ID   GPIIC_LACLM             Reviewed;         451 AA.
AC   A2RJV0;
DT   08-MAY-2019, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 80.
DE   RecName: Full=PTS system galactose-specific EIIC component {ECO:0000305};
GN   OrderedLocusNames=llmg_0963 {ECO:0000312|EMBL:CAL97555.1};
OS   Lactococcus lactis subsp. cremoris (strain MG1363).
OC   Bacteria; Firmicutes; Bacilli; Lactobacillales; Streptococcaceae;
OC   Lactococcus; Lactococcus cremoris subsp. cremoris.
OX   NCBI_TaxID=416870;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MG1363;
RX   PubMed=17307855; DOI=10.1128/jb.01768-06;
RA   Wegmann U., O'Connell-Motherway M., Zomer A., Buist G., Shearman C.,
RA   Canchaya C., Ventura M., Goesmann A., Gasson M.J., Kuipers O.P.,
RA   van Sinderen D., Kok J.;
RT   "The complete genome sequence of the lactic acid bacterial paradigm
RT   Lactococcus lactis subsp. cremoris MG1363.";
RL   J. Bacteriol. 189:3256-3270(2007).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=MG1363;
RX   PubMed=30123211; DOI=10.3389/fmicb.2018.01803;
RA   Solopova A., Bachmann H., Teusink B., Kok J., Kuipers O.P.;
RT   "Further elucidation of galactose utilization in Lactococcus lactis
RT   MG1363.";
RL   Front. Microbiol. 9:1803-1803(2018).
CC   -!- FUNCTION: The phosphoenolpyruvate-dependent sugar phosphotransferase
CC       system (PTS), a major carbohydrate active transport system, catalyzes
CC       the phosphorylation of incoming sugar substrates concomitant with their
CC       translocation across the cell membrane (By similarity). Involved in
CC       galactose transport with PtcA and PtcB (PubMed:30123211).
CC       {ECO:0000250|UniProtKB:P17334, ECO:0000269|PubMed:30123211}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|PROSITE-
CC       ProRule:PRU00428}; Multi-pass membrane protein {ECO:0000255|PROSITE-
CC       ProRule:PRU00428}.
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   -!- DISRUPTION PHENOTYPE: The galP/llmg_0963 double mutant grows poorly on
CC       galactose. {ECO:0000269|PubMed:30123211}.
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DR   EMBL; AM406671; CAL97555.1; -; Genomic_DNA.
DR   RefSeq; WP_011834904.1; NZ_WJVF01000006.1.
DR   AlphaFoldDB; A2RJV0; -.
DR   SMR; A2RJV0; -.
DR   STRING; 416870.llmg_0963; -.
DR   EnsemblBacteria; CAL97555; CAL97555; llmg_0963.
DR   KEGG; llm:llmg_0963; -.
DR   eggNOG; COG1455; Bacteria.
DR   HOGENOM; CLU_029688_1_0_9; -.
DR   OMA; FECINQL; -.
DR   PhylomeDB; A2RJV0; -.
DR   BioCyc; LLAC416870:LLMG_RS04900-MON; -.
DR   Proteomes; UP000000364; 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:0008982; F:protein-N(PI)-phosphohistidine-sugar phosphotransferase activity; IEA:InterPro.
DR   GO; GO:0009401; P:phosphoenolpyruvate-dependent sugar phosphotransferase system; IEA:UniProtKB-KW.
DR   InterPro; IPR003352; PTS_EIIC.
DR   InterPro; IPR004501; PTS_EIIC_3.
DR   InterPro; IPR004796; PTS_IIC_cello.
DR   Pfam; PF02378; PTS_EIIC; 1.
DR   PIRSF; PIRSF006351; PTS_EIIC-Cellobiose; 1.
DR   TIGRFAMs; TIGR00410; lacE; 1.
DR   PROSITE; PS51105; PTS_EIIC_TYPE_3; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Membrane; Phosphotransferase system; Sugar transport;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..451
FT                   /note="PTS system galactose-specific EIIC component"
FT                   /id="PRO_0000446880"
FT   TRANSMEM        40..60
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT   TRANSMEM        69..89
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        151..171
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT   TRANSMEM        190..210
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT   TRANSMEM        239..259
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT   TRANSMEM        263..283
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT   TRANSMEM        296..316
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT   TRANSMEM        332..352
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT   TRANSMEM        356..376
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT   TRANSMEM        403..423
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
FT   DOMAIN          8..427
FT                   /note="PTS EIIC type-3"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00428"
SQ   SEQUENCE   451 AA;  49298 MW;  1DC0D91A44CF6173 CRC64;
     MDKFEKWLNK TLMPLASKMN KNHFISALSE AFMRCMPLTL GIALLTIIGY FPVPAWVDFL
     NSIGLAQHFS AVIGAVTSAL AIYVTYNFAY SYVNRHEYNG HTAGLLSIAS LLMLMPQIIT
     VPVVKNIPTE FPKSAVVDSV SNVEAFQTVY TGSTGLIVAI IIGFIVSLVY IQLSKRNLVI
     KLPAGVPPMV VDSLSPAIIS MVIFCLMFGI RVGFSYTPFH DIFNFSTQLI QAPLTGAVAN
     PWVLMGIFTF GNFLWFFGIH PNLIGGILNP LLLTMSYANI DAYAAGKPVP YLQMMIVFAV
     GANAWGGSGN TYGLVISMFT AKSERYKQLL KLGAIPSIFN ISEPLLFGLP MMLNPLFFIP
     LVFQPAILGT VALGLAKILY ITNLNPMTAL LPWTTPAPVR MAISGGLPFL IIFAICLVLN
     VLIYYPFFKV AYNKALEEEK AAVELEGSET A