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Database: UniProt
Entry: E6MSK8_9BACT
LinkDB: E6MSK8_9BACT
Original site: E6MSK8_9BACT 
ID   E6MSK8_9BACT            Unreviewed;       458 AA.
AC   E6MSK8;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   27-MAR-2024, entry version 52.
DE   RecName: Full=L-lactate permease {ECO:0000256|RuleBase:RU365092};
GN   Name=lctP {ECO:0000313|EMBL:EFV03400.1};
GN   ORFNames=HMPREF9420_2476 {ECO:0000313|EMBL:EFV03400.1};
OS   Segatella salivae DSM 15606.
OC   Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Prevotellaceae;
OC   Segatella.
OX   NCBI_TaxID=888832 {ECO:0000313|EMBL:EFV03400.1, ECO:0000313|Proteomes:UP000003874};
RN   [1] {ECO:0000313|EMBL:EFV03400.1, ECO:0000313|Proteomes:UP000003874}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 15606 {ECO:0000313|EMBL:EFV03400.1,
RC   ECO:0000313|Proteomes:UP000003874};
RA   Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L.,
RA   Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V.,
RA   Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N., Okwuonu G.,
RA   Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W., Jakkamsetti A.,
RA   Pham P., Ruth R., San Lucas F., Warren J., Zhang J., Zhao Z., Zhou C.,
RA   Zhu D., Lee S., Bess C., Blankenburg K., Forbes L., Fu Q., Gubbala S.,
RA   Hirani K., Jayaseelan J.C., Lara F., Munidasa M., Palculict T., Patil S.,
RA   Pu L.-L., Saada N., Tang L., Weissenberger G., Zhu Y., Hemphill L.,
RA   Shang Y., Youmans B., Ayvaz T., Ross M., Santibanez J., Aqrawi P.,
RA   Gross S., Joshi V., Fowler G., Nazareth L., Reid J., Worley K.,
RA   Petrosino J., Highlander S., Gibbs R.;
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Uptake of L-lactate across the membrane. Can also transport
CC       D-lactate and glycolate. {ECO:0000256|RuleBase:RU365092}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU365092};
CC       Multi-pass membrane protein {ECO:0000256|RuleBase:RU365092}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the lactate permease family.
CC       {ECO:0000256|ARBA:ARBA00010100, ECO:0000256|RuleBase:RU365092}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU365092}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EFV03400.1}.
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DR   EMBL; AEQO01000191; EFV03400.1; -; Genomic_DNA.
DR   AlphaFoldDB; E6MSK8; -.
DR   STRING; 888832.HMPREF9420_2476; -.
DR   eggNOG; COG1620; Bacteria.
DR   HOGENOM; CLU_021628_0_0_10; -.
DR   Proteomes; UP000003874; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015129; F:lactate transmembrane transporter activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0022900; P:electron transport chain; IEA:InterPro.
DR   InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR   InterPro; IPR003804; Lactate_perm.
DR   PANTHER; PTHR30003:SF0; GLYCOLATE PERMEASE GLCA; 1.
DR   PANTHER; PTHR30003; L-LACTATE PERMEASE; 1.
DR   Pfam; PF02652; Lactate_perm; 1.
DR   PROSITE; PS50999; COX2_TM; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW   ECO:0000256|RuleBase:RU365092};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU365092};
KW   Reference proteome {ECO:0000313|Proteomes:UP000003874};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU365092};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU365092};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|RuleBase:RU365092}.
FT   TRANSMEM        6..23
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365092"
FT   TRANSMEM        60..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365092"
FT   TRANSMEM        127..146
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365092"
FT   TRANSMEM        158..179
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365092"
FT   TRANSMEM        185..203
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365092"
FT   TRANSMEM        224..246
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365092"
FT   TRANSMEM        270..293
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365092"
FT   TRANSMEM        305..323
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365092"
FT   TRANSMEM        329..348
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365092"
FT   TRANSMEM        439..457
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU365092"
FT   DOMAIN          1..29
FT                   /note="Cytochrome oxidase subunit II transmembrane region
FT                   profile"
FT                   /evidence="ECO:0000259|PROSITE:PS50999"
SQ   SEQUENCE   458 AA;  47983 MW;  A5398E83CC489128 CRC64;
     MLKAVFPILI IILMAIYSYN ILVESRQIEV IKRQFTAITS DKGILVLMLV WGFGGLLEGM
     AGFGTAVAIP AAILIGQGFK PMFSALVALI GNTVATGFGA VGVPVTTLCN EVALGGAAPV
     EAICETSSFA VIQLAPLFIL LPFIILTLTD RKAIVKNIIL SLWVGGISVV VQYLCAHFLG
     SETPAIIGSV AAILAILLYV KLFDRKGREG LPTARYSLGE TFKAWSVYLF ILLLILVSGA
     LCPPVNDFLK SHLVSKVAIP VIGSTFKFGW ISNAGLMLFL GATIGGLIQG LSFGRMMRIL
     ARTTVNLKNT IITIICLISL ASVMNYSGMI SAIASGLVAI TGGFYPFFAP LIGAVGTFVT
     GSDTSSNILF AKLQANVAGQ LGLTGYSTFY GVPGTETNWL VAANTTGATG GKMISPQSIA
     IATAACDMQG KDGEILRSAL PYAIGYIALG GLMVFLGL
//
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