PLAP_ECOLI
ID PLAP_ECOLI Reviewed; 452 AA.
AC P0AA47; P33016;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 116.
DE RecName: Full=Low-affinity putrescine importer PlaP {ECO:0000305};
DE AltName: Full=Putrescine low affinity permease {ECO:0000303|PubMed:21266585};
GN Name=plaP {ECO:0000303|PubMed:21266585}; Synonyms=yeeF;
GN OrderedLocusNames=b2014, JW5330;
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 / BHB2600;
RA Richterich P., Lakey N., Gryan G., Jaehn L., Mintz L., Robison K.,
RA Church G.M.;
RT "Automated multiplex sequencing of the E.coli genome.";
RL Submitted (OCT-1993) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097040; DOI=10.1093/dnares/3.6.379;
RA Itoh T., Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K.,
RA Kasai H., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T.,
RA Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S., Nakamura Y.,
RA Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y.,
RA Sivasundaram S., Tagami H., Takeda J., Takemoto K., Wada C., Yamamoto Y.,
RA Horiuchi T.;
RT "A 460-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 40.1-50.0 min region on the linkage map.";
RL DNA Res. 3:379-392(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 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 [6]
RP FUNCTION, ACTIVITY REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND GENE
RP NAME.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=21266585; DOI=10.1074/jbc.m110.176032;
RA Kurihara S., Suzuki H., Oshida M., Benno Y.;
RT "A novel putrescine importer required for type 1 pili-driven surface
RT motility induced by extracellular putrescine in Escherichia coli K-12.";
RL J. Biol. Chem. 286:10185-10192(2011).
CC -!- FUNCTION: Putrescine importer. Required for induction of type 1 pili-
CC driven surface motility. {ECO:0000269|PubMed:21266585}.
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:21266585};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28893;
CC Evidence={ECO:0000305|PubMed:21266585};
CC -!- ACTIVITY REGULATION: Putrescine uptake is inhibited by carbonyl cyanide
CC m-chlorophenylhydrazone (CCCP), which dissipates the proton motive
CC force. {ECO:0000269|PubMed:21266585}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=155 uM for putrescine {ECO:0000269|PubMed:21266585};
CC Vmax=9.3 nmol/min/mg enzyme {ECO:0000269|PubMed:21266585};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the amino acid-polyamine-organocation (APC)
CC superfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA16420.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; U00009; AAA16420.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC75075.2; -; Genomic_DNA.
DR EMBL; AP009048; BAA15842.2; -; Genomic_DNA.
DR PIR; E64966; E64966.
DR RefSeq; NP_416518.2; NC_000913.3.
DR RefSeq; WP_000019197.1; NZ_STEB01000048.1.
DR AlphaFoldDB; P0AA47; -.
DR SMR; P0AA47; -.
DR BioGRID; 4260417; 173.
DR IntAct; P0AA47; 1.
DR STRING; 511145.b2014; -.
DR TCDB; 2.A.3.1.14; the amino acid-polyamine-organocation (apc) family.
DR PaxDb; P0AA47; -.
DR PRIDE; P0AA47; -.
DR EnsemblBacteria; AAC75075; AAC75075; b2014.
DR EnsemblBacteria; BAA15842; BAA15842; BAA15842.
DR GeneID; 67417796; -.
DR GeneID; 946533; -.
DR KEGG; ecj:JW5330; -.
DR KEGG; eco:b2014; -.
DR PATRIC; fig|1411691.4.peg.238; -.
DR EchoBASE; EB1842; -.
DR eggNOG; COG0531; Bacteria.
DR HOGENOM; CLU_007946_6_0_6; -.
DR InParanoid; P0AA47; -.
DR OMA; PDNWRIP; -.
DR PhylomeDB; P0AA47; -.
DR BioCyc; EcoCyc:YEEF-MON; -.
DR BioCyc; MetaCyc:YEEF-MON; -.
DR PRO; PR:P0AA47; -.
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; IMP: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:0048870; P:cell motility; IMP:EcoCyc.
DR GO; GO:0015847; P:putrescine transport; IMP:EcoCyc.
DR InterPro; IPR002293; AA/rel_permease1.
DR Pfam; PF13520; AA_permease_2; 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..452
FT /note="Low-affinity putrescine importer PlaP"
FT /id="PRO_0000054215"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..48
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..95
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..123
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..199
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..283
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..339
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 340..360
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 361..381
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 382..394
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..417
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 439..452
FT /note="Cytoplasmic"
FT /evidence="ECO:0000269|PubMed:15919996"
SQ SEQUENCE 452 AA; 49538 MW; F8B618C6BD3E762E CRC64;
MSHNVTPNTS RVELRKTLTL VPVVMMGLAY MQPMTLFDTF GIVSGLTDGH VPTAYAFALI
AILFTALSYG KLVRRYPSAG SAYTYAQKSI SPTVGFMVGW SSLLDYLFAP MINILLAKIY
FEALVPSIPS WMFVVALVAF MTAFNLRSLK SVANFNTVIV VLQVVLIAVI LGMVVYGVFE
GEGAGTLAST RPFWSGDAHV IPMITGATIL CFSFTGFDGI SNLSEETKDA ERVIPRAIFL
TALIGGMIFI FATYFLQLYF PDISRFKDPD ASQPEIMLYV AGKAFQVGAL IFSTITVLAS
GMAAHAGVAR LMYVMGRDGV FPKSFFGYVH PKWRTPAMNI ILVGAIALLA INFDLVMATA
LINFGALVAF TFVNLSVISQ FWIREKRNKT LKDHFQYLFL PMCGALTVGA LWVNLEESSM
VLGLIWAAIG LIYLACVTKS FRNPVPQYED VA
