PLAP_ECO57
ID PLAP_ECO57 Reviewed; 452 AA.
AC P0AA48; P33016;
DT 13-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 13-SEP-2005, sequence version 1.
DT 03-AUG-2022, entry version 92.
DE RecName: Full=Low-affinity putrescine importer PlaP {ECO:0000250|UniProtKB:P0AA47};
GN Name=plaP; OrderedLocusNames=Z3176, ECs2816;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
CC -!- FUNCTION: Putrescine importer. {ECO:0000250|UniProtKB:P0AA47}.
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:0000250|UniProtKB:P0AA47};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:28893;
CC Evidence={ECO:0000250|UniProtKB:P0AA47};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P0AA47}; 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=AAG57073.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB36239.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE005174; AAG57073.1; ALT_INIT; Genomic_DNA.
DR EMBL; BA000007; BAB36239.1; ALT_INIT; Genomic_DNA.
DR RefSeq; NP_310843.2; NC_002695.1.
DR RefSeq; WP_000019197.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AA48; -.
DR SMR; P0AA48; -.
DR STRING; 155864.EDL933_3087; -.
DR EnsemblBacteria; AAG57073; AAG57073; Z3176.
DR EnsemblBacteria; BAB36239; BAB36239; ECs_2816.
DR GeneID; 67417796; -.
DR GeneID; 912852; -.
DR KEGG; ece:Z3176; -.
DR KEGG; ecs:ECs_2816; -.
DR PATRIC; fig|386585.9.peg.2952; -.
DR eggNOG; COG0531; Bacteria.
DR HOGENOM; CLU_007946_6_0_6; -.
DR OMA; PDNWRIP; -.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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:0015293; F:symporter activity; IEA:UniProtKB-KW.
DR GO; GO:0006865; P:amino acid transport; IEA:UniProtKB-KW.
DR InterPro; IPR002293; AA/rel_permease1.
DR Pfam; PF13520; AA_permease_2; 1.
PE 3: Inferred from homology;
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_0000054216"
FT TOPO_DOM 1..16
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 17..37
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 38..48
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 49..69
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 70..95
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 96..116
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 117..123
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 124..144
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 145..158
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 159..179
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 180..199
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 200..220
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 221..237
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 238..258
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 259..283
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 284..304
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 305..339
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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:0000255"
FT TRANSMEM 395..415
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 416..417
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 418..438
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 439..452
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
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
