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Database: UniProt
Entry: A0A241W1E5_9GAMM
LinkDB: A0A241W1E5_9GAMM
Original site: A0A241W1E5_9GAMM 
ID   A0A241W1E5_9GAMM        Unreviewed;       444 AA.
AC   A0A241W1E5;
DT   25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT   25-OCT-2017, sequence version 1.
DT   27-MAR-2024, entry version 26.
DE   RecName: Full=Polyamine export protein {ECO:0000256|ARBA:ARBA00039818};
GN   ORFNames=B9T31_03405 {ECO:0000313|EMBL:OTG87560.1};
OS   Acinetobacter sp. ANC 4558.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Moraxellales; Moraxellaceae;
OC   Acinetobacter.
OX   NCBI_TaxID=1977876 {ECO:0000313|EMBL:OTG87560.1, ECO:0000313|Proteomes:UP000194907};
RN   [1] {ECO:0000313|EMBL:OTG87560.1, ECO:0000313|Proteomes:UP000194907}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ANC 4558 {ECO:0000313|EMBL:OTG87560.1,
RC   ECO:0000313|Proteomes:UP000194907};
RA   Nemec A., Radolfova-Krizova L.;
RT   "High diversity of culturable Acinetobacter species in natural soil and
RT   water ecosystems.";
RL   Submitted (APR-2017) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OTG87560.1}.
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DR   EMBL; NEGH01000002; OTG87560.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A241W1E5; -.
DR   STRING; 1977876.B9T31_03405; -.
DR   OrthoDB; 9797674at2; -.
DR   Proteomes; UP000194907; Unassembled WGS sequence.
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        6..27
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          284..344
FT                   /note="CBS"
FT                   /evidence="ECO:0000259|PROSITE:PS51371"
SQ   SEQUENCE   444 AA;  50043 MW;  0F8935F63D17940A CRC64;
     MSLFQNIVII LLLIIGGGFL SLTEIAFAGA RKVKLKILAE AGEIRAQKVL DLQGNSADFF
     AASQIGMNAI AILGGILGEA AFRPYFVNFV DRFYDGPLTQ PIGFALSFTL VTSLFILFAD
     LMPKRLAMIA PEKIAIAVIN PIQIFIIICR PLAFFINAIA NVLFRLFKIN TKRDDNITFD
     DISAVMDAGA QAGVLQKQEH HFIENVFELE ERNVPSSMTT RENVIFFTLI ESEESIRQKL
     AEFPYSKFLV CNHNIDDVIG YVDTKDLLVR ILNNQKINQL NESTIRNVLT IPDTLTLSEL
     LDRFRSSKEK FAVVINEYAL VVGVITLSDI MITVMGDWVT PTDEDQQIIK RDENSWLIEG
     STPIEDLKHA LGIDEMPDDE SYETLAGFMM YRLRKIPRPA DTVIFNDYKF EVVDVDHFKI
     DQLLVTRLNS ITPLATEESK NNSE
//
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