PTLCB_STAAN
ID PTLCB_STAAN Reviewed; 570 AA.
AC Q99S77;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=PTS system lactose-specific EIICB component {ECO:0000250|UniProtKB:P11162};
DE AltName: Full=EIICB-Lac {ECO:0000250|UniProtKB:P11162};
DE Short=EII-Lac {ECO:0000250|UniProtKB:P11162};
DE Includes:
DE RecName: Full=PTS system lactose-specific EIIC component {ECO:0000250|UniProtKB:P11162};
DE AltName: Full=Lactose permease IIC component {ECO:0000250|UniProtKB:P11162};
DE Includes:
DE RecName: Full=PTS system lactose-specific EIIB component {ECO:0000250|UniProtKB:P11162};
DE EC=2.7.1.207 {ECO:0000250|UniProtKB:P11162};
DE AltName: Full=Lactose-specific phosphotransferase enzyme IIB component {ECO:0000250|UniProtKB:P11162};
GN Name=lacE {ECO:0000250|UniProtKB:P11162}; OrderedLocusNames=SA1992;
OS Staphylococcus aureus (strain N315).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=158879;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N315;
RX PubMed=11418146; DOI=10.1016/s0140-6736(00)04403-2;
RA Kuroda M., Ohta T., Uchiyama I., Baba T., Yuzawa H., Kobayashi I., Cui L.,
RA Oguchi A., Aoki K., Nagai Y., Lian J.-Q., Ito T., Kanamori M.,
RA Matsumaru H., Maruyama A., Murakami H., Hosoyama A., Mizutani-Ui Y.,
RA Takahashi N.K., Sawano T., Inoue R., Kaito C., Sekimizu K., Hirakawa H.,
RA Kuhara S., Goto S., Yabuzaki J., Kanehisa M., Yamashita A., Oshima K.,
RA Furuya K., Yoshino C., Shiba T., Hattori M., Ogasawara N., Hayashi H.,
RA Hiramatsu K.;
RT "Whole genome sequencing of meticillin-resistant Staphylococcus aureus.";
RL Lancet 357:1225-1240(2001).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=N315;
RA Vaezzadeh A.R., Deshusses J., Lescuyer P., Hochstrasser D.F.;
RT "Shotgun proteomic analysis of total and membrane protein extracts of S.
RT aureus strain N315.";
RL Submitted (OCT-2007) to UniProtKB.
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.
CC {ECO:0000250|UniProtKB:P11162}.
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:0000250|UniProtKB:P11162};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250|UniProtKB:P11162,
CC ECO:0000255|PROSITE-ProRule:PRU00428}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P11162, ECO:0000255|PROSITE-ProRule:PRU00428}.
CC -!- INDUCTION: Induced by lactose, galactose and galactose-6-P. Repressed
CC by glucose. {ECO:0000250|UniProtKB:P11162}.
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}.
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DR EMBL; BA000018; BAB43282.1; -; Genomic_DNA.
DR PIR; A90015; A90015.
DR AlphaFoldDB; Q99S77; -.
DR SMR; Q99S77; -.
DR EnsemblBacteria; BAB43282; BAB43282; BAB43282.
DR KEGG; sau:SA1992; -.
DR HOGENOM; CLU_029688_0_0_9; -.
DR OMA; ISAMPFM; -.
DR Proteomes; UP000000751; 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: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; Kinase; Membrane; Phosphoprotein; Phosphotransferase system;
KW Sugar transport; Transferase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..570
FT /note="PTS system lactose-specific EIICB component"
FT /id="PRO_0000186587"
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:0000250|UniProtKB:P11162"
FT MOD_RES 474
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000250|UniProtKB:P11162,
FT ECO:0000255|PROSITE-ProRule:PRU00423"
SQ SEQUENCE 570 AA; 62414 MW; 11B6FCC1B716028E CRC64;
MMQKLIAQIE KGKPFFEKLS RNIYLRAIRD GFISAMPVIL FSSIFLLIAY VPNIFGFKWD
KGMEAILMKP YNYTMGLVAF LVAGTTAKSL TDSFNRKLES TNQINFISTM LAAMCGFLFL
ASDPAKDGGF LSAFMGTKGL LTAFLSAFVT VIVYNFCVKR NITIKMPKEV PPNISQVFKD
LIPFSAVIII LYALDLVIRN SFKSNVAEGI LKLFEPLFTA ADGWIGVTII FGAFALFWFV
GIHGPSIVEP AIAAITYANI EANFKLLQAG EHADKIITSG TQMFIVTFGG TGATLVVPFM
FMWMTKSKRN KAIGRASVVP TFFGVNEPIL FGAPLVLNPV FFIPFVLAPI VNVWIFKLFV
EVLGINSFSV NLPWTTPGPL GIIMGTGFGL WSFVLAITLI VVDIIIYYPF LKVYDSEILD
EEEGRKESNS DLKEKVAANF DTKKADSILA ASGVSDDAAK ASNITEQTNV LVLCAGGGTS
GLLANALNKA AEEYHVPVKA AAGGYGAHMD IMKEYQLIIL APQVASNYED IKQDTDRLGI
KLAKTQGAEY IKLTRDGQAA LDFVQQQFEN
