PTLCB_LACCA
ID PTLCB_LACCA Reviewed; 577 AA.
AC P24400;
DT 01-MAR-1992, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-1992, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=PTS system lactose-specific EIICB component {ECO:0000303|PubMed:2125053};
DE AltName: Full=EIICB-Lac {ECO:0000303|PubMed:2125053};
DE Short=EII-Lac {ECO:0000303|PubMed:2125053};
DE Includes:
DE RecName: Full=PTS system lactose-specific EIIC component {ECO:0000303|PubMed:2125053};
DE AltName: Full=Lactose permease IIC component {ECO:0000303|PubMed:2125053};
DE Includes:
DE RecName: Full=PTS system lactose-specific EIIB component {ECO:0000303|PubMed:2125053};
DE EC=2.7.1.207 {ECO:0000269|PubMed:2125053};
DE AltName: Full=Lactose-specific phosphotransferase enzyme IIB component {ECO:0000303|PubMed:2125053};
GN Name=lacE {ECO:0000303|PubMed:2125053};
OS Lactobacillus casei.
OC Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC Lacticaseibacillus.
OX NCBI_TaxID=1582;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY,
RP MUTAGENESIS OF CYS-483, ACTIVE SITE, PHOSPHORYLATION AT CYS-483, AND
RP SUBCELLULAR LOCATION.
RX PubMed=2125053; DOI=10.1016/s0021-9258(18)45742-0;
RA Alpert C.-A., Chassy B.M.;
RT "Molecular cloning and DNA sequence of lacE, the gene encoding the lactose-
RT specific enzyme II of the phosphotransferase system of Lactobacillus casei.
RT Evidence that a cysteine residue is essential for sugar phosphorylation.";
RL J. Biol. Chem. 265:22561-22568(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:0000269|PubMed:2125053}.
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:2125053};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC ProRule:PRU00428, ECO:0000305|PubMed:2125053}; Multi-pass membrane
CC protein {ECO:0000255|PROSITE-ProRule:PRU00428}.
CC -!- INDUCTION: By lactose. The operon consists of lacABCDFEGX. A second
CC transcript of only lacF and lacE is also lactose-induced.
CC {ECO:0000250|UniProtKB:P23531}.
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; M60851; AAA72984.1; -; Genomic_DNA.
DR PIR; B23697; B23697.
DR AlphaFoldDB; P24400; -.
DR SMR; P24400; -.
DR STRING; 1582.AAW28_06690; -.
DR iPTMnet; P24400; -.
DR eggNOG; COG1440; Bacteria.
DR eggNOG; COG1455; Bacteria.
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:0046835; P:carbohydrate phosphorylation; IMP:CACAO.
DR GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR GO; GO:0016310; P:phosphorylation; IMP:CACAO.
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..577
FT /note="PTS system lactose-specific EIICB component"
FT /id="PRO_0000186583"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 63..83
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 100..120
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 176..196
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 219..239
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 280..300
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 326..346
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT TRANSMEM 386..406
FT /note="Helical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT DOMAIN 4..405
FT /note="PTS EIIC type-3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT DOMAIN 476..577
FT /note="PTS EIIB type-3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00423"
FT ACT_SITE 483
FT /note="Phosphocysteine intermediate; for EIIB activity"
FT /evidence="ECO:0000305|PubMed:2125053"
FT MOD_RES 483
FT /note="Phosphocysteine; by EIIA"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00423,
FT ECO:0000269|PubMed:2125053"
FT MUTAGEN 483
FT /note="C->H,S: Unable to be phosphorylated."
FT /evidence="ECO:0000269|PubMed:2125053"
SQ SEQUENCE 577 AA; 62392 MW; BE56852CAB0D76E4 CRC64;
MNKVFDKLKP VFEAIAANKY ISAIRDGFIA CMPIIIFSSI FMMVAYVPNA WGFYWPDNVT
NTLMVAYNYS MGLLALFVAG TTAKNLTDSK NLELPKTNQI NPVAVIVASE ISFVILSILP
LKTGVDLTYM GTQGLICAYI VGLIVPNIYY VCIKNNVTIK LPEQVPGNIA QSFKDLIPMG
LSVTAFWLFG VGFKAATGTV LPRWIIQVLS PLFQASDSYL GLALIAGAMA FFWFCGVQGP
SIVQPAVVPI MIANTAANLQ QYQAGQHVSH VLAMNTMDYV MNFGGTGATL VVPFIMLFAA
RSAQLKAVGK AAFVPCTFGV NEPVLFGMPI IMNPMLFIPF LATPIVNVCL FKFFVSVLGM
NSMMYTMPWT VPGPIGILIS TGFAPLAFVF VLLTLVLDVA IYFPFIRVYD STLLAEEKAK
EEVIEDDGMA VLASDTVSPS IPTGLTVATA TDDDATHVLP ETAPSAHGEA YFKQNEVDVL
VLCAGGGTSG ILANALNKLS KERGLKLSAA ARAYGQDMDL IKDMNMVILA PQMESMKGNL
KKITDKYGVK LVTTTGRQYI ELTNNGDMAL DFVESNL
