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
//