PTLCB_LACLL
ID PTLCB_LACLL Reviewed; 568 AA.
AC P23531;
DT 01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1991, sequence version 1.
DT 03-AUG-2022, entry version 109.
DE RecName: Full=PTS system lactose-specific EIICB component {ECO:0000303|PubMed:2125052};
DE AltName: Full=EIICB-Lac {ECO:0000303|PubMed:2125052};
DE Short=EII-Lac {ECO:0000303|PubMed:2125052};
DE Includes:
DE RecName: Full=PTS system lactose-specific EIIC component {ECO:0000303|PubMed:2125052};
DE AltName: Full=Lactose permease IIC component {ECO:0000303|PubMed:2125052};
DE Includes:
DE RecName: Full=PTS system lactose-specific EIIB component {ECO:0000303|PubMed:2125052};
DE EC=2.7.1.207 {ECO:0000250|UniProtKB:P24400};
DE AltName: Full=Lactose-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:2125052};
GN Name=lacE {ECO:0000303|PubMed:2125052};
OS Lactococcus lactis subsp. lactis (Streptococcus lactis).
OG Plasmid pLP712.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC Lactococcus.
OX NCBI_TaxID=1360;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, OPERON STRUCTURE, INDUCTION,
RP AND SUBCELLULAR LOCATION.
RC STRAIN=MG1820;
RX PubMed=2125052; DOI=10.1016/s0021-9258(18)45741-9;
RA de Vos W.M., Boerrigter I.J., van Rooyen R.J., Reiche B., Hengstenberg W.;
RT "Characterization of the lactose-specific enzymes of the phosphotransferase
RT system in Lactococcus lactis.";
RL J. Biol. Chem. 265:22554-22560(1990).
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:0000305|PubMed:2125052}.
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:P24400};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00428}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC ProRule:PRU00428, ECO:0000305|PubMed:2125052}.
CC -!- INDUCTION: By lactose. The operon consists of lacABCDFEGX. A second
CC transcript of only lacF and lacE is also lactose-induced.
CC {ECO:0000269|PubMed:2125052}.
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 -!- MISCELLANEOUS: This gene was sequenced from pMG820, a laboratory-
CC derived deletion of the naturally occurring plasmid pLP712.
CC {ECO:0000269|PubMed:2125052}.
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DR EMBL; M60447; AAA25182.1; -; Genomic_DNA.
DR PIR; B23696; B23696.
DR AlphaFoldDB; P23531; -.
DR SMR; P23531; -.
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 InterPro; IPR001763; Rhodanese-like_dom.
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 2: Evidence at transcript level;
KW Cell membrane; Kinase; Membrane; Phosphoprotein; Phosphotransferase system;
KW Plasmid; Sugar transport; Transferase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..568
FT /note="PTS system lactose-specific EIICB component"
FT /id="PRO_0000186584"
FT TRANSMEM 30..50
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 62..82
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 103..123
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 128..148
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 183..203
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 222..242
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 339..359
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 389..409
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT DOMAIN 7..409
FT /note="PTS EIIC type-3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT DOMAIN 466..568
FT /note="PTS EIIB type-3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00423"
FT ACT_SITE 473
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000250|UniProtKB:P24400"
FT MOD_RES 473
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000250|UniProtKB:P24400,
FT ECO:0000255|PROSITE-ProRule:PRU00423"
SQ SEQUENCE 568 AA; 61563 MW; BE5ECA7736762446 CRC64;
MHKLIELIEK GKPFFEKISR NIYLRAIRDG FIAGMPVILF SSIFILIAYV PNAWGFHWSK
DIETFLMTPY SYSMGILAFF VGGTTAKALT DSKNRDLPAT NQINFLSTML ASMVGFLLMA
AEPAKEGGFL TAFMGTKGLL TAFIAAFVTV NVYKVCVKNN VTIRMPEDVP PNISQVFKDL
IPFTVSVVLL YGLELLVKGT LGVTVAESIG TLIAPLFSAA DGYLGITLIF GAYAFFWFVG
IHGPSIVEPA IAAITYANID VNLHLIQAGQ HADKVITSGT QMFIATMGGT GATLIVPFLF
MWICKSDRNR AIGRASVVPT FFGVNEPILF GAPIVLNPIF FVPFIFAPIV NVWIFKFFVD
TLNMNSFSAN LPWVTPGPLG IVLGTNFQVL SFILAGLLVV VDTIIYYPFV KVYDEQILEE
ERSGKTNDAL KEKVAANFNT AKADAVLGKA DVAKEDVAAN NNITKETNVL VLCAGGGTSG
LLANALNKAA AEYNVPVKAA AGGYGAHREM LPEFDLVILA PQVASNFDDM KAETDKLGIK
LVKTEGAQYI KLTRDGQGAL AFVQQQFD
