PTJA_BACSU
ID PTJA_BACSU Reviewed; 110 AA.
AC P46319;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Lichenan-specific phosphotransferase enzyme IIA component;
DE AltName: Full=EIIA-Lic;
DE AltName: Full=EIII-Lic;
DE AltName: Full=PTS system lichenan-specific EIIA component;
GN Name=licA; Synonyms=celC; OrderedLocusNames=BSU38570;
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: Cytoplasm {ECO:0000305}.
CC -!- INDUCTION: Induced by lichenan, lichenan hydrolysate and cellobiose.
CC Subject to carbon catabolite repression.
CC -!- DOMAIN: The EIIA domain is phosphorylated by phospho-HPr on a histidyl
CC residue. Then, it transfers the phosphoryl group to the EIIB domain.
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DR EMBL; Z49992; CAA90287.1; -; Genomic_DNA.
DR EMBL; D83026; BAA11745.1; -; Genomic_DNA.
DR EMBL; AL009126; CAB15883.1; -; Genomic_DNA.
DR PIR; D69651; D69651.
DR RefSeq; NP_391736.1; NC_000964.3.
DR RefSeq; WP_003227313.1; NZ_JNCM01000034.1.
DR AlphaFoldDB; P46319; -.
DR SMR; P46319; -.
DR STRING; 224308.BSU38570; -.
DR TCDB; 4.A.3.2.2; the pts lactose-n,n'-diacetylchitobiose-Beta-glucoside (lac) family.
DR jPOST; P46319; -.
DR PaxDb; P46319; -.
DR PRIDE; P46319; -.
DR EnsemblBacteria; CAB15883; CAB15883; BSU_38570.
DR GeneID; 937374; -.
DR KEGG; bsu:BSU38570; -.
DR PATRIC; fig|224308.179.peg.4176; -.
DR eggNOG; COG1447; Bacteria.
DR InParanoid; P46319; -.
DR OMA; MEQSRMA; -.
DR PhylomeDB; P46319; -.
DR BioCyc; BSUB:BSU38570-MON; -.
DR Proteomes; UP000001570; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR CDD; cd00215; PTS_IIA_lac; 1.
DR InterPro; IPR003188; PTS_IIA_lac/cel.
DR InterPro; IPR036542; PTS_IIA_lac/cel_sf.
DR PANTHER; PTHR34382; PTHR34382; 1.
DR Pfam; PF02255; PTS_IIA; 1.
DR PIRSF; PIRSF000699; PTS_IILac_III; 1.
DR SUPFAM; SSF46973; SSF46973; 1.
DR TIGRFAMs; TIGR00823; EIIA-LAC; 1.
DR PROSITE; PS51095; PTS_EIIA_TYPE_3; 1.
PE 2: Evidence at transcript level;
KW Cytoplasm; Phosphotransferase system; Reference proteome; Sugar transport;
KW Transferase; Transport.
FT CHAIN 1..110
FT /note="Lichenan-specific phosphotransferase enzyme IIA
FT component"
FT /id="PRO_0000186493"
FT DOMAIN 3..101
FT /note="PTS EIIA type-3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00418"
FT ACT_SITE 77
FT /note="Tele-phosphohistidine intermediate; by HPr"
FT /evidence="ECO:0000250"
SQ SEQUENCE 110 AA; 12185 MW; AFF381CEBE9704A3 CRC64;
MNEEMEQIIF QIILHGGNGR SSAMEAIAAA KSGDAEEARK KLQDAAEELS KAHHYQTELI
QNEAGGEKTE MTLLMVHAQD HLMNAMTVKD MAAEIIELYE KITEQRGASI
