10.1073/pnas.0502950102;
RA Kuroda M., Yamashita A., Hirakawa H., Kumano M., Morikawa K., Higashide M.,
RA Maruyama A., Inose Y., Matoba K., Toh H., Kuhara S., Hattori M., Ohta T.;
RT "Whole genome sequence of Staphylococcus saprophyticus reveals the
RT pathogenesis of uncomplicated urinary tract infection.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:13272-13277(2005).
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; AP008934; BAE17739.1; -; Genomic_DNA.
DR RefSeq; WP_011302539.1; NZ_MTGA01000036.1.
DR AlphaFoldDB; Q49ZN7; -.
DR SMR; Q49ZN7; -.
DR STRING; 342451.SSP0594; -.
DR EnsemblBacteria; BAE17739; BAE17739; SSP0594.
DR KEGG; ssp:SSP0594; -.
DR PATRIC; fig|342451.11.peg.599; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR HOGENOM; CLU_012312_2_0_9; -.
DR OMA; VAHCMTR; -.
DR OrthoDB; 328780at2; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000006371; Chromosome.
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 Reference proteome; Sugar transport; Transferase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..479
FT /note="PTS system MurNAc-GlcNAc-specific EIIBC component"
FT /id="PRO_0000272184"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 169..189
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 195..215
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 229..249
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 269..289
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 303..323
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 379..399
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 445..465
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 125..479
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 479 AA; 50455 MW; 5C7E33963CFB0166 CRC64;
MTKEQILAEH IIDAVGGIDN MDNIINCMTR VRIKVLDEDK IDYEQLKSIK GVMGVVKDDR
VQVVVGPGTV NKVASHMSEL SGAPLGETIK HKSKDYRANA EAQAQANKSE FQSKQKRGKF
NKLLKTIANI FIPLIPAFIG AGLIGGIAAV LSNLLAAGQI SGEWVTQLVT VFNVIKDGML
AYLAIFTGIN AAKEFGATPG LGGVIGGTTL LTGLTDKNMI TNIFTGEPLQ PGQGGIIGVI
FAVWLLSIIE KRLHKIVPNS IDIIVTPTIT LFIIGLLTIF IFMPLAGFVS DGLVTVINGI
IDIGGVFSGF IIGAFFLPLV MLGLHHMFTP IHIEMINQTG ATYLLPIAAM AGAGQVGAAL
ALWVRCRKNT TLRDTLKGAL PVGFLGIGEP LIYGVTLPLG KPFITACIGG GIGGAVIGGI
GHIGATAIGP SGISLLPLIS DHMYLGYIAG LLVAYAGGFI FTYFFGTTKA MRESDTLGD
