PUTP_SALTY
ID PUTP_SALTY Reviewed; 502 AA.
AC P10502;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1996, sequence version 3.
DT 03-AUG-2022, entry version 148.
DE RecName: Full=Sodium/proline symporter {ECO:0000305};
DE AltName: Full=Proline permease;
GN Name=putP {ECO:0000303|PubMed:6090414}; OrderedLocusNames=STM1125;
OS Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=99287;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=LT2;
RX PubMed=2190188; DOI=10.1093/nar/18.10.3057;
RA Miller K., Maloy S.;
RT "DNA sequence of the putP gene from Salmonella typhimurium and predicted
RT structure of proline permease.";
RL Nucleic Acids Res. 18:3057-3057(1990).
RN [2]
RP SEQUENCE REVISION.
RA Miller K.;
RL Submitted (NOV-1990) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX PubMed=11677609; DOI=10.1038/35101614;
RA McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA Wilson R.K.;
RT "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL Nature 413:852-856(2001).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15.
RX PubMed=2851701; DOI=10.1007/bf00333408;
RA Hahn D.R., Myers R.S., Kent C.R., Maloy S.R.;
RT "Regulation of proline utilization in Salmonella typhimurium: molecular
RT characterization of the put operon, and DNA sequence of the put control
RT region.";
RL Mol. Gen. Genet. 213:125-133(1988).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-15, AND INDUCTION.
RX PubMed=1987118; DOI=10.1128/jb.173.1.211-219.1991;
RA Ostrovsky de Spicer P., O'Brien K., Maloy S.;
RT "Regulation of proline utilization in Salmonella typhimurium: a membrane-
RT associated dehydrogenase binds DNA in vitro.";
RL J. Bacteriol. 173:211-219(1991).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=6090414; DOI=10.1128/jb.160.1.22-27.1984;
RA Cairney J., Higgins C.F., Booth I.R.;
RT "Proline uptake through the major transport system of Salmonella
RT typhimurium is coupled to sodium ions.";
RL J. Bacteriol. 160:22-27(1984).
CC -!- FUNCTION: Catalyzes the sodium-dependent uptake of extracellular L-
CC proline. {ECO:0000269|PubMed:6090414}.
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:0000269|PubMed:6090414};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.6 uM for proline (in the presence of 0.1 mM Na(+))
CC {ECO:0000269|PubMed:6090414};
CC KM=3.4 uM for proline (in the presence of 10 mM Na(+))
CC {ECO:0000269|PubMed:6090414};
CC Vmax=0.7 nmol/min/mg enzyme (in the presence of 0.1 mM Na(+))
CC {ECO:0000269|PubMed:6090414};
CC Vmax=4.6 nmol/min/mg enzyme (in the presence of 10 mM Na(+))
CC {ECO:0000269|PubMed:6090414};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P07117}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- INDUCTION: Expression may be repressed by PutA in the absence of
CC proline. {ECO:0000269|PubMed:1987118}.
CC -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21)
CC family. {ECO:0000305}.
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DR EMBL; X52573; CAA36802.1; -; Genomic_DNA.
DR EMBL; AE006468; AAL20056.1; -; Genomic_DNA.
DR EMBL; X12569; CAA31080.1; -; Genomic_DNA.
DR PIR; S10220; S10220.
DR RefSeq; NP_460097.1; NC_003197.2.
DR RefSeq; WP_001018467.1; NC_003197.2.
DR AlphaFoldDB; P10502; -.
DR SMR; P10502; -.
DR STRING; 99287.STM1125; -.
DR PaxDb; P10502; -.
DR EnsemblBacteria; AAL20056; AAL20056; STM1125.
DR GeneID; 1252643; -.
DR KEGG; stm:STM1125; -.
DR PATRIC; fig|99287.12.peg.1192; -.
DR HOGENOM; CLU_018808_15_2_6; -.
DR OMA; CWTDLIQ; -.
DR PhylomeDB; P10502; -.
DR BioCyc; SENT99287:STM1125-MON; -.
DR Proteomes; UP000001014; 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:0071235; P:cellular response to proline; IDA:UniProtKB.
DR GO; GO:0015824; P:proline transport; IDA:UniProtKB.
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 InterPro; IPR018212; Na/solute_symporter_CS.
DR Pfam; PF00474; SSF; 1.
DR TIGRFAMs; TIGR02121; Na_Pro_sym; 1.
DR TIGRFAMs; TIGR00813; sss; 1.
DR PROSITE; PS00456; NA_SOLUT_SYMP_1; 1.
DR PROSITE; PS00457; NA_SOLUT_SYMP_2; 1.
DR PROSITE; PS50283; NA_SOLUT_SYMP_3; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell inner membrane; Cell membrane; Ion transport;
KW Membrane; Reference proteome; Sodium; Sodium transport; Symport;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..502
FT /note="Sodium/proline symporter"
FT /id="PRO_0000105401"
FT TRANSMEM 6..26
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..62
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 127..147
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 163..183
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 192..212
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 235..255
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 320..340
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 371..391
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 398..418
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 430..450
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 452..472
FT /note="Helical"
FT /evidence="ECO:0000255"
FT SITE 344
FT /note="Involved in high-affinity binding for sodium and
FT proline"
FT /evidence="ECO:0000250"
SQ SEQUENCE 502 AA; 54318 MW; 0AAEF13602631F65 CRC64;
MAISTPMLVT FCVYIFGMIL IGFIAWRSTK NFDDYILGGR SLGPFVTALS AGASDMSGWL
LMGLPGAIFL SGISESWIAI GLTLGAWINW KLVAGRLRVH TEFNNNALTL PDYFTGRFED
KSRVLRIISA LVILLFFTIY CASGIVAGAR LFESTFGMSY ETALWAGAAA TIIYTFIGGF
LAVSWTDTVQ ASLMIFALIL TPVMVIVGVG GFSESLEVIK QKSIENVDML KGLNFVAIIS
LMGWGLGYFG QPHILARFMA ADSHHSIVHA RRISMTWMIL CLAGAVAVGF FGIAYFNNNP
ALAGAVNQNS ERVFIELAQI LFNPWIAGVL LSAILAAVMS TLSCQLLVCS SAITEDLYKA
FLRKSASQQE LVWVGRVMVL VVALIAIALA ANPDNRVLGL VSYAWAGFGA AFGPVVLFSV
MWSRMTRNGA LAGMIIGAVT VIVWKQYGWL DLYEIIPGFI FGSLGIVIFS LLGKAPTAAM
QERFAKADAH YHSAPPSKLQ AE
