ID   PAEA_SALT1              Reviewed;         447 AA.
AC   A0A0F6BAS6;
DT   29-SEP-2021, integrated into UniProtKB/Swiss-Prot.
DT   24-JUN-2015, sequence version 1.
DT   03-AUG-2022, entry version 31.
DE   RecName: Full=Polyamine export protein {ECO:0000303|PubMed:33481283};
GN   Name=paeA {ECO:0000303|PubMed:33481283};
GN   Synonyms=ytfL {ECO:0000312|EMBL:ACY91628.1};
GN   OrderedLocusNames=STM14_5293 {ECO:0000312|EMBL:ACY91628.1};
OS   Salmonella typhimurium (strain 14028s / SGSC 2262).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=588858;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=14028s / SGSC 2262;
RX   PubMed=19897643; DOI=10.1128/jb.01233-09;
RA   Jarvik T., Smillie C., Groisman E.A., Ochman H.;
RT   "Short-term signatures of evolutionary change in the Salmonella enterica
RT   serovar typhimurium 14028 genome.";
RL   J. Bacteriol. 192:560-567(2010).
RN   [2]
RP   FUNCTION, AND DISRUPTION PHENOTYPE.
RC   STRAIN=ATCC 14028;
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:0000250|UniProtKB:P0AE45}; Multi-pass membrane protein
CC       {ECO:0000255}.
CC   -!- DISRUPTION PHENOTYPE: Deletion mutant loses viability in stationary
CC       phase when grown in acidic medium with nitrite. Mutant is sensitive to
CC       cadaverine and putrescine but not to spermine or spermidine at pH 9.
CC       {ECO:0000269|PubMed:33481283}.
CC   -!- SIMILARITY: Belongs to the UPF0053 family. PaeA subfamily.
CC       {ECO:0000305}.
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DR   EMBL; CP001363; ACY91628.1; -; Genomic_DNA.
DR   RefSeq; WP_000934974.1; NZ_CP043402.1.
DR   SMR; A0A0F6BAS6; -.
DR   EnsemblBacteria; ACY91628; ACY91628; STM14_5293.
DR   KEGG; seo:STM14_5293; -.
DR   PATRIC; fig|588858.6.peg.4790; -.
DR   HOGENOM; CLU_015237_4_0_6; -.
DR   OMA; YLTMEDV; -.
DR   BioCyc; SENT588858:STM14_RS23115-MON; -.
DR   Proteomes; UP000002695; 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; Repeat;
KW   Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..447
FT                   /note="Polyamine export protein"
FT                   /id="PRO_0000453544"
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;  49768 MW;  5CD6204B3025D758 CRC64;
     MLNSIFIIFC LIAVSAFFSI SEISLAASRK IKLKLLADEG SINAQRVLKM QENPGMFFTV
     VQIGLNAVAI LGGIVGDAAF SPAFSALFSH YMSPELSEQL SFILSFSLVT GLFILFADLT
     PKRIGMIAPE AVALRIINPM RFCLFVFRPL VWLFNGMANN IFRLFKIPMV RKDDITSDDI
     YAVVEAGALA GVLRKQEHEL IENVFELESR TVPSSMTSRE SIIWFDLHED EQSLKKKVAE
     HPHSKFLVCN EDIDHIIGYV DSKDLLNRVL ANQSMALNSG VQIRNTLIVP DTLTLSEALE
     SFKTAGEDFA VIMNEYALVV GIITLNDVMT TLMGDLVGQG LEEQIVARDE NSWLVDGGTP
     IDDVMRVLDI DEFPQSGNYE TIGGFMMFML RKIPKRTDSV KFSGYKFEVV DIDNYRIDQL
     LVTRLDNKSN VPAPKLPDAQ GKEDSAA