POTE_ECOLI
ID POTE_ECOLI Reviewed; 439 AA.
AC P0AAF1; P24170;
DT 11-OCT-2005, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Putrescine transporter PotE {ECO:0000255|HAMAP-Rule:MF_02073, ECO:0000305};
DE AltName: Full=Putrescine-proton symporter / putrescine-ornithine antiporter {ECO:0000255|HAMAP-Rule:MF_02073, ECO:0000305};
GN Name=potE {ECO:0000255|HAMAP-Rule:MF_02073, ECO:0000303|PubMed:1584788,
GN ECO:0000303|PubMed:1939141}; OrderedLocusNames=b0692, JW0679;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION IN PUTRESCINE UPTAKE,
RP SUBCELLULAR LOCATION, AND OPERON.
RC STRAIN=K12 / 3000/ DR112;
RX PubMed=1939141; DOI=10.1016/s0021-9258(18)54798-0;
RA Kashiwagi K., Suzuki T., Suzuki F., Furuchi T., Kobayashi H., Igarashi K.;
RT "Coexistence of the genes for putrescine transport protein and ornithine
RT decarboxylase at 16 min on Escherichia coli chromosome.";
RL J. Biol. Chem. 266:20922-20927(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8905232; DOI=10.1093/dnares/3.3.137;
RA Oshima T., Aiba H., Baba T., Fujita K., Hayashi K., Honjo A., Ikemoto K.,
RA Inada T., Itoh T., Kajihara M., Kanai K., Kashimoto K., Kimura S.,
RA Kitagawa M., Makino K., Masuda S., Miki T., Mizobuchi K., Mori H.,
RA Motomura K., Nakamura Y., Nashimoto H., Nishio Y., Saito N., Sampei G.,
RA Seki Y., Tagami H., Takemoto K., Wada C., Yamamoto Y., Yano M.,
RA Horiuchi T.;
RT "A 718-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 12.7-28.0 min region on the linkage map.";
RL DNA Res. 3:137-155(1996).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 [5]
RP FUNCTION IN PUTRESCINE EXPORT, CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND
RP BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=1584788; DOI=10.1073/pnas.89.10.4529;
RA Kashiwagi K., Miyamoto S., Suzuki F., Kobayashi H., Igarashi K.;
RT "Excretion of putrescine by the putrescine-ornithine antiporter encoded by
RT the potE gene of Escherichia coli.";
RL Proc. Natl. Acad. Sci. U.S.A. 89:4529-4533(1992).
RN [6]
RP FUNCTION IN PUTRESCINE UPTAKE AND EXPORT, CATALYTIC ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, TOPOLOGY,
RP AND MUTAGENESIS OF GLU-77; GLU-207 AND GLU-433.
RX PubMed=9045651; DOI=10.1074/jbc.272.10.6318;
RA Kashiwagi K., Shibuya S., Tomitori H., Kuraishi A., Igarashi K.;
RT "Excretion and uptake of putrescine by the PotE protein in Escherichia
RT coli.";
RL J. Biol. Chem. 272:6318-6323(1997).
RN [7]
RP SUBUNIT, AND MUTAGENESIS OF CYS-62; LYS-68; TYR-78; LYS-82; TYR-90; TYR-92;
RP TRP-201; CYS-210; CYS-285; CYS-286; TRP-292; LYS-301; TYR-308; TRP-422 AND
RP TYR-425.
RX PubMed=10964926; DOI=10.1074/jbc.m006083200;
RA Kashiwagi K., Kuraishi A., Tomitori H., Igarashi A., Nishimura K.,
RA Shirahata A., Igarashi K.;
RT "Identification of the putrescine recognition site on polyamine transport
RT protein PotE.";
RL J. Biol. Chem. 275:36007-36012(2000).
RN [8]
RP SUBCELLULAR LOCATION, AND TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [9]
RP REVIEW.
RX PubMed=21796432; DOI=10.1007/s00726-011-0989-9;
RA Tomitori H., Kashiwagi K., Igarashi K.;
RT "Structure and function of polyamine-amino acid antiporters CadB and PotE
RT in Escherichia coli.";
RL Amino Acids 42:733-740(2012).
CC -!- FUNCTION: Catalyzes both the uptake and excretion of putrescine. The
CC uptake of putrescine is dependent on the membrane potential and the
CC excretion involves putrescine-ornithine antiporter activity.
CC {ECO:0000255|HAMAP-Rule:MF_02073, ECO:0000269|PubMed:1584788,
CC ECO:0000269|PubMed:1939141, ECO:0000269|PubMed:9045651}.
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:0000255|HAMAP-Rule:MF_02073,
CC ECO:0000269|PubMed:9045651};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28893;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02073,
CC ECO:0000269|PubMed:1584788, ECO:0000269|PubMed:9045651};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-ornithine(out) + putrescine(in) = L-ornithine(in) +
CC putrescine(out); Xref=Rhea:RHEA:28827, ChEBI:CHEBI:46911,
CC ChEBI:CHEBI:326268; Evidence={ECO:0000255|HAMAP-Rule:MF_02073,
CC ECO:0000269|PubMed:1584788, ECO:0000269|PubMed:9045651};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:28828;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02073,
CC ECO:0000269|PubMed:1584788, ECO:0000269|PubMed:9045651};
CC -!- ACTIVITY REGULATION: Uptake activity, but not antiporter activity, is
CC inhibited by CCCP and N-ethylmaleimide (NEM). Uptake of putrescine is
CC inhibited by high concentrations of ornithine.
CC {ECO:0000269|PubMed:1584788, ECO:0000269|PubMed:9045651}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.8 uM for putrescine (for uptake activity)
CC {ECO:0000269|PubMed:9045651};
CC KM=73 uM for putrescine (for antiporter activity)
CC {ECO:0000269|PubMed:1584788, ECO:0000269|PubMed:9045651};
CC KM=108 uM for ornithine (for antiporter activity)
CC {ECO:0000269|PubMed:9045651};
CC Vmax=0.82 nmol/min/mg enzyme for antiporter activity
CC {ECO:0000269|PubMed:1584788};
CC pH dependence:
CC Optimum pH is 6.5 for uptake activity. Optimum pH is 9.2 for
CC antiporter activity. {ECO:0000269|PubMed:9045651};
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:10964926}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_02073, ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:9045651,
CC ECO:0000305|PubMed:1939141}; Multi-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_02073}.
CC -!- INDUCTION: Induced at low environmental pH. Part of the speFL-speF-potE
CC operon. {ECO:0000305|PubMed:1939141}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. Basic amino acid/polyamine antiporter (APA) (TC 2.A.3.2)
CC family. {ECO:0000255|HAMAP-Rule:MF_02073, ECO:0000305}.
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DR EMBL; M64495; AAA62786.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73786.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA35348.1; -; Genomic_DNA.
DR PIR; B40839; B40839.
DR RefSeq; NP_415219.1; NC_000913.3.
DR RefSeq; WP_000075845.1; NZ_STEB01000044.1.
DR AlphaFoldDB; P0AAF1; -.
DR SMR; P0AAF1; -.
DR BioGRID; 4261131; 16.
DR IntAct; P0AAF1; 1.
DR STRING; 511145.b0692; -.
DR TCDB; 2.A.3.2.1; the amino acid-polyamine-organocation (apc) family.
DR PaxDb; P0AAF1; -.
DR PRIDE; P0AAF1; -.
DR EnsemblBacteria; AAC73786; AAC73786; b0692.
DR EnsemblBacteria; BAA35348; BAA35348; BAA35348.
DR GeneID; 66671040; -.
DR GeneID; 945422; -.
DR KEGG; ecj:JW0679; -.
DR KEGG; eco:b0692; -.
DR PATRIC; fig|1411691.4.peg.1584; -.
DR EchoBASE; EB0746; -.
DR eggNOG; COG0531; Bacteria.
DR HOGENOM; CLU_007946_1_0_6; -.
DR InParanoid; P0AAF1; -.
DR OMA; AEKVMSV; -.
DR PhylomeDB; P0AAF1; -.
DR BioCyc; EcoCyc:POTE-MON; -.
DR BioCyc; MetaCyc:POTE-MON; -.
DR SABIO-RK; P0AAF1; -.
DR PRO; PR:P0AAF1; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005887; C:integral component of plasma membrane; ISM:EcoCyc.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
DR GO; GO:0015496; F:putrescine:ornithine antiporter activity; IDA:EcoCyc.
DR GO; GO:0015293; F:symporter activity; IDA:EcoCyc.
DR GO; GO:0015847; P:putrescine transport; IDA:EcoCyc.
DR HAMAP; MF_02073; Putrescine_transp; 1.
DR InterPro; IPR002293; AA/rel_permease1.
DR InterPro; IPR004754; Amino_acid_antiprt.
DR InterPro; IPR027566; Symport/antiport_PotE.
DR Pfam; PF13520; AA_permease_2; 1.
DR TIGRFAMs; TIGR00905; 2A0302; 1.
DR TIGRFAMs; TIGR04299; antiport_PotE; 1.
PE 1: Evidence at protein level;
KW Amino-acid transport; Antiport; Cell inner membrane; Cell membrane;
KW Membrane; Reference proteome; Symport; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..439
FT /note="Putrescine transporter PotE"
FT /id="PRO_0000054250"
FT TOPO_DOM 1..9
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9045651"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT TOPO_DOM 31..39
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:9045651"
FT TRANSMEM 40..60
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT TOPO_DOM 61..90
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9045651"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT TOPO_DOM 112..113
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:9045651"
FT TRANSMEM 114..134
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT TOPO_DOM 135..151
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9045651"
FT TRANSMEM 152..172
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT TOPO_DOM 173..185
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:9045651"
FT TRANSMEM 186..206
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT TOPO_DOM 207..224
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9045651"
FT TRANSMEM 225..245
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT TOPO_DOM 246..275
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:9045651"
FT TRANSMEM 276..296
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT TOPO_DOM 297..320
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9045651"
FT TRANSMEM 321..341
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT TOPO_DOM 342..353
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:9045651"
FT TRANSMEM 354..374
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT TOPO_DOM 375..386
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:9045651"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT TOPO_DOM 408..409
FT /note="Periplasmic"
FT /evidence="ECO:0000269|PubMed:9045651"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02073"
FT TOPO_DOM 431..439
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996,
FT ECO:0000269|PubMed:9045651"
FT MUTAGEN 62
FT /note="C->A,T: Strong decrease in both uptake and excretion
FT activities."
FT /evidence="ECO:0000269|PubMed:10964926"
FT MUTAGEN 62
FT /note="C->S: Moderate decrease in both uptake and excretion
FT activities."
FT /evidence="ECO:0000269|PubMed:10964926"
FT MUTAGEN 68
FT /note="K->A: Slight decrease in both uptake and excretion
FT activities."
FT /evidence="ECO:0000269|PubMed:10964926"
FT MUTAGEN 77
FT /note="E->A,D,N,Q: Strong decrease in both uptake and
FT excretion activities."
FT /evidence="ECO:0000269|PubMed:9045651"
FT MUTAGEN 78
FT /note="Y->L: Uptake activity decreases more than excretion
FT activity."
FT /evidence="ECO:0000269|PubMed:10964926"
FT MUTAGEN 82
FT /note="K->A: Slight decrease in both uptake and excretion
FT activities."
FT /evidence="ECO:0000269|PubMed:10964926"
FT MUTAGEN 90
FT /note="Y->L: Uptake activity decreases more than excretion
FT activity."
FT /evidence="ECO:0000269|PubMed:10964926"
FT MUTAGEN 92
FT /note="Y->L: Moderate decrease in both uptake and excretion
FT activities."
FT /evidence="ECO:0000269|PubMed:10964926"
FT MUTAGEN 201
FT /note="W->F,L,Y: Strong decrease in both uptake and
FT excretion activities."
FT /evidence="ECO:0000269|PubMed:10964926"
FT MUTAGEN 207
FT /note="E->A,D,N,Q: Lack of both uptake and excretion
FT activities."
FT /evidence="ECO:0000269|PubMed:9045651"
FT MUTAGEN 210
FT /note="C->A: Moderate decrease in both uptake and excretion
FT activities."
FT /evidence="ECO:0000269|PubMed:10964926"
FT MUTAGEN 285
FT /note="C->A: Moderate decrease in both uptake and excretion
FT activities."
FT /evidence="ECO:0000269|PubMed:10964926"
FT MUTAGEN 286
FT /note="C->A: Moderate decrease in both uptake and excretion
FT activities."
FT /evidence="ECO:0000269|PubMed:10964926"
FT MUTAGEN 292
FT /note="W->F,L,Y: Strong decrease in both uptake and
FT excretion activities."
FT /evidence="ECO:0000269|PubMed:10964926"
FT MUTAGEN 301
FT /note="K->A: Excretion activity decreases more than uptake
FT activity."
FT /evidence="ECO:0000269|PubMed:10964926"
FT MUTAGEN 308
FT /note="Y->L: Excretion activity decreases more than uptake
FT activity."
FT /evidence="ECO:0000269|PubMed:10964926"
FT MUTAGEN 422
FT /note="W->L: Uptake activity decreases more than excretion
FT activity."
FT /evidence="ECO:0000269|PubMed:10964926"
FT MUTAGEN 425
FT /note="Y->F: Moderate decrease in both uptake and excretion
FT activities."
FT /evidence="ECO:0000269|PubMed:10964926"
FT MUTAGEN 425
FT /note="Y->L: Strong decrease in both uptake and excretion
FT activities."
FT /evidence="ECO:0000269|PubMed:10964926"
FT MUTAGEN 433
FT /note="E->A,D,N,Q: Strong decrease in both uptake and
FT excretion activities."
FT /evidence="ECO:0000269|PubMed:9045651"
SQ SEQUENCE 439 AA; 46495 MW; C6F800284DA8C5C8 CRC64;
MSQAKSNKMG VVQLTILTMV NMMGSGIIML PTKLAEVGTI SIISWLVTAV GSMALAWAFA
KCGMFSRKSG GMGGYAEYAF GKSGNFMANY TYGVSLLIAN VAIAISAVGY GTELLGASLS
PVQIGLATIG VLWICTVANF GGARITGQIS SITVWGVIIP VVGLCIIGWF WFSPTLYVDS
WNPHHAPFFS AVGSSIAMTL WAFLGLESAC ANTDVVENPE RNVPIAVLGG TLGAAVIYIV
STNVIAGIVP NMELANSTAP FGLAFAQMFT PEVGKVIMAL MVMSCCGSLL GWQFTIAQVF
KSSSDEGYFP KIFSRVTKVD APVQGMLTIV IIQSGLALMT ISPSLNSQFN VLVNLAVVTN
IIPYILSMAA LVIIQKVANV PPSKAKVANF VAFVGAMYSF YALYSSGEEA MLYGSIVTFL
GWTLYGLVSP RFELKNKHG
