PTXBC_STAHJ
ID PTXBC_STAHJ Reviewed; 477 AA.
AC Q4L8H5;
DT 23-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-AUG-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
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=SH0741;
OS Staphylococcus haemolyticus (strain JCSC1435).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=279808;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCSC1435;
RX PubMed=16237012; DOI=10.1128/jb.187.21.7292-7308.2005;
RA Takeuchi F., Watanabe S., Baba T., Yuzawa H., Ito T., Morimoto Y.,
RA Kuroda M., Cui L., Takahashi M., Ankai A., Baba S., Fukui S., Lee J.C.,
RA Hiramatsu K.;
RT "Whole-genome sequencing of Staphylococcus haemolyticus uncovers the
RT extreme plasticity of its genome and the evolution of human-colonizing
RT staphylococcal species.";
RL J. Bacteriol. 187:7292-7308(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; AP006716; BAE04050.1; -; Genomic_DNA.
DR RefSeq; WP_011275065.1; NC_007168.1.
DR AlphaFoldDB; Q4L8H5; -.
DR SMR; Q4L8H5; -.
DR STRING; 279808.SH0741; -.
DR EnsemblBacteria; BAE04050; BAE04050; SH0741.
DR KEGG; sha:SH0741; -.
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; UP000000543; 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..477
FT /note="PTS system MurNAc-GlcNAc-specific EIIBC component"
FT /id="PRO_0000272183"
FT TRANSMEM 128..148
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 192..212
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 227..247
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 267..287
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 298..318
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 342..362
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 377..397
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 401..421
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 443..463
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 123..477
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT REGION 91..113
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 91..105
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 27
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
SQ SEQUENCE 477 AA; 50413 MW; C4239DC1037A9A6D CRC64;
MNKDQQLAHH ILDAVGGIDN VDNIIHCMTR VRLKINNETQ VDYPKLKNIE GVLGVIQDER
LQIVVGPGTV NEVSAEMVKL SGVQLGEDIP HRSNTSNIKN QAQQNKREFQ QKRKQSKMNT
ILKSIANIFI PLIPAFIGAG LIGGIAAVLN NFITAGTISA DWVKQLVAVL NVIKDGMLAY
LAIFTGFNAA KVFGATPGLG GVIGGTTLLT GITEDNPIKN VFTGEPLIAG QGGIIGVILA
VWLLSIIEKK LHKIVPNAID IIVTPTISLL IIGLLTIFFF MPIAGFISDG LVGVVNWVIG
VGGIFSGFII GAFFLPLVML GLHHIFTPIH IELINQSGAT YLLPIAAMAG AGQVGAALAL
WVRCKNNTTL RTAIKGALPV GFLGIGEPLI YGVTLPLGRP FITACLGGGI GGAVIGGIGH
IGATAIGPSG ISLLPLIAHQ KYLGYIIGLL SAYLAGFIFT YFFGTTKEMR NLNKLGD
