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LACY_LACHE
ID   LACY_LACHE              Reviewed;         638 AA.
AC   Q7WTB2;
DT   16-AUG-2004, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2003, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Lactose permease;
DE   AltName: Full=Lactose transport protein;
DE   AltName: Full=Lactose transporter;
DE   AltName: Full=Lactose-proton symporter;
DE   Includes:
DE     RecName: Full=Putative phosphotransferase enzyme IIA component;
DE              EC=2.7.1.-;
DE     AltName: Full=Putative PTS system EIIA component;
GN   Name=lacS;
OS   Lactobacillus helveticus (Lactobacillus suntoryeus).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lactobacillus.
OX   NCBI_TaxID=1587;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND TRANSCRIPTIONAL REGULATION.
RC   STRAIN=ATCC 15009 / DSM 20075 / BCRC 12936 / JCM 1120 / NBRC 15019 / NCIMB
RC   11971 / NRRL B-4526 / Lh12;
RX   PubMed=12788721; DOI=10.1128/aem.69.6.3238-3243.2003;
RA   Fortina M.G., Ricci G., Mora D., Guglielmetti S., Manachini P.L.;
RT   "Unusual organization for lactose and galactose gene clusters in
RT   Lactobacillus helveticus.";
RL   Appl. Environ. Microbiol. 69:3238-3243(2003).
CC   -!- FUNCTION: Responsible for transport of beta-galactosides into the cell,
CC       with the concomitant uptake of protons (symport system), and also for
CC       transport of homologous and heterologous exchange of beta-galactosides.
CC       {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- INDUCTION: By lactose. {ECO:0000269|PubMed:12788721}.
CC   -!- DOMAIN: The PTS EIIA type-1 domain may serve a regulatory function,
CC       through its phosphorylation activity. {ECO:0000250}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       sodium:galactoside symporter (TC 2.A.2) family. {ECO:0000305}.
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DR   EMBL; AJ512878; CAD55501.1; -; Genomic_DNA.
DR   RefSeq; WP_003627050.1; NZ_SCLV01000034.1.
DR   AlphaFoldDB; Q7WTB2; -.
DR   SMR; Q7WTB2; -.
DR   STRING; 326425.lhe_1439; -.
DR   GeneID; 66452191; -.
DR   eggNOG; COG2190; Bacteria.
DR   eggNOG; COG2211; 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:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:InterPro.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0006814; P:sodium ion transport; IEA:InterPro.
DR   Gene3D; 1.20.1250.20; -; 1.
DR   Gene3D; 2.70.70.10; -; 1.
DR   InterPro; IPR011055; Dup_hybrid_motif.
DR   InterPro; IPR039672; MFS_2.
DR   InterPro; IPR036259; MFS_trans_sf.
DR   InterPro; IPR001927; Na/Gal_symport.
DR   InterPro; IPR018043; Na/Gal_symport_CS.
DR   InterPro; IPR001127; PTS_EIIA_1_perm.
DR   PANTHER; PTHR11328; PTHR11328; 1.
DR   Pfam; PF00358; PTS_EIIA_1; 1.
DR   SUPFAM; SSF103473; SSF103473; 1.
DR   SUPFAM; SSF51261; SSF51261; 1.
DR   TIGRFAMs; TIGR00792; gph; 1.
DR   TIGRFAMs; TIGR00830; PTBA; 1.
DR   PROSITE; PS00872; NA_GALACTOSIDE_SYMP; 1.
DR   PROSITE; PS51093; PTS_EIIA_TYPE_1; 1.
DR   PROSITE; PS00371; PTS_EIIA_TYPE_1_HIS; 1.
PE   2: Evidence at transcript level;
KW   Cell membrane; Kinase; Membrane; Phosphoprotein; Sugar transport; Symport;
KW   Transferase; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..638
FT                   /note="Lactose permease"
FT                   /id="PRO_0000170758"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        56..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        94..114
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        121..141
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        166..186
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        261..281
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        291..311
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        320..340
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        343..363
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        395..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        429..449
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          503..610
FT                   /note="PTS EIIA type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00416"
FT   REGION          1..470
FT                   /note="Permease"
FT   MOD_RES         558
FT                   /note="Phosphohistidine; by HPr"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   638 AA;  69669 MW;  7B00C98B7D8893D0 CRC64;
     MHNHKVSGKQ IVSYASFCLG NLGHSAFYGV MSTYFIIFIT SGMFSGLNQS VADKLIGLIT
     GLMVLVRIIE LVIDPILGNV VDNTKTRWGK FKPWILIGTV VSAALLLILF TGIFGLAQQN
     WILFAILFVL IYIAFDVFYS LSDVSYWGMV PALSEDSHER GIYTSLGAFS GIIGWNSLPI
     IVVPLVTGVT YAVTGKHEEG APGWFAFAAV ISALAIICAL IVCFGTKEKH NIIRDSAKQK
     TTLRQVFGAI FHNDQILWPS LAYLLYSLAA VITNGVLFYM YKFVIGKPND FWVVGIIATI
     IGCCINPSFP VLNKYIPRKW LFIAGQTCMV LAYVLFIFGH NNVFLMDLGL VLFNINFALL
     VTVLTLTDAI EYGQLKIGQR NEAVVLAVRP MIDKFAGAVS NALVGYVAIA AGMTGSATAA
     DMTSKGINTF NMMALYIPLA LAVLSIVVFS LKVTLSEKKH AQVIEELKSK LAQGEIEKKT
     SVDTGTKEVT IYAPADGELM QMSSVVDEDG KPFPGKGFAI EPSSGQIYAP FDGTIKFTFG
     TKHAFEIVSQ NGLQVVVHVG LGTVNLRGEG FETFYDDGQT VKKGDKLLEF DRDLALNNGY
     KDTIVIFYTQ PGRIQNSGTI QAGKDIKHGE KVVDVQFK
 
 
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