PTYBC_ECOLI
ID PTYBC_ECOLI Reviewed; 474 AA.
AC P77272;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=PTS system N-acetylmuramic acid-specific EIIBC component {ECO:0000303|PubMed:15060041};
DE AltName: Full=EIIBC-MurNAc {ECO:0000303|PubMed:15060041};
DE Includes:
DE RecName: Full=N-acetylmuramic acid-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:15060041};
DE EC=2.7.1.192 {ECO:0000269|PubMed:15060041};
DE AltName: Full=PTS system N-acetylmuramic acid-specific EIIB component {ECO:0000303|PubMed:15060041};
DE Includes:
DE RecName: Full=N-acetylmuramic acid permease IIC component {ECO:0000303|PubMed:15060041};
DE AltName: Full=PTS system N-acetylmuramic acid-specific EIIC component {ECO:0000303|PubMed:15060041};
GN Name=murP; Synonyms=yfeV; OrderedLocusNames=b2429, JW2422;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9205837; DOI=10.1093/dnares/4.2.91;
RA Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N., Mizobuchi K.,
RA Mori H., Nakade S., Nakamura Y., Nashimoto H., Oshima T., Oyama S.,
RA Saito N., Sampei G., Satoh Y., Sivasundaram S., Tagami H., Takahashi H.,
RA Takeda J., Takemoto K., Uehara K., Wada C., Yamagata S., Horiuchi T.;
RT "Construction of a contiguous 874-kb sequence of the Escherichia coli-K12
RT genome corresponding to 50.0-68.8 min on the linkage map and analysis of
RT its sequence features.";
RL DNA Res. 4:91-113(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION IN MURNAC UPTAKE, AND CATALYTIC ACTIVITY.
RX PubMed=15060041; DOI=10.1128/jb.186.8.2385-2392.2004;
RA Dahl U., Jaeger T., Nguyen B.T., Sattler J.M., Mayer C.;
RT "Identification of a phosphotransferase system of Escherichia coli required
RT for growth on N-acetylmuramic acid.";
RL J. Bacteriol. 186:2385-2392(2004).
RN [5]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [6]
RP FUNCTION IN ANHMURNAC UPTAKE.
RX PubMed=16452451; DOI=10.1128/jb.188.4.1660-1662.2006;
RA Uehara T., Suefuji K., Jaeger T., Mayer C., Park J.T.;
RT "MurQ etherase is required by Escherichia coli in order to metabolize
RT anhydro-N-acetylmuramic acid obtained either from the environment or from
RT its own cell wall.";
RL J. Bacteriol. 188:1660-1662(2006).
RN [7]
RP INDUCTION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=18723630; DOI=10.1128/jb.00642-08;
RA Jaeger T., Mayer C.;
RT "The transcriptional factors MurR and catabolite activator protein regulate
RT N-acetylmuramic acid catabolism in Escherichia coli.";
RL J. Bacteriol. 190:6598-6608(2008).
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 responsible for growth on MurNAc as the sole
CC source of carbon and energy. Is also able to take up anhydro-N-
CC acetylmuramic acid (anhMurNAc), but cannot phosphorylate the carbon 6,
CC probably because of the 1,6-anhydro ring. {ECO:0000269|PubMed:15060041,
CC ECO:0000269|PubMed:16452451}.
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:0000269|PubMed:15060041};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00426}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC ProRule:PRU00426}.
CC -!- INDUCTION: Induced by MurNAc 6-phosphate that releases the repressor
CC MurR from the DNA. Also up-regulated by the cAMP receptor protein crp
CC via the binding of crp-cAMP to a class I site upstream of the murQ
CC promoter. Repressed by MurR in the absence of MurNAc 6-phosphate.
CC {ECO:0000269|PubMed:18723630}.
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}.
CC -!- MISCELLANEOUS: The PTS domain EIIA required for activity was shown to
CC be the crr-encoded enzyme IIA-glucose, EIIA-Glc.
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DR EMBL; U00096; AAC75482.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA16313.1; -; Genomic_DNA.
DR PIR; D65017; D65017.
DR RefSeq; NP_416924.1; NC_000913.3.
DR RefSeq; WP_001040483.1; NZ_CP047127.1.
DR AlphaFoldDB; P77272; -.
DR SMR; P77272; -.
DR BioGRID; 4260573; 11.
DR STRING; 511145.b2429; -.
DR TCDB; 4.A.1.2.7; the pts glucose-glucoside (glc) family.
DR PaxDb; P77272; -.
DR PRIDE; P77272; -.
DR EnsemblBacteria; AAC75482; AAC75482; b2429.
DR EnsemblBacteria; BAA16313; BAA16313; BAA16313.
DR GeneID; 946894; -.
DR KEGG; ecj:JW2422; -.
DR KEGG; eco:b2429; -.
DR PATRIC; fig|1411691.4.peg.4302; -.
DR EchoBASE; EB3915; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR HOGENOM; CLU_012312_2_0_6; -.
DR InParanoid; P77272; -.
DR OMA; VAHCMTR; -.
DR PhylomeDB; P77272; -.
DR BioCyc; EcoCyc:MON0-5; -.
DR BioCyc; MetaCyc:MON0-5; -.
DR BRENDA; 2.7.1.192; 2026.
DR PRO; PR:P77272; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0016020; C:membrane; IDA:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
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:0090588; F:protein-phosphocysteine-N-acetylmuramate phosphotransferase system transporter activity; IMP:EcoCyc.
DR GO; GO:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IBA:GO_Central.
DR GO; GO:0034219; P:carbohydrate transmembrane transport; IMP:EcoCyc.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IMP:EcoCyc.
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 1: Evidence at protein level;
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_0000186709"
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; 49802 MW; EA5D8849A303737C CRC64;
MAKEISSELL NTILTRVGGP GNIASCGNCM TRLRLGVHDS SLVDPNIKTL EGVKGVILTS
DQVQVVFGPG KAHRAAKAMS ELLGEAPVQD AAEIAAQNKR QLKAKQTSGV QQFLAKFATI
FTPLIPGFIA AGLLLGIATL IATVMHVPAD AQGTLPDALN FMKVFSKGLF TFLVILVGYN
AAQAFGGTGV NGAIIAALFL LGYNPAATTG YYAGFHDFFG LPIDPRGNII GVLIAAWACA
RIEGMVRRFM PDDLDMLLTS LITLLITATL AYLIIMPLGG WLFEGMSWLF MHLNSNPFGC
AVLAGLFLIA VVFGVHQGFI PVYLALMDSQ GFNSLFPILS MAGAGQVGAA LALYWRAQPH
SALRSQVRGA IIPGLLGVGE PLIYGVTLPR MKPFVTACLG GAAGGLFIGL IAWWGLPMGL
NSAFGPSGLV ALPLMTSAQG ILPAMAVYAG GILVAWVCGF IFTTLFGCRN VNLD
