PTYBC_SHIDS
ID PTYBC_SHIDS Reviewed; 474 AA.
AC Q32DC5;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=PTS system N-acetylmuramic acid-specific EIIBC component {ECO:0000250|UniProtKB:P77272};
DE AltName: Full=EIIBC-MurNAc {ECO:0000250|UniProtKB:P77272};
DE Includes:
DE RecName: Full=N-acetylmuramic acid-specific phosphotransferase enzyme IIB component {ECO:0000250|UniProtKB:P77272};
DE EC=2.7.1.192 {ECO:0000250|UniProtKB:P77272};
DE AltName: Full=PTS system N-acetylmuramic acid-specific EIIB component {ECO:0000250|UniProtKB:P77272};
DE Includes:
DE RecName: Full=N-acetylmuramic acid permease IIC component {ECO:0000250|UniProtKB:P77272};
DE AltName: Full=PTS system N-acetylmuramic acid-specific EIIC component {ECO:0000250|UniProtKB:P77272};
GN Name=murP; OrderedLocusNames=SDY_2625;
OS Shigella dysenteriae serotype 1 (strain Sd197).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=300267;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sd197;
RX PubMed=16275786; DOI=10.1093/nar/gki954;
RA Yang F., Yang J., Zhang X., Chen L., Jiang Y., Yan Y., Tang X., Wang J.,
RA Xiong Z., Dong J., Xue Y., Zhu Y., Xu X., Sun L., Chen S., Nie H., Peng J.,
RA Xu J., Wang Y., Yuan Z., Wen Y., Yao Z., Shen Y., Qiang B., Hou Y., Yu J.,
RA Jin Q.;
RT "Genome dynamics and diversity of Shigella species, the etiologic agents of
RT bacillary dysentery.";
RL Nucleic Acids Res. 33:6445-6458(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 N-acetylmuramic acid (MurNAc) transport, yielding
CC cytoplasmic MurNAc-6-P. Is also able to take up anhydro-N-acetylmuramic
CC acid (anhMurNAc), but cannot phosphorylate the carbon 6, probably
CC because of the 1,6-anhydro ring. {ECO:0000250|UniProtKB:P77272}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=N(pros)-phospho-L-histidyl-[protein] + N-acetyl-beta-D-
CC muramate(out) = L-histidyl-[protein] + N-acetyl-beta-D-muramate 6-
CC phosphate(in); Xref=Rhea:RHEA:33399, Rhea:RHEA-COMP:9745, Rhea:RHEA-
CC COMP:9746, ChEBI:CHEBI:29979, ChEBI:CHEBI:58721, ChEBI:CHEBI:64837,
CC ChEBI:CHEBI:64848; EC=2.7.1.192;
CC Evidence={ECO:0000250|UniProtKB:P77272};
CC -!- SUBCELLULAR LOCATION: Cell inner 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 {ECO:0000255|PROSITE-ProRule:PRU00421}.
CC -!- DOMAIN: The EIIC domain forms the PTS system translocation channel and
CC contains the specific substrate-binding site. {ECO:0000255|PROSITE-
CC ProRule:PRU00426}.
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DR EMBL; CP000034; ABB62680.1; -; Genomic_DNA.
DR RefSeq; WP_001040498.1; NC_007606.1.
DR RefSeq; YP_404171.1; NC_007606.1.
DR AlphaFoldDB; Q32DC5; -.
DR SMR; Q32DC5; -.
DR STRING; 300267.SDY_2625; -.
DR EnsemblBacteria; ABB62680; ABB62680; SDY_2625.
DR KEGG; sdy:SDY_2625; -.
DR PATRIC; fig|300267.13.peg.3162; -.
DR HOGENOM; CLU_012312_2_0_6; -.
DR OMA; VAHCMTR; -.
DR Proteomes; UP000002716; 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: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 inner membrane; Cell membrane; Kinase; Membrane;
KW Phosphotransferase system; Reference proteome; Sugar transport;
KW Transferase; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..474
FT /note="PTS system N-acetylmuramic acid-specific EIIBC
FT component"
FT /id="PRO_0000248959"
FT TOPO_DOM 1..123
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 145..157
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 179..180
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 181..201
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 202..217
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 239..260
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 261..281
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 282..301
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 302..322
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 323..334
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 335..355
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 356..368
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 369..389
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 390..393
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 394..414
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 415..440
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 441..461
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TOPO_DOM 462..474
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 1..89
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT DOMAIN 115..474
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT ACT_SITE 29
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
SQ SEQUENCE 474 AA; 49812 MW; 44F99A26507D3001 CRC64;
MAKEISSELL NTILTRVGGP GNIASCGNCM TRLRLGVHDS SLVDPNIKTL EGVKGVILTS
DQVQVVFGPG KAHRATKAMS ELLGEAPVQD AAEIAAQNKR QLKAKQTSGV QQFLAKFATI
FTPLIPGFIA AGLLLGIATL IATVMHVPAD AQGTLPDALN FMKVFSKGLF TFLVILVGYN
AAQAFGGTGV NGAIIAALFL LGYNPAATTG YYAGFHDFFG LPIDPRGNII GVLIAAWACA
RIEGMVRRFM PDDLDMLLTS LITLLITATL AYLIIMPLGG WLFEGMSWLF MHLNSNPLGC
AVLAGLFLIA VVFGVHQGFI PVYLALMDSQ GFNSLFPILS MAGAGQVGAA LALYWRAQPH
SGLRSQVRGA IIPGLLGVGE PLIYGVTLPR MKPFITACLG GAAGGLFIGL IAWWGLPMGL
NSAFGPSGLV ALPLMTSAQG ILPAMAIYAG GILVAWVCGF IFTTLFGCRN VNLD
