PTYBC_PHOLL
ID PTYBC_PHOLL Reviewed; 492 AA.
AC Q7N9D9;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-2003, sequence version 1.
DT 03-AUG-2022, entry version 112.
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=plu0402;
OS Photorhabdus laumondii subsp. laumondii (strain DSM 15139 / CIP 105565 /
OS TT01).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Photorhabdus.
OX NCBI_TaxID=243265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15139 / CIP 105565 / TT01;
RX PubMed=14528314; DOI=10.1038/nbt886;
RA Duchaud E., Rusniok C., Frangeul L., Buchrieser C., Givaudan A.,
RA Taourit S., Bocs S., Boursaux-Eude C., Chandler M., Charles J.-F.,
RA Dassa E., Derose R., Derzelle S., Freyssinet G., Gaudriault S., Medigue C.,
RA Lanois A., Powell K., Siguier P., Vincent R., Wingate V., Zouine M.,
RA Glaser P., Boemare N., Danchin A., Kunst F.;
RT "The genome sequence of the entomopathogenic bacterium Photorhabdus
RT luminescens.";
RL Nat. Biotechnol. 21:1307-1313(2003).
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; BX571860; CAE12697.1; -; Genomic_DNA.
DR RefSeq; WP_011144788.1; NC_005126.1.
DR AlphaFoldDB; Q7N9D9; -.
DR SMR; Q7N9D9; -.
DR STRING; 243265.plu0402; -.
DR EnsemblBacteria; CAE12697; CAE12697; plu0402.
DR GeneID; 24168253; -.
DR KEGG; plu:plu0402; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR HOGENOM; CLU_012312_2_0_6; -.
DR OMA; FGIHQGF; -.
DR OrthoDB; 328780at2; -.
DR BioCyc; PLUM243265:PLU_RS01955-MON; -.
DR Proteomes; UP000002514; 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..492
FT /note="PTS system N-acetylmuramic acid-specific EIIBC
FT component"
FT /id="PRO_0000248957"
FT TRANSMEM 125..145
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 193..213
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 265..285
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 378..398
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 403..423
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 450..470
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 123..487
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 492 AA; 52102 MW; 588081D67ABA87C6 CRC64;
MAKINQSVIA QILKAIGNAN NVAQCGNCMT RLRLTLRDST QVDKVALKQI PNVLGIIESD
DQFQIVLGPG KAQAAAEIMN ELLNSSTPTA QSKPSDTHLA NIASANKKQL KEKQVSAVHK
FLTKFATIFT PLIPGFIAVG LLLGFATLLE QITIQGVEHP NTILVEIIGY MKVFSKGMFS
FLSILIGYNA QKAFGGSGIN GAIIASLFVL SYNPDATSGF YSGISTFFGY SIDPRGNIIG
VLIAAILGAW VERQVRKIIP DNLDMILTSA ITLLIMGAIA FIFIMPLGSY LFSGMSWLFL
HLNGNPFGTA ILAGLFLLAV MFGVHQGFVP VYFALMEAQG FNSLFPILAM AGGGQVGAAL
ALYVKAKKDS LLRTQIKGAI IPGLLGIGEP LIYGVTLPRI KPFITACLGG AAGGFFIGLI
AYLGLPVGLN TVFGPSGLVA LPLMTSNNGI FVGMAVYAAG LVVAYISGFV LTLIFGSKKI
EVLKADVQSQ KE
