PUUP_ECOLI
ID PUUP_ECOLI Reviewed; 461 AA.
AC P76037; P77557;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 15-DEC-1998, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=Putrescine importer PuuP {ECO:0000303|PubMed:19181795};
GN Name=puuP {ECO:0000303|PubMed:15590624}; Synonyms=ycjJ;
GN OrderedLocusNames=b1296, JW1289;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP FUNCTION AS A PUTRESCINE IMPORTER, AND NOMENCLATURE.
RC STRAIN=K12;
RX PubMed=15590624; DOI=10.1074/jbc.m411114200;
RA Kurihara S., Oda S., Kato K., Kim H.G., Koyanagi T., Kumagai H., Suzuki H.;
RT "A novel putrescine utilization pathway involves gamma-glutamylated
RT intermediates of Escherichia coli K-12.";
RL J. Biol. Chem. 280:4602-4608(2005).
RN [5]
RP FUNCTION IN PUTRESCINE DEGRADATION AND AS A PUTRESCINE IMPORTER,
RP MUTAGENESIS OF TYR-110, INDUCTION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=K12;
RX PubMed=19181795; DOI=10.1128/jb.01314-08;
RA Kurihara S., Tsuboi Y., Oda S., Kim H.G., Kumagai H., Suzuki H.;
RT "The putrescine importer PuuP of Escherichia coli K-12.";
RL J. Bacteriol. 191:2776-2782(2009).
RN [6]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP INDUCTION.
RX PubMed=23719730; DOI=10.1007/s00726-013-1517-x;
RA Terui Y., Saroj S.D., Sakamoto A., Yoshida T., Higashi K., Kurihara S.,
RA Suzuki H., Toida T., Kashiwagi K., Igarashi K.;
RT "Properties of putrescine uptake by PotFGHI and PuuP and their
RT physiological significance in Escherichia coli.";
RL Amino Acids 46:661-670(2014).
RN [7]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / BW25113, and K12 / MG1655 / ATCC 47076;
RX PubMed=27803167; DOI=10.1074/jbc.m116.762450;
RA Sugiyama Y., Nakamura A., Matsumoto M., Kanbe A., Sakanaka M., Higashi K.,
RA Igarashi K., Katayama T., Suzuki H., Kurihara S.;
RT "A novel putrescine exporter SapBCDF of Escherichia coli.";
RL J. Biol. Chem. 291:26343-26351(2016).
CC -!- FUNCTION: Involved in the uptake of putrescine (PubMed:15590624,
CC PubMed:19181795, PubMed:27803167, PubMed:23719730). Imports putrescine
CC for its utilization as an energy source in the absence of glucose
CC (PubMed:23719730). {ECO:0000269|PubMed:15590624,
CC ECO:0000269|PubMed:19181795, ECO:0000269|PubMed:23719730,
CC ECO:0000269|PubMed:27803167}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(in) + putrescine(in) = H(+)(out) + putrescine(out);
CC Xref=Rhea:RHEA:28891, ChEBI:CHEBI:15378, ChEBI:CHEBI:326268;
CC Evidence={ECO:0000305|PubMed:23719730};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28893;
CC Evidence={ECO:0000305|PubMed:23719730};
CC -!- ACTIVITY REGULATION: Putrescine uptake is inhibited by carbonyl cyanide
CC m-chlorophenylhydrazone (CCCP), which dissipates the proton motive
CC force. {ECO:0000269|PubMed:23719730}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=3.7 uM for putrescine {ECO:0000269|PubMed:19181795};
CC KM=6.2 uM for putrescine {ECO:0000269|PubMed:23719730};
CC Vmax=19.9 nmol/min/mg enzyme {ECO:0000269|PubMed:19181795};
CC Vmax=8.3 nmol/min/mg enzyme {ECO:0000269|PubMed:23719730};
CC -!- PATHWAY: Amine and polyamine degradation; putrescine degradation.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000305}; Multi-pass
CC membrane protein {ECO:0000255}.
CC -!- INDUCTION: Repressed by PuuR. {ECO:0000269|PubMed:19181795,
CC ECO:0000269|PubMed:23719730}.
CC -!- DISRUPTION PHENOTYPE: No visible growth phenotype, no change in
CC extracellular putrescine levels, if the putrescine export operon
CC sapBCDF is also deleted growth is slower.
CC {ECO:0000269|PubMed:27803167}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. {ECO:0000305}.
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DR EMBL; U00096; AAC74378.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA14856.2; -; Genomic_DNA.
DR PIR; C64878; C64878.
DR RefSeq; NP_415812.4; NC_000913.3.
DR RefSeq; WP_000996856.1; NZ_SSZK01000012.1.
DR AlphaFoldDB; P76037; -.
DR SMR; P76037; -.
DR BioGRID; 4260139; 3.
DR DIP; DIP-11601N; -.
DR IntAct; P76037; 3.
DR STRING; 511145.b1296; -.
DR TCDB; 2.A.3.1.13; the amino acid-polyamine-organocation (apc) family.
DR PaxDb; P76037; -.
DR PRIDE; P76037; -.
DR EnsemblBacteria; AAC74378; AAC74378; b1296.
DR EnsemblBacteria; BAA14856; BAA14856; BAA14856.
DR GeneID; 946287; -.
DR KEGG; ecj:JW1289; -.
DR KEGG; eco:b1296; -.
DR PATRIC; fig|511145.12.peg.1351; -.
DR EchoBASE; EB3666; -.
DR eggNOG; COG0531; Bacteria.
DR HOGENOM; CLU_007946_6_0_6; -.
DR InParanoid; P76037; -.
DR OMA; TRILMSM; -.
DR PhylomeDB; P76037; -.
DR BioCyc; EcoCyc:B1296-MON; -.
DR BioCyc; MetaCyc:B1296-MON; -.
DR UniPathway; UPA00188; -.
DR PRO; PR:P76037; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015489; F:putrescine transmembrane transporter activity; EXP:EcoCyc.
DR GO; GO:0015295; F:solute:proton symporter activity; IDA:EcoCyc.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
DR GO; GO:0009447; P:putrescine catabolic process; IMP:EcoCyc.
DR GO; GO:0015847; P:putrescine transport; IMP:EcoCyc.
DR InterPro; IPR004841; AA-permease/SLC12A_dom.
DR Pfam; PF00324; AA_permease; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Symport; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..461
FT /note="Putrescine importer PuuP"
FT /id="PRO_0000054211"
FT TRANSMEM 27..47
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 54..74
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 125..145
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 162..182
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 204..224
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 242..262
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 275..295
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 344..364
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 365..385
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 399..419
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 422..442
FT /note="Helical"
FT /evidence="ECO:0000255"
FT MUTAGEN 110
FT /note="Y->X: The uptake activity is reduced to one-eighth
FT of that of wild-type."
FT /evidence="ECO:0000269|PubMed:19181795"
SQ SEQUENCE 461 AA; 50853 MW; B027F1FA01C1B5BB CRC64;
MAINSPLNIA AQPGKTRLRK SLKLWQVVMM GLAYLTPMTV FDTFGIVSGI SDGHVPASYL
LALAGVLFTA ISYGKLVRQF PEAGSAYTYA QKSINPHVGF MVGWSSLLDY LFLPMINVLL
AKIYLSALFP EVPPWVWVVT FVAILTAANL KSVNLVANFN TLFVLVQISI MVVFIFLVVQ
GLHKGEGVGT VWSLQPFISE NAHLIPIITG ATIVCFSFLG FDAVTTLSEE TPDAARVIPK
AIFLTAVYGG VIFIAASFFM QLFFPDISRF KDPDAALPEI ALYVGGKLFQ SIFLCTTFVN
TLASGLASHA SVSRLLYVMG RDNVFPERVF GYVHPKWRTP ALNVIMVGIV ALSALFFDLV
TATALINFGA LVAFTFVNLS VFNHFWRRKG MNKSWKDHFH YLLMPLVGAL TVGVLWVNLE
STSLTLGLVW ASLGGAYLWY LIRRYRKVPL YDGDRTPVSE T
