ID I8U7R0_9ALTE Unreviewed; 429 AA.
AC I8U7R0;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=Polyamine export protein {ECO:0000256|ARBA:ARBA00039818};
GN ORFNames=AGRI_04522 {ECO:0000313|EMBL:EIW89336.1};
OS Alishewanella agri BL06.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Alishewanella.
OX NCBI_TaxID=1195246 {ECO:0000313|EMBL:EIW89336.1, ECO:0000313|Proteomes:UP000035062};
RN [1] {ECO:0000313|EMBL:EIW89336.1, ECO:0000313|Proteomes:UP000035062}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BL06 {ECO:0000313|EMBL:EIW89336.1,
RC ECO:0000313|Proteomes:UP000035062};
RX PubMed=22933763; DOI=10.1128/JB.01129-12;
RA Kim J., Jung J., Sung J.S., Chun J., Park W.;
RT "Genome Sequence of Pectin-Degrading Alishewanella agri, Isolated from
RT Landfill Soil.";
RL J. Bacteriol. 194:5135-5136(2012).
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:EIW89336.1}.
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DR EMBL; AKKU01000011; EIW89336.1; -; Genomic_DNA.
DR RefSeq; WP_008983826.1; NZ_AKKU01000011.1.
DR AlphaFoldDB; I8U7R0; -.
DR STRING; 1195246.AGRI_04522; -.
DR PATRIC; fig|1195246.3.peg.890; -.
DR eggNOG; COG1253; Bacteria.
DR Proteomes; UP000035062; 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}; Reference proteome {ECO:0000313|Proteomes:UP000035062};
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..29
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 58..78
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 98..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..341
FT /note="CBS"
FT /evidence="ECO:0000259|PROSITE:PS51371"
SQ SEQUENCE 429 AA; 48055 MW; 9C17CD9E1CE66C35 CRC64;
MTTLEYLLVM FLLVAASSFF SISEIALAAS RKMRLRMLAT EGDVRAEKVL QLQEHPGNFF
TVVQIGLNAV AILGGILGES AFTPYFSSLL ALISSEPWVQ PAAFTLSVFF VTSLFILFAD
LMPKRLAMIA PEQIALRIVS PMLFLILVLR PFVWLFNGLA NLFFSLFKVP TMRKDDITPD
DIMAMMDAGA QAGVLQEHEH QLLENVFDME SRTVTSAMTA RESLIFFTKD ESQDNIKAKI
AEHPHAKFLV CDKVLDQVVG YVDTRDILMQ VLHDQPISLS KEGIVRAPLI IPDTLSLYEV
LEHFKSAGID FAIILNEYAL VVGIITLKDV MSIVMGELVS SEEDQIVARD NNSWLVEGLT
PLADVMRVLG IDSFPDAENY ETIAGFMMYS LRKIPKRTDF VLHGGYKFEV VDIDSYKIDQ
LLVTRIEQP
//
