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Database: UniProt
Entry: Q2FWY7
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Original site: Q2FWY7 
ID   PUTP_STAA8              Reviewed;         512 AA.
AC   Q2FWY7; O30986;
DT   10-FEB-2009, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2006, sequence version 1.
DT   24-JAN-2024, entry version 102.
DE   RecName: Full=Sodium/proline symporter;
DE   AltName: Full=Proline permease {ECO:0000303|PubMed:9453610};
GN   Name=putP {ECO:0000303|PubMed:9453610}; OrderedLocusNames=SAOUHSC_02119;
OS   Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC   Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC   Staphylococcus.
OX   NCBI_TaxID=93061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE, AND FUNCTION IN
RP   PROLINE UPTAKE.
RX   PubMed=9453610; DOI=10.1128/iai.66.2.567-572.1998;
RA   Schwan W.R., Coulter S.N., Ng E.Y.W., Langhorne M.H., Ritchie H.D.,
RA   Brody L.L., Westbrock-Wadman S., Bayer A.S., Folger K.R., Stover C.K.;
RT   "Identification and characterization of the putP proline permease that
RT   contributes to in vivo survival of Staphylococcus aureus in animal
RT   models.";
RL   Infect. Immun. 66:567-572(1998).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC 8325 / PS 47;
RA   Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT   "The Staphylococcus aureus NCTC 8325 genome.";
RL   (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL   Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington
RL   D.C. (2006).
RN   [3]
RP   DISRUPTION PHENOTYPE.
RX   PubMed=9916085; DOI=10.1128/iai.67.2.740-744.1999;
RA   Bayer A.S., Coulter S.N., Stover C.K., Schwan W.R.;
RT   "Impact of the high-affinity proline permease gene (putP) on the virulence
RT   of Staphylococcus aureus in experimental endocarditis.";
RL   Infect. Immun. 67:740-744(1999).
RN   [4]
RP   INDUCTION BY NACL AND L-PROLINE.
RX   PubMed=16368996; DOI=10.1128/iai.74.1.399-409.2006;
RA   Schwan W.R., Lehmann L., McCormick J.;
RT   "Transcriptional activation of the Staphylococcus aureus putP gene by low-
RT   proline-high osmotic conditions and during infection of murine and human
RT   tissues.";
RL   Infect. Immun. 74:399-409(2006).
CC   -!- FUNCTION: Catalyzes the sodium-dependent uptake of extracellular L-
CC       proline (By similarity). Since most S.aureus strains are L-proline
CC       auxotrophs, this transporter may aid the bacterial persistence during
CC       an infection of tissues with low proline concentrations
CC       (PubMed:9453610). {ECO:0000250|UniProtKB:P07117,
CC       ECO:0000269|PubMed:9453610}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=L-proline(in) + Na(+)(in) = L-proline(out) + Na(+)(out);
CC         Xref=Rhea:RHEA:28967, ChEBI:CHEBI:29101, ChEBI:CHEBI:60039;
CC         Evidence={ECO:0000250|UniProtKB:P07117};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000255}.
CC   -!- INDUCTION: Up-regulated by high osmotic environment, such as increasing
CC       concentrations of NaCl, and low L-proline concentrations.
CC       {ECO:0000269|PubMed:16368996}.
CC   -!- DISRUPTION PHENOTYPE: Cells lacking this gene display an approximate
CC       33% overall decline in L-proline uptake and exhibit significantly
CC       reduced virulence in several animal models, thus showing a negative
CC       impact on the ability of this pathogen to survive in vivo.
CC       {ECO:0000269|PubMed:9453610, ECO:0000269|PubMed:9916085}.
CC   -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21)
CC       family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAC38087.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; AF024571; AAC38087.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; CP000253; ABD31169.1; -; Genomic_DNA.
DR   PIR; T48676; T48676.
DR   RefSeq; WP_000957020.1; NZ_LS483365.1.
DR   RefSeq; YP_500611.1; NC_007795.1.
DR   AlphaFoldDB; Q2FWY7; -.
DR   SMR; Q2FWY7; -.
DR   STRING; 93061.SAOUHSC_02119; -.
DR   PaxDb; 1280-SAXN108_2002; -.
DR   GeneID; 3921191; -.
DR   KEGG; sao:SAOUHSC_02119; -.
DR   PATRIC; fig|93061.5.peg.1923; -.
DR   eggNOG; COG0591; Bacteria.
DR   HOGENOM; CLU_018808_15_2_9; -.
DR   OMA; CWTDLIQ; -.
DR   OrthoDB; 9810181at2; -.
DR   PRO; PR:Q2FWY7; -.
DR   Proteomes; UP000008816; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015193; F:L-proline transmembrane transporter activity; IBA:GO_Central.
DR   GO; GO:0005298; F:proline:sodium symporter activity; IBA:GO_Central.
DR   GO; GO:0031402; F:sodium ion binding; IEA:InterPro.
DR   GO; GO:0015824; P:proline transport; IBA:GO_Central.
DR   GO; GO:0055085; P:transmembrane transport; IBA:GO_Central.
DR   CDD; cd11475; SLC5sbd_PutP; 1.
DR   Gene3D; 1.20.1730.10; Sodium/glucose cotransporter; 1.
DR   InterPro; IPR038377; Na/Glc_symporter_sf.
DR   InterPro; IPR011851; Na/Pro_symporter.
DR   InterPro; IPR001734; Na/solute_symporter.
DR   NCBIfam; TIGR02121; Na_Pro_sym; 1.
DR   NCBIfam; TIGR00813; sss; 1.
DR   PANTHER; PTHR48086:SF3; SODIUM/PROLINE SYMPORTER; 1.
DR   PANTHER; PTHR48086; SODIUM/PROLINE SYMPORTER-RELATED; 1.
DR   Pfam; PF00474; SSF; 1.
DR   PROSITE; PS50283; NA_SOLUT_SYMP_3; 1.
PE   1: Evidence at protein level;
KW   Amino-acid transport; Cell membrane; Ion transport; Membrane;
KW   Reference proteome; Sodium; Sodium transport; Symport; Transmembrane;
KW   Transmembrane helix; Transport.
FT   CHAIN           1..512
FT                   /note="Sodium/proline symporter"
FT                   /id="PRO_0000364102"
FT   TRANSMEM        16..36
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        54..74
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        85..105
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        139..159
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        174..194
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        200..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        240..260
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        286..306
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        327..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        381..401
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        410..430
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        438..458
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        467..487
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   CONFLICT        30..36
FT                   /note="IVIGFYG -> MLLAFT (in Ref. 1; AAC38087)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        146
FT                   /note="V -> I (in Ref. 1; AAC38087)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   512 AA;  55976 MW;  C0B4AC52311A96DD CRC64;
     MLTMGTALSQ QVDANWQTYI MIAVYFLILI VIGFYGYKQA TGNLSEYMLG GRSIGPYITA
     LSAGASDMSG WMIMGLPGSV YSTGLSAMWI TIGLTLGAYI NYFVVAPRLR VYTELAGDAI
     TLPDFFKNRL NDKNNVLKII SGLIIVVFFT LYTHSGFVSG GKLFESAFGL DYHFGLILVA
     FIVIFYTFFG GYLAVSITDF FQGVIMLIAM VMVPIVAMMN LNGWGTFHDV AAMKPTNLNL
     FKGLSFIGII SLFSWGLGYF GQPHIIVRFM SIKSHKMLPK ARRLGISWMA VGLLGAVAVG
     LTGIAFVPAY HIKLEDPETL FIVMSQVLFH PLVGGFLLAA ILAAIMSTIS SQLLVTSSSL
     TEDFYKLIRG EEKAKTHQKE FVMIGRLSVL VVAIVAIAIA WNPNDTILNL VGNAWAGFGA
     SFSPLVLFAL YWKGLTRAGA VSGMVSGALV VIVWIAWIKP LAHINEIFGL YEIIPGFIVS
     VIVTYVVSKL TKKPGAFVET DLNKVRDIVR EK
//
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