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Database: UniProt
Entry: A0A0X8GR39_9BURK
LinkDB: A0A0X8GR39_9BURK
Original site: A0A0X8GR39_9BURK 
ID   A0A0X8GR39_9BURK        Unreviewed;       437 AA.
AC   A0A0X8GR39;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 29.
DE   RecName: Full=Polyamine export protein {ECO:0000256|ARBA:ARBA00039818};
GN   ORFNames=VN23_20115 {ECO:0000313|EMBL:AMC36726.1};
OS   Janthinobacterium sp. B9-8.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Janthinobacterium.
OX   NCBI_TaxID=1236179 {ECO:0000313|EMBL:AMC36726.1, ECO:0000313|Proteomes:UP000069577};
RN   [1] {ECO:0000313|EMBL:AMC36726.1, ECO:0000313|Proteomes:UP000069577}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=B9-8 {ECO:0000313|EMBL:AMC36726.1,
RC   ECO:0000313|Proteomes:UP000069577};
RA   Xu X., Jin W., Wu Q., Jiang L., Huang H.;
RT   "The whole genome sequence of Janthinbacterium sp. B9-8, a bacterium
RT   isolated from low temperature sewage.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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; CP014222; AMC36726.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0X8GR39; -.
DR   STRING; 1236179.VN23_20115; -.
DR   KEGG; jab:VN23_20115; -.
DR   OrthoDB; 9797674at2; -.
DR   Proteomes; UP000069577; 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; 1.
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}; 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        101..121
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        133..155
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          286..343
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
SQ   SEQUENCE   437 AA;  48786 MW;  2DE3074063EB88A2 CRC64;
     MMNGLLIIFI LILISAFFSV SEIALAAARK HKLQQMSEDG DKRADLVLAL QERPGDFFTV
     VQVGVNAVAI LGGILGEPTF SPVFKALFIQ LDVHVETAET LGFLMSFTLV TGLFIQFADL
     IPKRIGMAVP ETTAVKVVAP ILFCIFLMRP LVFIFDGIAN MLFNAFNLPA VRRDEITTDD
     IVAMADAGAM AGTVRRKEHN LIENVFELET RTVTSVMTAR ESVIFFSLNE AEETIRARML
     ADPHSKFLLC ENSIDSVFAY IDAKDILQLV LKGGEINLLE GLKQYGNRKL LTIPDTLSLS
     EVLEQFKEAR EDFAVILNEY ALVVGIITLN DVTIQLMGSM VDPGADQIVQ RDESSWLVDG
     VTPIEDVKKA LNIDELKDEE NYETIAGFMM YMLKRIPKKA ELLIFGDYKF EVVDIDNFRI
     DQLLVTRITP QKKADSE
//
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