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Database: UniProt
Entry: A3MYV0_ACTP2
LinkDB: A3MYV0_ACTP2
Original site: A3MYV0_ACTP2 
ID   A3MYV0_ACTP2            Unreviewed;       431 AA.
AC   A3MYV0;
DT   03-APR-2007, integrated into UniProtKB/TrEMBL.
DT   03-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 107.
DE   RecName: Full=Polyamine export protein {ECO:0000256|ARBA:ARBA00039818};
GN   OrderedLocusNames=APL_0228 {ECO:0000313|EMBL:ABN73336.1};
OS   Actinobacillus pleuropneumoniae serotype 5b (strain L20).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Actinobacillus.
OX   NCBI_TaxID=416269 {ECO:0000313|EMBL:ABN73336.1, ECO:0000313|Proteomes:UP000001432};
RN   [1] {ECO:0000313|EMBL:ABN73336.1, ECO:0000313|Proteomes:UP000001432}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=L20 {ECO:0000313|EMBL:ABN73336.1,
RC   ECO:0000313|Proteomes:UP000001432};
RX   PubMed=18065534; DOI=10.1128/JB.01845-07;
RA   Foote S.J., Bosse J.T., Bouevitch A.B., Langford P.R., Young N.M.,
RA   Nash J.H.;
RT   "The complete genome sequence of Actinobacillus pleuropneumoniae L20
RT   (serotype 5b).";
RL   J. Bacteriol. 190:1495-1496(2008).
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:0000256|ARBA:ARBA00037177}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|ARBA:ARBA00004429}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004429}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the UPF0053 family. PaeA subfamily.
CC       {ECO:0000256|ARBA:ARBA00038280}.
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DR   EMBL; CP000569; ABN73336.1; -; Genomic_DNA.
DR   RefSeq; WP_005600282.1; NC_009053.1.
DR   AlphaFoldDB; A3MYV0; -.
DR   STRING; 416269.APL_0228; -.
DR   EnsemblBacteria; ABN73336; ABN73336; APL_0228.
DR   GeneID; 69417393; -.
DR   KEGG; apl:APL_0228; -.
DR   eggNOG; COG1253; Bacteria.
DR   HOGENOM; CLU_015237_4_0_6; -.
DR   Proteomes; UP000001432; Chromosome.
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; 3.30.465.10; -; 1.
DR   Gene3D; 3.10.580.10; CBS-domain; 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   PANTHER; PTHR22777; HEMOLYSIN-RELATED; 1.
DR   PANTHER; PTHR22777:SF16; POLYAMINE EXPORT PROTEIN; 1.
DR   Pfam; PF00571; CBS; 1.
DR   Pfam; PF01595; CNNM; 1.
DR   Pfam; PF03471; CorC_HlyC; 1.
DR   SMART; SM01091; CorC_HlyC; 1.
DR   SUPFAM; SSF54631; CBS-domain pair; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51371; CBS; 2.
DR   PROSITE; PS51846; CNNM; 1.
PE   3: Inferred from homology;
KW   CBS domain {ECO:0000256|ARBA:ARBA00023122, ECO:0000256|PROSITE-
KW   ProRule:PRU00703}; Cell inner membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022519};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|PROSITE-
KW   ProRule:PRU01193}; Reference proteome {ECO:0000313|Proteomes:UP000001432};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|PROSITE-
KW   ProRule:PRU01193};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|PROSITE-
KW   ProRule:PRU01193}.
FT   TRANSMEM        6..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        59..82
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        102..122
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        134..156
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          1..199
FT                   /note="CNNM transmembrane"
FT                   /evidence="ECO:0000259|PROSITE:PS51846"
FT   DOMAIN          218..279
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
FT   DOMAIN          284..341
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
SQ   SEQUENCE   431 AA;  48759 MW;  FAC43684999A309A CRC64;
     MSLFEASLII LLLIVTSAVI SSAEISLAGA RKLKLQSMIN EGDLRAEKVL KLQEQPGRFI
     TVVQIGLNMV AILGGVVGES AINPYFSELL SKYTQAEWVD SAASWIAFII VTSAFVLFAD
     LMPKRLAMTY PEKIAVRTIG VMMFCIALFK PLVLFFDWIA NTLFKFFHVS TVRQDNMTSE
     DIVAVVDAGA KAGILKAQEH YLIENVFEMQ ERRVTSTMTT REHIVFLNRT DNREKVLETL
     GEDPYSKVLI CDDGLDKILG YIETHDLLTQ YLKNDNVSLT DAKLLKKSLF IPDTLSLYEV
     LELFKSAGED FAVIVNEYAL VVGILTLNDV MSIVMGELVS TEEEQIVRRD EDSWLIDGAT
     PLEDVMKALE IESFPNAENY ETIGGFMMYM LRKIPKKTDF VLYDQYKFEI IDTENFKIDQ
     LMVSFRKDIS N
//
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