PAEA_ECOLI
ID PAEA_ECOLI Reviewed; 447 AA.
AC P0AE45; P39319; Q2M687;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 120.
DE RecName: Full=Polyamine export protein {ECO:0000303|PubMed:33481283};
GN Name=paeA {ECO:0000303|PubMed:33481283}; Synonyms=ytfL;
GN OrderedLocusNames=b4218, JW4177;
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 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
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].
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 TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
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 [5]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=33481283; DOI=10.1111/mmi.14686;
RA Iwadate Y., Ramezanifard R., Golubeva Y.A., Fenlon L.A., Slauch J.M.;
RT "PaeA (YtfL) protects from cadaverine and putrescine stress in Salmonella
RT Typhimurium and E. coli.";
RL Mol. Microbiol. 115:1379-1394(2021).
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:0000269|PubMed:33481283}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:15919996}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- DISRUPTION PHENOTYPE: Deletion of the gene results in increased
CC sensitivity to cadaverine and putrescine, but not to spermidine and
CC spermine. {ECO:0000269|PubMed:33481283}.
CC -!- SIMILARITY: Belongs to the UPF0053 family. PaeA subfamily.
CC {ECO:0000305}.
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DR EMBL; U14003; AAA97114.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77175.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78219.1; -; Genomic_DNA.
DR PIR; S56443; S56443.
DR RefSeq; NP_418639.1; NC_000913.3.
DR RefSeq; WP_000935036.1; NZ_STEB01000013.1.
DR AlphaFoldDB; P0AE45; -.
DR SMR; P0AE45; -.
DR BioGRID; 4259306; 58.
DR DIP; DIP-48233N; -.
DR IntAct; P0AE45; 4.
DR STRING; 511145.b4218; -.
DR TCDB; 1.A.112.2.11; the cyclin m mg2+ exporter (cnnm) family.
DR jPOST; P0AE45; -.
DR PaxDb; P0AE45; -.
DR PRIDE; P0AE45; -.
DR EnsemblBacteria; AAC77175; AAC77175; b4218.
DR EnsemblBacteria; BAE78219; BAE78219; BAE78219.
DR GeneID; 948735; -.
DR KEGG; ecj:JW4177; -.
DR KEGG; eco:b4218; -.
DR PATRIC; fig|1411691.4.peg.2483; -.
DR EchoBASE; EB2405; -.
DR eggNOG; COG1253; Bacteria.
DR HOGENOM; CLU_015237_4_0_6; -.
DR InParanoid; P0AE45; -.
DR OMA; YLTMEDV; -.
DR PhylomeDB; P0AE45; -.
DR BioCyc; EcoCyc:G7873-MON; -.
DR PRO; PR:P0AE45; -.
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: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 1: Evidence at protein level;
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_0000088362"
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:0000269|PubMed:15919996"
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
