PTLCB_STAAU
ID PTLCB_STAAU Reviewed; 570 AA.
AC P11162;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=PTS system lactose-specific EIICB component {ECO:0000303|PubMed:2824493};
DE AltName: Full=EIICB-Lac {ECO:0000303|PubMed:2824493};
DE Short=EII-Lac {ECO:0000303|PubMed:2824493};
DE Includes:
DE RecName: Full=PTS system lactose-specific EIIC component {ECO:0000303|PubMed:2824493};
DE AltName: Full=Lactose permease IIC component {ECO:0000303|PubMed:2824493};
DE Includes:
DE RecName: Full=PTS system lactose-specific EIIB component {ECO:0000303|PubMed:2824493};
DE EC=2.7.1.207 {ECO:0000269|PubMed:4684716, ECO:0000269|PubMed:7737179, ECO:0000305|PubMed:4567791};
DE AltName: Full=Lactose-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:2824493};
GN Name=lacE {ECO:0000303|PubMed:2824493};
OS Staphylococcus aureus.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=2824493; DOI=10.1016/s0021-9258(18)49276-9;
RA Breidt F. Jr., Hengstenberg W., Finkeldei U., Stewart G.C.;
RT "Identification of the genes for the lactose-specific components of the
RT phosphotransferase system in the lac operon of Staphylococcus aureus.";
RL J. Biol. Chem. 262:16444-16449(1987).
RN [2]
RP PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL
RP PROPERTIES, MUTAGENESIS OF CYS-474, PHOSPHORYLATION AT CYS-474, ACTIVE
RP SITE, AND SUBCELLULAR LOCATION.
RX PubMed=7737179; DOI=10.1111/j.1432-1033.1995.0798m.x;
RA Peters D., Frank R., Hengstenberg W.;
RT "Lactose-specific enzyme II of the phosphoenolpyruvate-dependent
RT phosphotransferase system of Staphylococcus aureus. Purification of the
RT histidine-tagged transmembrane component IICBLac and its hydrophilic IIB
RT domain by metal-affinity chromatography, and functional characterization.";
RL Eur. J. Biochem. 228:798-804(1995).
RN [3]
RP INDUCTION.
RX PubMed=14086091; DOI=10.1128/jb.86.6.1211-1215.1963;
RA McClatchy J.K., Rosenblum E.D.;
RT "Induction of lactose utilization in Staphylococcus aureus.";
RL J. Bacteriol. 86:1211-1215(1963).
RN [4]
RP INDUCTION.
RX PubMed=5665876; DOI=10.1016/0006-291x(68)90634-7;
RA Simoni R.D., Smith M.F., Roseman S.;
RT "Resolution of a staphylococcal phosphotransferase system into four protein
RT components and its relation to sugar transport.";
RL Biochem. Biophys. Res. Commun. 31:804-811(1968).
RN [5]
RP SUBCELLULAR LOCATION.
RX PubMed=11947593; DOI=10.1016/0014-5793(70)80286-1;
RA Hengstenberg W.;
RT "Solubilization of the membrane bound lactose specific component of the
RT staphylococcal PEP dependant phosphotransferase system.";
RL FEBS Lett. 8:277-280(1970).
RN [6]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=5156374; DOI=10.1111/j.1432-1033.1971.tb01621.x;
RA Korte T., Hengstenberg W.;
RT "Purification and characterization of the inducible lactose-specific
RT membrane-bound component of the staphylococcal phosphenolpyruvate-dependent
RT phosphotransferase system.";
RL Eur. J. Biochem. 23:295-302(1971).
RN [7]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBSTRATE SPECIFICITY.
RX PubMed=4567791; DOI=10.1016/s0021-9258(19)44355-x;
RA Simoni R.D., Nakazawa T., Hays J.B., Roseman S.;
RT "Sugar transport. IV. Isolation and characterization of the lactose
RT phosphotransferase system in Staphylococcus aureus.";
RL J. Biol. Chem. 248:932-940(1973).
RN [8]
RP FUNCTION, CATALYTIC ACTIVITY, AND REACTION MECHANISM.
RX PubMed=4684716; DOI=10.1016/s0021-9258(19)44357-3;
RA Simoni R.D., Hays J.B., Nakazawa T., Roseman S.;
RT "Sugar transport. VI. Phosphoryl transfer in the lactose phosphotransferase
RT system of Staphylococcus aureus.";
RL J. Biol. Chem. 248:957-965(1973).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=7053084; DOI=10.1111/j.1432-1033.1981.tb05065.x;
RA Schaefer A., Schrecker O., Hengstenberg W.;
RT "The staphylococcal phosphoenolpyruvate-dependent phosphotransferase
RT system. Purification and characterisation of the galactoside-specific
RT membrane-component enzyme II.";
RL Eur. J. Biochem. 113:289-294(1981).
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 LacEF PTS system is involved in lactose transport, but can
CC also use galactose, isopropyl beta-thio-galactopyranoside and
CC thiomethyl beta-D-galactopyranoside (TMG) as substrates.
CC {ECO:0000269|PubMed:4567791, ECO:0000269|PubMed:4684716,
CC ECO:0000269|PubMed:7737179, ECO:0000305|PubMed:2824493,
CC ECO:0000305|PubMed:5156374}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=lactose(out) + N(pros)-phospho-L-histidyl-[protein] = L-
CC histidyl-[protein] + lactose 6-phosphate(in); Xref=Rhea:RHEA:42400,
CC Rhea:RHEA-COMP:9745, Rhea:RHEA-COMP:9746, ChEBI:CHEBI:17716,
CC ChEBI:CHEBI:29979, ChEBI:CHEBI:64837, ChEBI:CHEBI:79080;
CC EC=2.7.1.207; Evidence={ECO:0000269|PubMed:4684716,
CC ECO:0000269|PubMed:7737179, ECO:0000305|PubMed:4567791};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.4 uM for o-nitrophenyl-beta-D-galactopyranoside (ONPG)
CC {ECO:0000269|PubMed:7737179};
CC Vmax=30 nmol/min/mg enzyme with o-nitrophenyl-beta-D-
CC galactopyranoside (ONPG) as substrate {ECO:0000269|PubMed:7737179};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00428, ECO:0000269|PubMed:11947593,
CC ECO:0000269|PubMed:5156374, ECO:0000269|PubMed:7737179}; Multi-pass
CC membrane protein {ECO:0000255|PROSITE-ProRule:PRU00428,
CC ECO:0000305|PubMed:2824493, ECO:0000305|PubMed:7053084}.
CC -!- INDUCTION: Induced by lactose, galactose and galactose-6-P. Repressed
CC by glucose. {ECO:0000269|PubMed:14086091, ECO:0000269|PubMed:5665876}.
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}.
CC -!- DOMAIN: The PTS EIIB type-3 domain is phosphorylated by phospho-EIIA on
CC a cysteinyl residue. Then, it transfers the phosphoryl group to the
CC sugar substrate concomitantly with the sugar uptake processed by the
CC PTS EIIC type-3 domain. {ECO:0000255|PROSITE-ProRule:PRU00423}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA26649.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; J03479; AAA26649.1; ALT_INIT; Genomic_DNA.
DR PIR; B28474; B28474.
DR AlphaFoldDB; P11162; -.
DR SMR; P11162; -.
DR TCDB; 4.A.3.1.1; the pts lactose-n,n'-diacetylchitobiose-Beta-glucoside (lac) family.
DR iPTMnet; P11162; -.
DR SABIO-RK; P11162; -.
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:0022869; F:protein-N(PI)-phosphohistidine-lactose phosphotransferase system transporter 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; cd05565; PTS_IIB_lactose; 1.
DR InterPro; IPR004801; LacE.
DR InterPro; IPR036095; PTS_EIIB-like_sf.
DR InterPro; IPR003501; PTS_EIIB_2/3.
DR InterPro; IPR013012; PTS_EIIB_3.
DR InterPro; IPR003352; PTS_EIIC.
DR InterPro; IPR004501; PTS_EIIC_3.
DR InterPro; IPR041713; PTS_IIB.
DR Pfam; PF02378; PTS_EIIC; 1.
DR Pfam; PF02302; PTS_IIB; 1.
DR SUPFAM; SSF52794; SSF52794; 1.
DR TIGRFAMs; TIGR00394; lac_pts_IIC; 1.
DR TIGRFAMs; TIGR00410; lacE; 1.
DR TIGRFAMs; TIGR00853; pts-lac; 1.
DR PROSITE; PS51100; PTS_EIIB_TYPE_3; 1.
DR PROSITE; PS51105; PTS_EIIC_TYPE_3; 1.
PE 1: Evidence at protein level;
KW Cell membrane; Direct protein sequencing; Kinase; Membrane; Phosphoprotein;
KW Phosphotransferase system; Sugar transport; Transferase; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..570
FT /note="PTS system lactose-specific EIICB component"
FT /id="PRO_0000186591"
FT TRANSMEM 31..51
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 65..85
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 133..153
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 223..243
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 283..303
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT DOMAIN 9..410
FT /note="PTS EIIC type-3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT DOMAIN 467..570
FT /note="PTS EIIB type-3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00423"
FT ACT_SITE 474
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000305|PubMed:7737179"
FT MOD_RES 474
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00423,
FT ECO:0000269|PubMed:7737179"
FT MUTAGEN 474
FT /note="C->S: Unable to be phosphorylated."
FT /evidence="ECO:0000269|PubMed:7737179"
SQ SEQUENCE 570 AA; 62447 MW; 50E7D5EB8A444E91 CRC64;
MMQKLIAQIE KGKPFFEKLS RNIYLRAIRD GFISAMPVIL FSSIFLLIAY VPNIFGFKWD
KGMEAILMKP YNYTMGLVAF LVAGTTAKSL TDSFNRKLES TNQINFISTM QAAMCGFLFL
ASDPAKDGGF LSAFMGTKGL LTAFLSAFVT VIVYNFCVKR NITIKMPKEV PPNISQVFKD
LIPFSAVIII LYALDLVIRN SFKSNVAEGI LKLFEPLFTA ADGWIGVTII FGAFALFWFV
GIHGPSIVEP AIAAITYANI EANFKLLQAG EHADKIITSG TQMFIVTFGG TGATLVVPFM
FMWMTKSKRN KAIGRASVVP TFFGVNEPIL FGAPLVLNPV FFIPFVLAPI VNVWIFKLFV
EVLGMNSFSV NLPWTTPGPL GIIMGTGFGL WSFVLAITLI VVDIIIYYPF LKVYDSEILD
EEEGRKESNS DLKEKVAANF DTKKADSILA ASGVSDDAAK ASNITEQTNV LVLCAGGGTS
GLLANALNKA AEEYHVPVKA AAGGYGAHMD IMKEYQLIIL APQVASNYED IKQDTDRLGI
KLAKTQGAEY IKLTRDGQAA LDFVQQQFEN
