PUTP_BACSU
ID PUTP_BACSU Reviewed; 473 AA.
AC P94392; Q797Q4;
DT 20-JAN-2009, integrated into UniProtKB/Swiss-Prot.
DT 24-MAR-2009, sequence version 3.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=High-affinity proline transporter PutP {ECO:0000303|PubMed:22139509};
GN Name=putP {ECO:0000303|PubMed:22139509}; Synonyms=ycgO;
GN OrderedLocusNames=BSU03220;
OS Bacillus subtilis (strain 168).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=224308;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=168;
RX PubMed=8969502; DOI=10.1099/13500872-142-11-3047;
RA Yamane K., Kumano M., Kurita K.;
RT "The 25 degrees-36 degrees region of the Bacillus subtilis chromosome:
RT determination of the sequence of a 146 kb segment and identification of 113
RT genes.";
RL Microbiology 142:3047-3056(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=168;
RX PubMed=9384377; DOI=10.1038/36786;
RA Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V.,
RA Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R.,
RA Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S.,
RA Bruschi C.V., Caldwell B., Capuano V., Carter N.M., Choi S.-K.,
RA Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F.,
RA Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D.,
RA Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M.,
RA Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P.,
RA Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K.,
RA Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S.,
RA Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y.,
RA Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G.,
RA Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J.,
RA Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C.,
RA Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S.,
RA Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B.,
RA Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S.,
RA Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M.,
RA Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y.,
RA Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J.,
RA Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A.,
RA Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M.,
RA Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S.,
RA Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E.,
RA Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K.,
RA Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E.,
RA Yoshikawa H., Danchin A.;
RT "The complete genome sequence of the Gram-positive bacterium Bacillus
RT subtilis.";
RL Nature 390:249-256(1997).
RN [3]
RP INDUCTION.
RX PubMed=21840319; DOI=10.1016/j.jmb.2011.08.003;
RA Belitsky B.R.;
RT "Indirect repression by Bacillus subtilis CodY via displacement of the
RT activator of the proline utilization operon.";
RL J. Mol. Biol. 413:321-336(2011).
RN [4]
RP INDUCTION.
RC STRAIN=168;
RX PubMed=21964733; DOI=10.1099/mic.0.054197-0;
RA Huang S.C., Lin T.H., Shaw G.C.;
RT "PrcR, a PucR-type transcriptional activator, is essential for proline
RT utilization and mediates proline-responsive expression of the proline
RT utilization operon putBCP in Bacillus subtilis.";
RL Microbiology 157:3370-3377(2011).
RN [5]
RP FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, INDUCTION, AND DISRUPTION
RP PHENOTYPE.
RC STRAIN=168 / JH642;
RX PubMed=22139509; DOI=10.1128/jb.06380-11;
RA Moses S., Sinner T., Zaprasis A., Stoeveken N., Hoffmann T., Belitsky B.R.,
RA Sonenshein A.L., Bremer E.;
RT "Proline utilization by Bacillus subtilis: uptake and catabolism.";
RL J. Bacteriol. 194:745-758(2012).
CC -!- FUNCTION: Catalyzes the high-affinity uptake of extracellular proline.
CC Important for the use of proline as a sole carbon and energy source or
CC a sole nitrogen source. {ECO:0000269|PubMed:22139509}.
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:0000305|PubMed:22139509};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=8 uM for proline {ECO:0000269|PubMed:22139509};
CC Vmax=29 nmol/min/mg enzyme {ECO:0000269|PubMed:22139509};
CC Vmax=28 nmol/min/mg enzyme (in the presence of 0.4 M NaCl)
CC {ECO:0000269|PubMed:22139509};
CC Vmax=158 nmol/min/mg enzyme (in the presence of 1 mM proline)
CC {ECO:0000269|PubMed:22139509};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000255}.
CC -!- INDUCTION: The expression of the putBCP operon is induced in a PutR-
CC dependent fashion by very low concentrations of L-proline in the growth
CC medium. CodY represses the operon by displacing PutR from DNA.
CC {ECO:0000269|PubMed:21840319, ECO:0000269|PubMed:21964733,
CC ECO:0000269|PubMed:22139509}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the putBCP operon abolishes L-proline
CC utilization. {ECO:0000269|PubMed:22139509}.
CC -!- SIMILARITY: Belongs to the sodium:solute symporter (SSF) (TC 2.A.21)
CC family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAA08956.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; D50453; BAA08956.1; ALT_INIT; Genomic_DNA.
DR EMBL; AL009126; CAB12116.2; -; Genomic_DNA.
DR PIR; B69759; B69759.
DR RefSeq; NP_388204.2; NC_000964.3.
DR RefSeq; WP_010886399.1; NC_000964.3.
DR AlphaFoldDB; P94392; -.
DR SMR; P94392; -.
DR STRING; 224308.BSU03220; -.
DR PaxDb; P94392; -.
DR PRIDE; P94392; -.
DR EnsemblBacteria; CAB12116; CAB12116; BSU_03220.
DR GeneID; 938330; -.
DR KEGG; bsu:BSU03220; -.
DR PATRIC; fig|224308.43.peg.330; -.
DR eggNOG; COG0591; Bacteria.
DR InParanoid; P94392; -.
DR OMA; CWTDLIQ; -.
DR PhylomeDB; P94392; -.
DR BioCyc; BSUB:BSU03220-MON; -.
DR SABIO-RK; P94392; -.
DR Proteomes; UP000001570; 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:0015193; F:L-proline transmembrane transporter activity; IMP:CACAO.
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 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 Cell membrane; Ion transport; Membrane; Reference proteome; Sodium;
KW Sodium transport; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..473
FT /note="High-affinity proline transporter PutP"
FT /id="PRO_0000360821"
FT TRANSMEM 32..52
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 56..76
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 146..166
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 218..238
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 256..276
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 299..319
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 376..396
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 408..428
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 431..451
FT /note="Helical"
FT /evidence="ECO:0000255"
SQ SEQUENCE 473 AA; 51144 MW; 71B3A7E237F2D937 CRC64;
MLLIGYFAYK RTSNLTDYML GGRSLGPAVT ALSAGAADMS GWLLMGLPGA MFSTGLSGAW
IVIGLCLGAW ANWLYVAPRL RTYTEKAGNS ITIPGFLENR FGDQTKLLRL FSGIVILVFF
TFYVSSGMVS GGVLFNSILG MDYHTGLWIV TGVVVAYTLF GGFLAVSWTD FVQGIIMFAA
LILVPIVTFF HTGGAGDTVA EIRSVDPDMF NIFKGTSVLG IISLFAWGLG YFGQPHIIVR
FMAITSVKEI KRARRIGMGW MILSAVGAVL TGLGGIAYYH QRGMTLKDPE TIFIQLGNIL
FHPIITGFLI SAILAAIMST ISSQLLVTSS SLVEDLYKSM FRRSASDKEL VFLGRLAVLA
VSIVALVLAW EKNNTILGLV SYAWAGFGAS FGPVVLLSLF WKRMTKWGAL AGMIVGAATV
IIWANAGLSD FLYEMIPGFA ASLLSVFFVS ILTQAPSQAV TDQFNDYQDT MSQ
