PTXBC_STAES
ID PTXBC_STAES Reviewed; 474 AA.
AC Q8CNB2;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=SE_1890;
OS Staphylococcus epidermidis (strain ATCC 12228 / FDA PCI 1200).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=176280;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 12228 / FDA PCI 1200;
RX PubMed=12950922; DOI=10.1046/j.1365-2958.2003.03671.x;
RA Zhang Y.-Q., Ren S.-X., Li H.-L., Wang Y.-X., Fu G., Yang J., Qin Z.-Q.,
RA Miao Y.-G., Wang W.-Y., Chen R.-S., Shen Y., Chen Z., Yuan Z.-H.,
RA Zhao G.-P., Qu D., Danchin A., Wen Y.-M.;
RT "Genome-based analysis of virulence genes in a non-biofilm-forming
RT Staphylococcus epidermidis strain (ATCC 12228).";
RL Mol. Microbiol. 49:1577-1593(2003).
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; AE015929; AAO05531.1; -; Genomic_DNA.
DR RefSeq; NP_765445.1; NC_004461.1.
DR RefSeq; WP_001830059.1; NZ_WBME01000032.1.
DR AlphaFoldDB; Q8CNB2; -.
DR SMR; Q8CNB2; -.
DR STRING; 176280.SE_1890; -.
DR EnsemblBacteria; AAO05531; AAO05531; SE_1890.
DR GeneID; 50018008; -.
DR KEGG; sep:SE_1890; -.
DR PATRIC; fig|176280.10.peg.1847; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR HOGENOM; CLU_012312_2_0_9; -.
DR OMA; VAHCMTR; -.
DR UniPathway; UPA00544; -.
DR Proteomes; UP000001411; 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 Sugar transport; Transferase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..474
FT /note="PTS system MurNAc-GlcNAc-specific EIIBC component"
FT /id="PRO_0000272182"
FT TRANSMEM 129..149
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 167..187
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 193..213
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 268..288
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 343..363
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 444..464
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 124..474
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 474 AA; 50266 MW; 117F3B63BE50E376 CRC64;
MSKEERLAKD ITHALGGSQN ISNIIHCMTR VRIKVHNDAK VNYDELKSIN GVLGVVEDER
IQVVVGPGIV NKVAKLMADQ SGATLAEETT ENQSYKSQAE KRAYEHKKQF QSQRKQSKWN
KVLKSIANIF IPLIPAFIGA GLIGGIAAIL SNLLTAGSIS GQWIQQIVTV LNVIKDGMLF
YLAIFTGINS AKVFGATPGL GGVIGGTTLL TGITDENPIK NIFTGEHLAA GQGGIIGVIF
AVWLLSMVEK RLHKIIPNSI DIIVTPTITL LLIGLLTIFI IMPLAGFVSD GLVYVINWII
GVGGIFSGFI IGAFFLPLVM LGLHHIFTPI HIELINQTGS TYLLPIAAMA GAGQVGAAIA
LWVRCGKNKE LRNTLKGALP VGFLGIGEPL IYGVTLPLGR PFFTACIGGG VGGAVIGGIG
HIGATAVGPS GISLLPLIAN NMYLGYIVGL LAAYAGGFIF TYFFGTTKEM RNPE
