PTYBC_PASMU
ID PTYBC_PASMU Reviewed; 476 AA.
AC Q9CKN5;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 120.
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=PM1575;
OS Pasteurella multocida (strain Pm70).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Pasteurella.
OX NCBI_TaxID=272843;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Pm70;
RX PubMed=11248100; DOI=10.1073/pnas.051634598;
RA May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.;
RT "Complete genomic sequence of Pasteurella multocida Pm70.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001).
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; AE004439; AAK03659.1; -; Genomic_DNA.
DR RefSeq; WP_005724420.1; NC_002663.1.
DR AlphaFoldDB; Q9CKN5; -.
DR SMR; Q9CKN5; -.
DR STRING; 747.DR93_424; -.
DR PRIDE; Q9CKN5; -.
DR EnsemblBacteria; AAK03659; AAK03659; PM1575.
DR KEGG; pmu:PM1575; -.
DR HOGENOM; CLU_012312_2_0_6; -.
DR OMA; FGIHQGF; -.
DR Proteomes; UP000000809; 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..476
FT /note="PTS system N-acetylmuramic acid-specific EIIBC
FT component"
FT /id="PRO_0000248956"
FT TRANSMEM 118..138
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 186..206
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 220..240
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 265..285
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 304..324
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 337..357
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 396..416
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 1..89
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT DOMAIN 116..476
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT ACT_SITE 28
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
SQ SEQUENCE 476 AA; 50204 MW; D8955DA5DFD1643E CRC64;
MATIDNAMIH SLIQHLGGKS NIQSVTNCMT RLRVTLHDSS VVDKDELKKI QGVLGVVEAD
EQLQLILGPG KATKAAEMMK ASLGDNMSSP SLQEIARTQK QQIKSAQTSS IHQFFAKFAT
IFTPLIPGFI GAGLLLGLAT VLQQAFVAGV ENPNAFLVDL IAYMKVFSKG LFSFLSILIG
YNAAKAFGGS GVNGAILASL FILGYNPEAT KGIYSGLSNF FGLTIDPRGN IIGVLIAAIV
GAKVERWVRK FIPDSLDMAL TSTVTLLIMG CFTFLFIMPI GVYLFNGMSW LFSNLNGNPL
GTAVLAGLFL ISVMLGIHQG FVPVYFALVE TQGFNALFPV LAMAGAGQVG AALALYFKAN
KGAVLRDQIK GAIIPGFLGI GEPLIYGVTL PRVKPFITAC IGGAAGGFTI GLIAYLGFPM
GLNTVFGPSG LLAIPLMTSP NGVLPAIATY LLGTVVAYAT GFITTYFFAT KDVDLS
