ID   PTJB_BACSU              Reviewed;         102 AA.
AC   P46318;
DT   01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1995, sequence version 1.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Lichenan-specific phosphotransferase enzyme IIB component;
DE            EC=2.7.1.-;
DE   AltName: Full=EIIB-Lic;
DE   AltName: Full=PTS system lichenan-specific EIIB component;
GN   Name=licB; Synonyms=celA; OrderedLocusNames=BSU38590;
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).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY.
RC   STRAIN=168;
RX   PubMed=17218307; DOI=10.1074/mcp.m600464-mcp200;
RA   Macek B., Mijakovic I., Olsen J.V., Gnad F., Kumar C., Jensen P.R.,
RA   Mann M.;
RT   "The serine/threonine/tyrosine phosphoproteome of the model bacterium
RT   Bacillus subtilis.";
RL   Mol. Cell. Proteomics 6:697-707(2007).
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 lichenan transport.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- INDUCTION: Induced by lichenan, lichenan hydrolysate and cellobiose.
CC       Subject to carbon catabolite repression.
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.
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DR   EMBL; Z49992; CAA90285.1; -; Genomic_DNA.
DR   EMBL; D83026; BAA11743.1; -; Genomic_DNA.
DR   EMBL; AL009126; CAB15885.1; -; Genomic_DNA.
DR   PIR; E69651; E69651.
DR   RefSeq; NP_391738.1; NC_000964.3.
DR   RefSeq; WP_003218755.1; NZ_JNCM01000034.1.
DR   AlphaFoldDB; P46318; -.
DR   SMR; P46318; -.
DR   STRING; 224308.BSU38590; -.
DR   TCDB; 4.A.3.2.2; the pts lactose-n,n'-diacetylchitobiose-Beta-glucoside (lac) family.
DR   iPTMnet; P46318; -.
DR   jPOST; P46318; -.
DR   PaxDb; P46318; -.
DR   PRIDE; P46318; -.
DR   EnsemblBacteria; CAB15885; CAB15885; BSU_38590.
DR   GeneID; 64305640; -.
DR   GeneID; 937379; -.
DR   KEGG; bsu:BSU38590; -.
DR   PATRIC; fig|224308.179.peg.4178; -.
DR   eggNOG; COG1440; Bacteria.
DR   InParanoid; P46318; -.
DR   OMA; IKEYDVC; -.
DR   PhylomeDB; P46318; -.
DR   BioCyc; BSUB:BSU38590-MON; -.
DR   Proteomes; UP000001570; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; 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   InterPro; IPR036095; PTS_EIIB-like_sf.
DR   InterPro; IPR003501; PTS_EIIB_2/3.
DR   InterPro; IPR013012; PTS_EIIB_3.
DR   Pfam; PF02302; PTS_IIB; 1.
DR   SUPFAM; SSF52794; SSF52794; 1.
DR   TIGRFAMs; TIGR00853; pts-lac; 1.
DR   PROSITE; PS51100; PTS_EIIB_TYPE_3; 1.
PE   1: Evidence at protein level;
KW   Cytoplasm; Kinase; Phosphoprotein; Phosphotransferase system;
KW   Reference proteome; Sugar transport; Transferase; Transport.
FT   CHAIN           1..102
FT                   /note="Lichenan-specific phosphotransferase enzyme IIB
FT                   component"
FT                   /id="PRO_0000186487"
FT   DOMAIN          1..102
FT                   /note="PTS EIIB type-3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00423"
FT   ACT_SITE        7
FT                   /note="Phosphocysteine intermediate"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         37
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000269|PubMed:17218307"
SQ   SEQUENCE   102 AA;  10955 MW;  169F90331BDBBE9E CRC64;
     MNILLVCAAG MSTSLLVSKM EKSAQEQGKD YTIWAVSGDS VQNHIDKADV LLLGPQVRYM
     LPQLKKLGES KGVPVDVINT VHYGTCNGAE VLKSAEQLGH VS