ID   PANT_LACLM              Reviewed;         196 AA.
AC   A2RIQ0;
DT   31-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   06-MAR-2007, sequence version 1.
DT   03-AUG-2022, entry version 57.
DE   RecName: Full=Pantothenic acid transporter PanT;
DE   AltName: Full=Pantothenic acid ECF transporter S component PanT;
GN   Name=panT; OrderedLocusNames=llmg_0542;
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   SUBUNIT, SUBCELLULAR LOCATION, EXPRESSION IN E.COLI, AND FUNCTION.
RC   STRAIN=MG1363;
RX   PubMed=21135102; DOI=10.1074/jbc.m110.199224;
RA   ter Beek J., Duurkens R.H., Erkens G.B., Slotboom D.J.;
RT   "Quaternary structure and functional unit of energy coupling factor (ECF)-
RT   type transporters.";
RL   J. Biol. Chem. 286:5471-5475(2011).
CC   -!- FUNCTION: Probably a pantothenic acid-binding protein that interacts
CC       with the energy-coupling factor (ECF) ABC-transporter complex. Unlike
CC       classic ABC transporters this ECF transporter provides the energy
CC       necessary to transport a number of different substrates. The substrates
CC       themselves are bound by transmembrane, not extracytoplasmic soluble
CC       proteins. {ECO:0000269|PubMed:21135102}.
CC   -!- SUBUNIT: In E.coli forms a stable energy-coupling factor (ECF)
CC       transporter complex composed of 2 membrane-embedded substrate-binding
CC       protein (S component), 2 ATP-binding proteins (A and A' components) and
CC       2 transmembrane proteins (T component), probably with a stoichiometry
CC       of 2:1:1:2. May be able to interact with more than 1 S component at a
CC       time. {ECO:0000269|PubMed:21135102}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305|PubMed:21135102};
CC       Multi-pass membrane protein {ECO:0000305|PubMed:21135102}.
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DR   EMBL; AM406671; CAL97145.1; -; Genomic_DNA.
DR   RefSeq; WP_011834573.1; NZ_WJVF01000027.1.
DR   AlphaFoldDB; A2RIQ0; -.
DR   SMR; A2RIQ0; -.
DR   STRING; 416870.llmg_0542; -.
DR   EnsemblBacteria; CAL97145; CAL97145; llmg_0542.
DR   KEGG; llm:llmg_0542; -.
DR   eggNOG; COG4684; Bacteria.
DR   HOGENOM; CLU_088550_3_0_9; -.
DR   OMA; SIMYGPR; -.
DR   PhylomeDB; A2RIQ0; -.
DR   BioCyc; LLAC416870:LLMG_RS02835-MON; -.
DR   Proteomes; UP000000364; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   InterPro; IPR024529; ECF_trnsprt_substrate-spec.
DR   Pfam; PF12822; ECF_trnsprt; 1.
PE   1: Evidence at protein level;
KW   Cell membrane; Membrane; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..196
FT                   /note="Pantothenic acid transporter PanT"
FT                   /id="PRO_0000409012"
FT   TRANSMEM        10..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        58..78
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        99..119
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        131..151
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        161..181
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   196 AA;  21128 MW;  C260D9F3D16C2EAD CRC64;
     MKKSKASDVA ILAIFIAIMV VVQLFTQFVI NVWPFPVKPT LLHLPVIIGS IILGWRKGAF
     LGLVWGLISF VTATIVTTPT SFLFSPFQPV IGTHHGSPWG LFIAFIPRIL VGILPYFVYK
     IANNRLGAGL AAFAGTATNT VLVLTSIFLF FGSTLKWSLS YLLGAIVATN SLTEVIIAVI
     LTTAIVPALT KARNNS