ID A0A290ZPV7_9RHOO Unreviewed; 431 AA.
AC A0A290ZPV7;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Polyamine export protein {ECO:0000256|ARBA:ARBA00039818};
GN ORFNames=CCZ27_14825 {ECO:0000313|EMBL:ATE61045.1};
OS Thauera sp. K11.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Rhodocyclales; Zoogloeaceae;
OC Thauera.
OX NCBI_TaxID=2005884 {ECO:0000313|EMBL:ATE61045.1, ECO:0000313|Proteomes:UP000217984};
RN [1] {ECO:0000313|EMBL:ATE61045.1, ECO:0000313|Proteomes:UP000217984}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K11 {ECO:0000313|EMBL:ATE61045.1,
RC ECO:0000313|Proteomes:UP000217984};
RA Xi L., Qiao N.;
RT "Thauera phenolivorans sp. nov., a phenol derivative-degrading bacterium
RT isolated from activated sludge and an emended description of the genus
RT Thauera.";
RL Submitted (SEP-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}.
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DR EMBL; CP023439; ATE61045.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A290ZPV7; -.
DR KEGG; thk:CCZ27_14825; -.
DR OrthoDB; 9797674at2; -.
DR Proteomes; UP000217984; 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:UP000217984};
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..28
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 58..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 101..120
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 132..155
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..198
FT /note="CNNM transmembrane"
FT /evidence="ECO:0000259|PROSITE:PS51846"
FT DOMAIN 217..276
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
FT DOMAIN 283..339
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 431 AA; 47579 MW; 892C8F9BB52F0713 CRC64;
MLLNQLFAIA LLIAVSAFFS LAEISLAASR KIKLRQLADE GREPAARVLA LQQNPGHFFT
VVQIALNAIA ILGGIVGEQA LSPQVADLLR PLYDGVHLDT IGFLIAFGFV TSLFVLFADV
MPKRIAMVRP EAVAMAVVQP IQLCMWLFAP LVWMFDGIAD RLLRFFKLPS ARPEDITAGD
IVAMADAGAQ AGVLLRQEQQ LISNVFELDT RIVPSAMTAR DSIVFLTLAE SEESIRNKIA
ASPHGKFPVC KDAIDNVIGY VDWKDILPRI LDGQPLSLRN APIVRNVLVL PDSLSLFEAL
ERFRDAKEDF ALVVNEYALV VGLLTLQDVM STVMGELVSP FQEDMIVRRD DNSWLIDGAT
PIEDVMAALD IAQFEGFDNY ETIAGFLMYT LRKVPRRTDS VNYGGYTFEV VDIDNYRIDQ
VLVTRDGSGE G
//