PUTP_STAA8
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 25-MAY-2022, entry version 96.
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; Firmicutes; 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};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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; 1280.SAXN108_2002; -.
DR EnsemblBacteria; ABD31169; ABD31169; SAOUHSC_02119.
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 PRO; PR:Q2FWY7; -.
DR Proteomes; UP000008816; 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: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; IEA:InterPro.
DR CDD; cd11475; SLC5sbd_PutP; 1.
DR Gene3D; 1.20.1730.10; -; 1.
DR InterPro; IPR038377; Na/Glc_symporter_sf.
DR InterPro; IPR011851; Na/Pro_symporter.
DR InterPro; IPR001734; Na/solute_symporter.
DR Pfam; PF00474; SSF; 1.
DR TIGRFAMs; TIGR02121; Na_Pro_sym; 1.
DR TIGRFAMs; TIGR00813; sss; 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
