PTJC_BACSU
ID PTJC_BACSU Reviewed; 452 AA.
AC P46317;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Lichenan permease IIC component;
DE AltName: Full=EIIC-Lic;
DE AltName: Full=PTS system lichenan-specific EIIC component;
GN Name=licC; Synonyms=celB; OrderedLocusNames=BSU38580;
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;
RX PubMed=8990303; DOI=10.1128/jb.179.2.496-506.1997;
RA Tobisch S., Glaser P., Krueger S., Hecker M.;
RT "Identification and characterization of a new beta-glucoside utilization
RT system in Bacillus subtilis.";
RL J. Bacteriol. 179:496-506(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168 / BGSC1A1;
RX PubMed=8969509; DOI=10.1099/13500872-142-11-3113;
RA Yoshida K., Shindo K., Sano H., Seki S., Fujimura M., Yanai N., Miwa Y.,
RA Fujita Y.;
RT "Sequencing of a 65 kb region of the Bacillus subtilis genome containing
RT the lic and cel loci, and creation of a 177 kb contig covering the gnt-
RT sacXY region.";
RL Microbiology 142:3113-3123(1996).
RN [3]
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).
CC -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC system (PTS), a major carbohydrate active -transport system, catalyzes
CC the phosphorylation of incoming sugar substrates concomitant with their
CC translocation across the cell membrane. This system is involved in
CC lichenan transport.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00428}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC ProRule:PRU00428}.
CC -!- INDUCTION: Induced by lichenan, lichenan hydrolysate and cellobiose.
CC Subject to carbon catabolite repression.
CC -!- DOMAIN: The EIIC domain forms the PTS system translocation channel and
CC contains the specific substrate-binding site.
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DR EMBL; Z49992; CAA90286.1; -; Genomic_DNA.
DR EMBL; D83026; BAA11744.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15884.1; -; Genomic_DNA.
DR PIR; F69651; F69651.
DR RefSeq; NP_391737.1; NC_000964.3.
DR RefSeq; WP_003243273.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P46317; -.
DR SMR; P46317; -.
DR STRING; 224308.BSU38580; -.
DR TCDB; 4.A.3.2.2; the pts lactose-n,n'-diacetylchitobiose-Beta-glucoside (lac) family.
DR jPOST; P46317; -.
DR PaxDb; P46317; -.
DR PRIDE; P46317; -.
DR EnsemblBacteria; CAB15884; CAB15884; BSU_38580.
DR GeneID; 937375; -.
DR KEGG; bsu:BSU38580; -.
DR PATRIC; fig|224308.179.peg.4177; -.
DR eggNOG; COG1455; Bacteria.
DR InParanoid; P46317; -.
DR OMA; IFTQQFF; -.
DR PhylomeDB; P46317; -.
DR BioCyc; BSUB:BSU38580-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 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 2: Evidence at transcript level;
KW Cell membrane; Membrane; Phosphotransferase system; Reference proteome;
KW Sugar transport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..452
FT /note="Lichenan permease IIC component"
FT /id="PRO_0000186484"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 104..124
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 138..158
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 246..266
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 291..311
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 351..373
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 402..422
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT DOMAIN 8..421
FT /note="PTS EIIC type-3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
SQ SEQUENCE 452 AA; 48534 MW; 396AE5531486C429 CRC64;
MNKVNQILEE KVMPIAGRIA GQRHLQALRD GIILTMPLII IGSFFLIIGN LPIPGYAEFM
AKTFGSSWSE KLAYPVDATF EIMGLVAAFG IAYRLAEKYG VDALSAGAIS LAAFLLATPY
QVPFMPDGAT KEIMVGGGIP LSLMGSKGLF VAMIIAMVST EIYRLIIQRN LVFKMPDGVP
PAVSKSFVAL IPGFAVIFLI WAARLIVEAT PFESLHNIVS VLLGTPLSIL GGSLGGSLVA
EAVKMLLWAC GLHGANIVGG VMAPIWYGAM DANRIAFQAG EELPKIFTQQ FFDIWVNIGG
SGATLALVVT MFLRARSKQM KQLGKLAVGP AIFNINEPII FGMPIVMNPM LLLPFIITPL
VTVTLTYIGM STGLVAKPAG IAVPWTMPPI FSGYLATGGK VSGAVMQAIN IAVSFVVYYP
FFRMWDKQKL KEENDLELVQ TPAATDDKEA AL
