PTEC_BACSU
ID PTEC_BACSU Reviewed; 442 AA.
AC O05507; Q797E0;
DT 05-MAY-2009, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1997, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=PTS system oligo-beta-mannoside-specific EIIC component {ECO:0000303|PubMed:18177310};
DE AltName: Full=Glucomannan utilization protein C {ECO:0000303|PubMed:18177310};
DE AltName: Full=Oligo-beta-mannoside permease IIC component {ECO:0000303|PubMed:18177310};
GN Name=gmuC {ECO:0000303|PubMed:18177310}; Synonyms=ydhO;
GN OrderedLocusNames=BSU05830;
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 / JH642;
RX PubMed=9202461; DOI=10.1099/00221287-143-6-1861;
RA Sadaie Y., Yata K., Fujita M., Sagai H., Itaya M., Kasahara Y.,
RA Ogasawara N.;
RT "Nucleotide sequence and analysis of the phoB-rrnE-groESL region of the
RT Bacillus subtilis chromosome.";
RL Microbiology 143:1861-1866(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 FUNCTION IN GLUCOMANNAN UTILIZATION, AND INDUCTION.
RC STRAIN=168;
RX PubMed=18177310; DOI=10.1111/j.1574-6968.2007.01018.x;
RA Sadaie Y., Nakadate H., Fukui R., Yee L.M., Asai K.;
RT "Glucomannan utilization operon of Bacillus subtilis.";
RL FEMS Microbiol. Lett. 279:103-109(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. The
CC enzyme II GmuABC PTS system is involved in the transport of oligo-
CC glucomannans such as cellobiose or mannobiose.
CC {ECO:0000305|PubMed:18177310}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00428}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC ProRule:PRU00428}.
CC -!- INDUCTION: Up-regulated by konjac glucomannan and by cellobiose and
CC mannobiose, the possible degradation products of glucomannan. Repressed
CC by glucose via the carbon catabolite repression system. Also repressed
CC by GmuR. {ECO:0000269|PubMed:18177310}.
CC -!- DOMAIN: The EIIC type-3 domain forms the PTS system translocation
CC channel and contains the specific substrate-binding site.
CC {ECO:0000255|PROSITE-ProRule:PRU00428}.
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DR EMBL; D88802; BAA19707.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB12402.1; -; Genomic_DNA.
DR PIR; C69785; C69785.
DR RefSeq; NP_388464.1; NC_000964.3.
DR RefSeq; WP_003244271.1; NZ_JNCM01000031.1.
DR AlphaFoldDB; O05507; -.
DR SMR; O05507; -.
DR STRING; 224308.BSU05830; -.
DR TCDB; 4.A.3.2.10; the pts lactose-n,n'-diacetylchitobiose-Beta-glucoside (lac) family.
DR PaxDb; O05507; -.
DR PRIDE; O05507; -.
DR EnsemblBacteria; CAB12402; CAB12402; BSU_05830.
DR GeneID; 939882; -.
DR KEGG; bsu:BSU05830; -.
DR PATRIC; fig|224308.179.peg.627; -.
DR eggNOG; COG1455; Bacteria.
DR InParanoid; O05507; -.
DR OMA; VFVIWFP; -.
DR PhylomeDB; O05507; -.
DR BioCyc; BSUB:BSU05830-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR GO; GO:1901264; P:carbohydrate derivative transport; IBA:GO_Central.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR GO; GO:0015774; P:polysaccharide transport; IEA:UniProtKB-KW.
DR InterPro; IPR003352; PTS_EIIC.
DR InterPro; IPR004501; PTS_EIIC_3.
DR InterPro; IPR004796; PTS_IIC_cello.
DR Pfam; PF02378; PTS_EIIC; 1.
DR PIRSF; PIRSF006351; PTS_EIIC-Cellobiose; 1.
DR TIGRFAMs; TIGR00359; cello_pts_IIC; 1.
DR TIGRFAMs; TIGR00410; lacE; 1.
DR PROSITE; PS51105; PTS_EIIC_TYPE_3; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Membrane; Phosphotransferase system;
KW Polysaccharide transport; Reference proteome; Sugar transport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..442
FT /note="PTS system oligo-beta-mannoside-specific EIIC
FT component"
FT /id="PRO_0000372432"
FT TRANSMEM 28..48
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 97..117
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 138..157
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 177..197
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 205..225
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 286..306
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 329..349
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 391..411
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT DOMAIN 5..411
FT /note="PTS EIIC type-3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
SQ SEQUENCE 442 AA; 48436 MW; 295BD7005291B36E CRC64;
MFEKISQFLV PIAGRLNNNR YLQVLRDAFM LAFPLTIFGS IFVVLTNLPF LNKIMNASML
TSFQSHFGIA STATMGIMSV FVVFGIGYYL SKSYQVEAVF GGAIALVSFL LLTPFIIQPE
TGDAITGVIP VDRLGAKGMF LGMITAFLSG EIYRRIVQKN LTIKMPAGVP PAVAKSFAAL
IPAFITLTVF LLINVMVTLF FKTNMHDVIY HAIQAPLVGL GSGIIPTLIA VFFIQILWFF
GLHGQIIINS VMDPIWNTLQ VENLSAYTAG KEIPHIISKP FMEIYTVGMG GTGMTLAIVF
TILIFMKSRQ MKQVSKLGLA PGIFNVNEPI IFGLPIVMNP IIIVPWVLAP MVVTLVTYLA
MSAGLVPPPT GVTVPWTVPL FINGIMATNS IMGGVMQLIN LLIVFVIWFP FLKAMDKLNL
AKEKEQAVQE TAAQQNDNSI KM
