PTWCB_BACSU
ID PTWCB_BACSU Reviewed; 452 AA.
AC O34521; Q79ET9;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 135.
DE RecName: Full=PTS system N-acetylglucosamine-specific EIICB component;
DE AltName: Full=EIICB-Nag;
DE Includes:
DE RecName: Full=N-acetylglucosamine permease IIC component;
DE AltName: Full=PTS system N-acetylglucosamine-specific EIIC component;
DE Includes:
DE RecName: Full=N-acetylglucosamine-specific phosphotransferase enzyme IIB component;
DE EC=2.7.1.- {ECO:0000255|PROSITE-ProRule:PRU00421};
DE AltName: Full=PTS system N-acetylglucosamine-specific EIIB component;
GN Name=nagP; OrderedLocusNames=BSU07700;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / AC327;
RX PubMed=9272861; DOI=10.1016/s0378-1119(97)00130-3;
RA Yamamoto H., Uchiyama S., Nugroho F.A., Sekiguchi J.;
RT "Cloning and sequencing of a 35.7 kb in the 70 degree-73 degree region of
RT the Bacillus subtilis genome reveal genes for a new two-component system,
RT three spore germination proteins, an iron uptake system and a general
RT stress response protein.";
RL Gene 194:191-199(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP INDUCTION.
RX PubMed=21602348; DOI=10.1128/jb.00264-11;
RA Bertram R., Rigali S., Wood N., Lulko A.T., Kuipers O.P., Titgemeyer F.;
RT "Regulon of the N-acetylglucosamine utilization regulator NagR in Bacillus
RT subtilis.";
RL J. Bacteriol. 193:3525-3536(2011).
RN [4]
RP INTERACTION WITH FLOT, AND SUBCELLULAR LOCATION.
RC STRAIN=168;
RX PubMed=23651456; DOI=10.1111/mmi.12252;
RA Bach J.N., Bramkamp M.;
RT "Flotillins functionally organize the bacterial membrane.";
RL Mol. Microbiol. 88:1205-1217(2013).
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-acetylglucosamine transport (By similarity).
CC {ECO:0000250}.
CC -!- SUBUNIT: Interacts with FloT. {ECO:0000269|PubMed:23651456}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00426, ECO:0000269|PubMed:23651456}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00426}. Membrane raft
CC {ECO:0000269|PubMed:23651456}; Multi-pass membrane protein.
CC Note=Present in detergent-resistant membrane (DRM) fractions that may
CC be equivalent to eukaryotic membrane rafts; these rafts include
CC proteins involved in signaling, molecule trafficking and protein
CC secretion. {ECO:0000269|PubMed:23651456}.
CC -!- INDUCTION: Expression is repressed by the HTH-type transcriptional
CC regulator NagR. {ECO:0000269|PubMed:21602348}.
CC -!- DOMAIN: The EIIC domain type-1 forms the PTS system translocation
CC channel and contains the specific substrate-binding site.
CC {ECO:0000255|PROSITE-ProRule:PRU00426}.
CC -!- DOMAIN: The PTS EIIB type-1 domain is phosphorylated by phospho-EIIA on
CC a cysteinyl residue. Then, it transfers the phosphoryl group to the
CC sugar substrate concomitantly with the sugar uptake processed by the
CC PTS EIIC type-1 domain. {ECO:0000255|PROSITE-ProRule:PRU00421}.
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DR EMBL; D86417; BAA22299.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12599.1; -; Genomic_DNA.
DR PIR; D69810; D69810.
DR RefSeq; NP_388651.1; NC_000964.3.
DR RefSeq; WP_003243372.1; NZ_JNCM01000032.1.
DR AlphaFoldDB; O34521; -.
DR SMR; O34521; -.
DR STRING; 224308.BSU07700; -.
DR TCDB; 4.A.1.1.7; the pts glucose-glucoside (glc) family.
DR PaxDb; O34521; -.
DR DNASU; 938807; -.
DR EnsemblBacteria; CAB12599; CAB12599; BSU_07700.
DR GeneID; 938807; -.
DR KEGG; bsu:BSU07700; -.
DR PATRIC; fig|224308.179.peg.836; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR InParanoid; O34521; -.
DR OMA; IVHCARP; -.
DR PhylomeDB; O34521; -.
DR BioCyc; BSUB:BSU07700-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; IBA:GO_Central.
DR GO; GO:0045121; C:membrane raft; IEA:UniProtKB-SubCell.
DR GO; GO:0019866; C:organelle inner membrane; IEA:InterPro.
DR GO; GO:0016301; F:kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0015572; F:N-acetylglucosamine transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR GO; GO:0090587; F:protein-phosphocysteine-glucosamine phosphotransferase system transporter activity; IBA:GO_Central.
DR GO; GO:0090563; F:protein-phosphocysteine-sugar phosphotransferase activity; IBA:GO_Central.
DR GO; GO:0015764; P:N-acetylglucosamine transport; IBA:GO_Central.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IBA:GO_Central.
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 InterPro; IPR010974; PTS_IIBC_nag.
DR Pfam; PF00367; PTS_EIIB; 1.
DR Pfam; PF02378; PTS_EIIC; 1.
DR SUPFAM; SSF55604; SSF55604; 1.
DR TIGRFAMs; TIGR00826; EIIB_glc; 1.
DR TIGRFAMs; TIGR01998; PTS-II-BC-nag; 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 membrane; Kinase; Membrane; Phosphotransferase system;
KW Reference proteome; Sugar transport; Transferase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..452
FT /note="PTS system N-acetylglucosamine-specific EIICB
FT component"
FT /id="PRO_0000367594"
FT TRANSMEM 8..28
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 130..150
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 257..277
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 279..299
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 1..361
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 375..452
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT ACT_SITE 397
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
SQ SEQUENCE 452 AA; 48580 MW; 073A32A906843D53 CRC64;
MLSFLQKLGK SFMLPIAVLP AVGIILALGR EDVFNIPFVY QAGTAVFDHL PLIFAIGIAI
GISKDSNGAA GLSGAISYLM LDAATKTIDK TNNMAVFGGI IAGLIAGYTY NRFKDTKLPE
YLGFFSGRRL VPILTAIITI ILAGIFGVVW PPIQSCINSF GEWMLGLGGI GAGIFGLFNR
LLIPLGLHHV LNNIFWFQFG EYNGVTGDLA RFFAKDPTAG TYMTGFFPIM MFGLPAACLA
MVVTAKPSKR KATAGMMIGF ALTAFITGIT EPIEFAFMFL SPLLYAVHAV LTGLSLFIVN
WLGIRSGFSF SAGAIDYVLS YGIAEKPLLL LLVGICYAAV YFIVFYVLIK ALNLKTPGRE
DDDVDEVLDE NTVQDVNENI MLKGLGGKEN LQTIDHCATR LRLTVKDTAL VDEALLKKAG
AKGVVKSGGQ SVQVIIGPNV EFAAEELRAA VK
