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PTS system N-acetylmuramic acid-specific EIIBC component (EIIBC-MurNAc) [Includes: N-acetylmuramic acid-specific phosphotransferase enzyme IIB component (EC 2.7.1.192) (PTS system N-acetylmuramic acid-specific EIIB component); N-acetylmuramic acid permease IIC component (PTS system N-acetylmuramic acid-specific EIIC component)]

 PTYBC_ECOLI             Reviewed;         474 AA.
P77272;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
01-FEB-1997, sequence version 1.
28-MAR-2018, entry version 144.
RecName: Full=PTS system N-acetylmuramic acid-specific EIIBC component {ECO:0000303|PubMed:15060041};
AltName: Full=EIIBC-MurNAc {ECO:0000303|PubMed:15060041};
Includes:
RecName: Full=N-acetylmuramic acid-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:15060041};
EC=2.7.1.192 {ECO:0000269|PubMed:15060041};
AltName: Full=PTS system N-acetylmuramic acid-specific EIIB component {ECO:0000303|PubMed:15060041};
Includes:
RecName: Full=N-acetylmuramic acid permease IIC component {ECO:0000303|PubMed:15060041};
AltName: Full=PTS system N-acetylmuramic acid-specific EIIC component {ECO:0000303|PubMed:15060041};
Name=murP; Synonyms=yfeV; OrderedLocusNames=b2429, JW2422;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9205837; DOI=10.1093/dnares/4.2.91;
Yamamoto Y., Aiba H., Baba T., Hayashi K., Inada T., Isono K.,
Itoh T., Kimura S., Kitagawa M., Makino K., Miki T., Mitsuhashi N.,
Mizobuchi K., Mori H., Nakade S., Nakamura Y., Nashimoto H.,
Oshima T., Oyama S., Saito N., Sampei G., Satoh Y., Sivasundaram S.,
Tagami H., Takahashi H., Takeda J., Takemoto K., Uehara K., Wada C.,
Yamagata S., Horiuchi T.;
"Construction of a contiguous 874-kb sequence of the Escherichia coli-
K12 genome corresponding to 50.0-68.8 min on the linkage map and
analysis of its sequence features.";
DNA Res. 4:91-113(1997).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J.,
Mau B., Shao Y.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[4]
FUNCTION IN MURNAC UPTAKE, AND CATALYTIC ACTIVITY.
PubMed=15060041; DOI=10.1128/JB.186.8.2385-2392.2004;
Dahl U., Jaeger T., Nguyen B.T., Sattler J.M., Mayer C.;
"Identification of a phosphotransferase system of Escherichia coli
required for growth on N-acetylmuramic acid.";
J. Bacteriol. 186:2385-2392(2004).
[5]
TOPOLOGY [LARGE SCALE ANALYSIS].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=15919996; DOI=10.1126/science.1109730;
Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
"Global topology analysis of the Escherichia coli inner membrane
proteome.";
Science 308:1321-1323(2005).
[6]
FUNCTION IN ANHMURNAC UPTAKE.
PubMed=16452451; DOI=10.1128/JB.188.4.1660-1662.2006;
Uehara T., Suefuji K., Jaeger T., Mayer C., Park J.T.;
"MurQ etherase is required by Escherichia coli in order to metabolize
anhydro-N-acetylmuramic acid obtained either from the environment or
from its own cell wall.";
J. Bacteriol. 188:1660-1662(2006).
[7]
INDUCTION.
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=18723630; DOI=10.1128/JB.00642-08;
Jaeger T., Mayer C.;
"The transcriptional factors MurR and catabolite activator protein
regulate N-acetylmuramic acid catabolism in Escherichia coli.";
J. Bacteriol. 190:6598-6608(2008).
-!- FUNCTION: The phosphoenolpyruvate-dependent sugar
phosphotransferase system (sugar PTS), a major carbohydrate active
transport system, catalyzes the phosphorylation of incoming sugar
substrates concomitantly with their translocation across the cell
membrane. This system is involved in N-acetylmuramic acid (MurNAc)
transport, yielding cytoplasmic MurNAc-6-P. Is responsible for
growth on MurNAc as the sole source of carbon and energy. Is also
able to take up anhydro-N-acetylmuramic acid (anhMurNAc), but
cannot phosphorylate the carbon 6, probably because of the 1,6-
anhydro ring. {ECO:0000269|PubMed:15060041,
ECO:0000269|PubMed:16452451}.
-!- CATALYTIC ACTIVITY: [Protein]-N(pi)-phospho-L-histidine + N-
acetylmuramate(Side 1) = [protein]-L-histidine + N-acetylmuramate
6-phosphate(Side 2). {ECO:0000269|PubMed:15060041}.
-!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|PROSITE-
ProRule:PRU00426}; Multi-pass membrane protein
{ECO:0000255|PROSITE-ProRule:PRU00426}.
-!- INDUCTION: Induced by MurNAc 6-phosphate that releases the
repressor MurR from the DNA. Also up-regulated by the cAMP
receptor protein crp via the binding of crp-cAMP to a class I site
upstream of the murQ promoter. Repressed by MurR in the absence of
MurNAc 6-phosphate. {ECO:0000269|PubMed:18723630}.
-!- DOMAIN: The EIIB domain is phosphorylated by phospho-EIIA on a
cysteinyl or histidyl residue, depending on the transported sugar.
Then, it transfers the phosphoryl group to the sugar substrate
concomitantly with the sugar uptake processed by the EIIC domain.
{ECO:0000255|PROSITE-ProRule:PRU00421}.
-!- DOMAIN: The EIIC domain forms the PTS system translocation channel
and contains the specific substrate-binding site.
{ECO:0000255|PROSITE-ProRule:PRU00426}.
-!- MISCELLANEOUS: The PTS domain EIIA required for activity was shown
to be the crr-encoded enzyme IIA-glucose, EIIA-Glc.
-----------------------------------------------------------------------
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EMBL; U00096; AAC75482.1; -; Genomic_DNA.
EMBL; AP009048; BAA16313.1; -; Genomic_DNA.
PIR; D65017; D65017.
RefSeq; NP_416924.1; NC_000913.3.
RefSeq; WP_001040483.1; NZ_CP014272.1.
ProteinModelPortal; P77272; -.
BioGrid; 4260573; 11.
STRING; 316385.ECDH10B_2594; -.
TCDB; 4.A.1.2.7; the pts glucose-glucoside (glc) family.
PaxDb; P77272; -.
PRIDE; P77272; -.
EnsemblBacteria; AAC75482; AAC75482; b2429.
EnsemblBacteria; BAA16313; BAA16313; BAA16313.
GeneID; 946894; -.
KEGG; ecj:JW2422; -.
KEGG; eco:b2429; -.
PATRIC; fig|1411691.4.peg.4302; -.
EchoBASE; EB3915; -.
EcoGene; EG14163; murP.
eggNOG; ENOG4105C5Y; Bacteria.
eggNOG; COG2190; LUCA.
HOGENOM; HOG000102024; -.
InParanoid; P77272; -.
KO; K11191; -.
KO; K11192; -.
OMA; RIESEPN; -.
PhylomeDB; P77272; -.
BioCyc; EcoCyc:MONOMER0-5; -.
BioCyc; MetaCyc:MONOMER0-5; -.
PRO; PR:P77272; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
GO; GO:0016020; C:membrane; IDA:EcoCyc.
GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
GO; GO:0090588; F:protein-phosphocysteine-N-acetylmuramate phosphotransferase system transporter activity; IMP:EcoCyc.
GO; GO:0034219; P:carbohydrate transmembrane transport; IMP:EcoCyc.
GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IMP:EcoCyc.
CDD; cd00212; PTS_IIB_glc; 1.
Gene3D; 3.30.1360.60; -; 1.
InterPro; IPR036878; Glu_permease_IIB.
InterPro; IPR018113; PTrfase_EIIB_Cys.
InterPro; IPR003352; PTS_EIIC.
InterPro; IPR013013; PTS_EIIC_1.
InterPro; IPR001996; PTS_IIB_1.
Pfam; PF00367; PTS_EIIB; 1.
Pfam; PF02378; PTS_EIIC; 1.
SUPFAM; SSF55604; SSF55604; 1.
PROSITE; PS51098; PTS_EIIB_TYPE_1; 1.
PROSITE; PS01035; PTS_EIIB_TYPE_1_CYS; 1.
PROSITE; PS51103; PTS_EIIC_TYPE_1; 1.
1: Evidence at protein level;
Cell inner membrane; Cell membrane; Complete proteome; Kinase;
Membrane; Phosphotransferase system; Reference proteome;
Sugar transport; Transferase; Transmembrane; Transmembrane helix;
Transport.
CHAIN 1 474 PTS system N-acetylmuramic acid-specific
EIIBC component.
/FTId=PRO_0000186709.
TOPO_DOM 1 123 Cytoplasmic. {ECO:0000255}.
TRANSMEM 124 144 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
TOPO_DOM 145 157 Periplasmic. {ECO:0000255}.
TRANSMEM 158 178 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
TOPO_DOM 179 180 Cytoplasmic. {ECO:0000255}.
TRANSMEM 181 201 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
TOPO_DOM 202 217 Periplasmic. {ECO:0000255}.
TRANSMEM 218 238 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
TOPO_DOM 239 260 Cytoplasmic. {ECO:0000255}.
TRANSMEM 261 281 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
TOPO_DOM 282 301 Periplasmic. {ECO:0000255}.
TRANSMEM 302 322 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
TOPO_DOM 323 334 Cytoplasmic. {ECO:0000255}.
TRANSMEM 335 355 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
TOPO_DOM 356 368 Periplasmic. {ECO:0000255}.
TRANSMEM 369 389 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
TOPO_DOM 390 393 Cytoplasmic. {ECO:0000255}.
TRANSMEM 394 414 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
TOPO_DOM 415 440 Periplasmic. {ECO:0000255}.
TRANSMEM 441 461 Helical. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
TOPO_DOM 462 474 Cytoplasmic. {ECO:0000255}.
DOMAIN 1 89 PTS EIIB type-1. {ECO:0000255|PROSITE-
ProRule:PRU00421}.
DOMAIN 115 474 PTS EIIC type-1. {ECO:0000255|PROSITE-
ProRule:PRU00426}.
ACT_SITE 29 29 Phosphocysteine intermediate; for EIIB
activity. {ECO:0000255|PROSITE-
ProRule:PRU00421}.
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


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