PAEA_ECO57
ID PAEA_ECO57 Reviewed; 447 AA.
AC P0AE47; P39319;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 108.
DE RecName: Full=Polyamine export protein {ECO:0000250|UniProtKB:A0A0F6BAS6};
GN Name=paeA {ECO:0000250|UniProtKB:A0A0F6BAS6}; Synonyms=ytfL;
GN OrderedLocusNames=Z5829, ECs5196;
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: Involved in cadaverine and putrescine tolerance in stationary
CC phase. May facilitate the efflux of both cadaverine and putrescine from
CC the cytoplasm, reducing potentially toxic levels under certain stress
CC conditions. {ECO:0000250|UniProtKB:A0A0F6BAS6}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P0AE45}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- SIMILARITY: Belongs to the UPF0053 family. PaeA subfamily.
CC {ECO:0000305}.
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DR EMBL; AE005174; AAG59416.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB38619.1; -; Genomic_DNA.
DR PIR; D86119; D86119.
DR PIR; D91278; D91278.
DR RefSeq; NP_313223.1; NC_002695.1.
DR RefSeq; WP_000935036.1; NZ_SEKU01000001.1.
DR AlphaFoldDB; P0AE47; -.
DR SMR; P0AE47; -.
DR STRING; 155864.EDL933_5564; -.
DR EnsemblBacteria; AAG59416; AAG59416; Z5829.
DR EnsemblBacteria; BAB38619; BAB38619; ECs_5196.
DR GeneID; 913900; -.
DR KEGG; ece:Z5829; -.
DR KEGG; ecs:ECs_5196; -.
DR PATRIC; fig|386585.9.peg.5431; -.
DR eggNOG; COG1253; Bacteria.
DR HOGENOM; CLU_015237_4_0_6; -.
DR OMA; YLTMEDV; -.
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:0050660; F:flavin adenine dinucleotide binding; IEA:InterPro.
DR CDD; cd04590; CBS_pair_CorC_HlyC_assoc; 1.
DR Gene3D; 3.10.580.10; -; 1.
DR Gene3D; 3.30.465.10; -; 1.
DR InterPro; IPR000644; CBS_dom.
DR InterPro; IPR046342; CBS_dom_sf.
DR InterPro; IPR002550; CNNM.
DR InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR InterPro; IPR044751; Ion_transp-like_CBS.
DR InterPro; IPR005170; Transptr-assoc_dom.
DR Pfam; PF00571; CBS; 1.
DR Pfam; PF03471; CorC_HlyC; 1.
DR Pfam; PF01595; DUF21; 1.
DR SMART; SM01091; CorC_HlyC; 1.
DR SUPFAM; SSF54631; SSF54631; 1.
DR SUPFAM; SSF56176; SSF56176; 1.
DR PROSITE; PS51371; CBS; 2.
DR PROSITE; PS51846; CNNM; 1.
PE 3: Inferred from homology;
KW CBS domain; Cell inner membrane; Cell membrane; Membrane;
KW Reference proteome; Repeat; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..447
FT /note="Polyamine export protein"
FT /id="PRO_0000088363"
FT TOPO_DOM 1..4
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 5..25
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 26..54
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 55..75
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 76..99
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 100..120
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 121..141
FT /note="Periplasmic"
FT /evidence="ECO:0000305"
FT TRANSMEM 142..162
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 163..447
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0AE45"
FT DOMAIN 1..197
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01193"
FT DOMAIN 216..275
FT /note="CBS 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
FT DOMAIN 282..343
FT /note="CBS 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00703"
SQ SEQUENCE 447 AA; 49763 MW; 22C0DB3FAE5D926F CRC64;
MLNSILVILC LIAVSAFFSM SEISLAASRK IKLKLLADEG NINAQRVLNM QENPGMFFTV
VQIGLNAVAI LGGIVGDAAF SPAFHSLFSR YMSAELSEQL SFILSFSLVT GMFILFADLT
PKRIGMIAPE AVALRIINPM RFCLYVCTPL VWFFNGLANI IFRIFKLPMV RKDDITSDDI
YAVVEAGALA GVLRKQEHEL IENVFELESR TVPSSMTPRE NVIWFDLHED EQSLKNKVAE
HPHSKFLVCN EDIDHIIGYV DSKDLLNRVL ANQSLALNSG VQIRNTLIVP DTLTLSEALE
SFKTAGEDFA VIMNEYALVV GIITLNDVMT TLMGDLVGQG LEEQIVARDE NSWLIDGGTP
IDDVMRVLDI DEFPQSGNYE TIGGFMMFML RKIPKRTDSV KFAGYKFEVV DIDNYRIDQL
LVTRIDSKAT ALSPKLPDAK DKEESVA
