PTS3B_STRMU
ID PTS3B_STRMU Reviewed; 664 AA.
AC P12655;
DT 01-OCT-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1989, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=PTS system sucrose-specific EIIBCA component;
DE AltName: Full=EIIBCA-Scr;
DE Short=EII-Scr;
DE Includes:
DE RecName: Full=Sucrose-specific phosphotransferase enzyme IIB component;
DE EC=2.7.1.-;
DE AltName: Full=PTS system sucrose-specific EIIB component;
DE Includes:
DE RecName: Full=Sucrose permease IIC component;
DE AltName: Full=PTS system sucrose-specific EIIC component;
DE Includes:
DE RecName: Full=Sucrose-specific phosphotransferase enzyme IIA component;
DE AltName: Full=PTS system sucrose-specific EIIA component;
GN Name=scrA; OrderedLocusNames=SMU_1841;
OS Streptococcus mutans serotype c (strain ATCC 700610 / UA159).
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Streptococcus.
OX NCBI_TaxID=210007;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=GS-5;
RX PubMed=2536656; DOI=10.1128/jb.171.1.263-271.1989;
RA Sato Y., Poy F., Jacobson G.R., Kuramitsu H.K.;
RT "Characterization and sequence analysis of the scrA gene encoding enzyme
RT IIScr of the Streptococcus mutans phosphoenolpyruvate-dependent sucrose
RT phosphotransferase system.";
RL J. Bacteriol. 171:263-271(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700610 / UA159;
RX PubMed=12397186; DOI=10.1073/pnas.172501299;
RA Ajdic D.J., McShan W.M., McLaughlin R.E., Savic G., Chang J., Carson M.B.,
RA Primeaux C., Tian R., Kenton S., Jia H.G., Lin S.P., Qian Y., Li S.,
RA Zhu H., Najar F.Z., Lai H., White J., Roe B.A., Ferretti J.J.;
RT "Genome sequence of Streptococcus mutans UA159, a cariogenic dental
RT pathogen.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:14434-14439(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 639-664.
RC STRAIN=GS-5;
RX PubMed=8336109; DOI=10.1099/00221287-139-5-921;
RA Sato Y., Yamamoto Y., Kizaki H., Kuramitsu H.K.;
RT "Isolation, characterization and sequence analysis of the scrK gene
RT encoding fructokinase of Streptococcus mutans.";
RL J. Gen. Microbiol. 139:921-927(1993).
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 sucrose transport.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
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.
CC -!- DOMAIN: The EIIC domain forms the PTS system translocation channel and
CC contains the specific substrate-binding site.
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; M22711; AAA26971.1; -; Genomic_DNA.
DR EMBL; AE014133; AAN59464.1; -; Genomic_DNA.
DR EMBL; D13175; BAA02466.1; -; Genomic_DNA.
DR PIR; B32243; B32243.
DR RefSeq; NP_722158.1; NC_004350.2.
DR RefSeq; WP_002262657.1; NC_004350.2.
DR AlphaFoldDB; P12655; -.
DR SMR; P12655; -.
DR STRING; 210007.SMU_1841; -.
DR PRIDE; P12655; -.
DR EnsemblBacteria; AAN59464; AAN59464; SMU_1841.
DR KEGG; smu:SMU_1841; -.
DR PATRIC; fig|210007.7.peg.1644; -.
DR eggNOG; COG1263; Bacteria.
DR eggNOG; COG1264; Bacteria.
DR eggNOG; COG2190; Bacteria.
DR HOGENOM; CLU_012312_2_1_9; -.
DR OMA; FLSIYPK; -.
DR PhylomeDB; P12655; -.
DR BRENDA; 2.7.1.211; 14748.
DR Proteomes; UP000002512; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; 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 CDD; cd00212; PTS_IIB_glc; 1.
DR Gene3D; 2.70.70.10; -; 1.
DR Gene3D; 3.30.1360.60; -; 1.
DR InterPro; IPR011055; Dup_hybrid_motif.
DR InterPro; IPR036878; Glu_permease_IIB.
DR InterPro; IPR018113; PTrfase_EIIB_Cys.
DR InterPro; IPR001127; PTS_EIIA_1_perm.
DR InterPro; IPR003352; PTS_EIIC.
DR InterPro; IPR013013; PTS_EIIC_1.
DR InterPro; IPR001996; PTS_IIB_1.
DR InterPro; IPR010973; PTS_IIBC_sucr.
DR Pfam; PF00358; PTS_EIIA_1; 1.
DR Pfam; PF00367; PTS_EIIB; 1.
DR Pfam; PF02378; PTS_EIIC; 1.
DR SUPFAM; SSF51261; SSF51261; 1.
DR SUPFAM; SSF55604; SSF55604; 1.
DR TIGRFAMs; TIGR00826; EIIB_glc; 1.
DR TIGRFAMs; TIGR00830; PTBA; 1.
DR TIGRFAMs; TIGR01996; PTS-II-BC-sucr; 1.
DR PROSITE; PS51093; PTS_EIIA_TYPE_1; 1.
DR PROSITE; PS00371; PTS_EIIA_TYPE_1_HIS; 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 4: Predicted;
KW Cell membrane; Kinase; Membrane; Phosphotransferase system;
KW Reference proteome; Sugar transport; Transferase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..664
FT /note="PTS system sucrose-specific EIIBCA component"
FT /id="PRO_0000186676"
FT TRANSMEM 109..129
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 158..178
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 187..207
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 271..291
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 310..330
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 411..433
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT TRANSMEM 453..473
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 1..86
FT /note="PTS EIIB type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT DOMAIN 108..492
FT /note="PTS EIIC type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00426"
FT DOMAIN 533..637
FT /note="PTS EIIA type-1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT ACT_SITE 25
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00421"
FT ACT_SITE 585
FT /note="Tele-phosphohistidine intermediate; for EIIA
FT activity"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
SQ SEQUENCE 664 AA; 69989 MW; 809E63E32281A9A1 CRC64;
MDYSKVASEV ITAVGKDNLV AAAHCATRLR LVLKDDSKVD QKALDKNADV KGTFKTDGQY
QVIIGPGDVN FVYDEIIKQT GLTEVSTDDL KKIAASGKKF NPIMALIKLL SDIFVPIIPA
LVAGGLLMAL NNFLTSEGLF GTKSLVQQFP IIKGSSDMIQ LMSAAPFWFL PILVGISAAK
RFGANQFLGA SIGMIMVAPG AANIIGLAAN APISKAATIG AYTGFWNIFG LHVTQASYTY
QVIPVLVAVW LLSILEKFFH KRLPSAVDFT FTPLLSVIIT GFLTFIVIGP VMKEVSDWLT
NGIVWLYDTT GFLGMGVFGA LYSPVVMTGL HQSFPAIETQ LISAFQNGTG HGDFIFVTAS
MANVAQGAAT FAIYFLTKDK KMKGLSSSSG VSALLGITEP ALFGVNLKYR FPFFCALIGS
ASAAAIAGLL QVVAVSLGSA GFLGFLSIKA SSIPFYVVCE LISFAIAFAV TYGYGKTKAV
DVFAAEAAVE EAIEEVQEIP EEAASAANKA QVTDEVLAAP LAGEAVELTS VNDPVFSSEA
MGKGIAIKPS GNTVYAPVDG TVQIAFDTGH AYGIKSDNGA EILIHIGIDT VSMEGKGFEQ
KVQADQKIKK GDVLGTFDSD KIAEAGLDNT TMFIVTNTAD YASVETLASS GTVAVGDSLL
EVKK
