ID   A0A1H9WTF1_9BACI        Unreviewed;      1141 AA.
AC   A0A1H9WTF1;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 19.
DE   SubName: Full=Hydrophobic/amphiphilic exporter-1, HAE1 family {ECO:0000313|EMBL:SES37071.1};
GN   ORFNames=SAMN05444126_1476 {ECO:0000313|EMBL:SES37071.1};
OS   Salisediminibacterium haloalkalitolerans.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae;
OC   Salisediminibacterium.
OX   NCBI_TaxID=1464123 {ECO:0000313|EMBL:SES37071.1, ECO:0000313|Proteomes:UP000199318};
RN   [1] {ECO:0000313|EMBL:SES37071.1, ECO:0000313|Proteomes:UP000199318}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10nlg {ECO:0000313|EMBL:SES37071.1,
RC   ECO:0000313|Proteomes:UP000199318};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; FOGV01000047; SES37071.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H9WTF1; -.
DR   STRING; 1464123.SAMN05444126_1476; -.
DR   OrthoDB; 9757876at2; -.
DR   Proteomes; UP000199318; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   Gene3D; 3.30.70.1430; Multidrug efflux transporter AcrB pore domain; 2.
DR   Gene3D; 3.30.70.1440; Multidrug efflux transporter AcrB pore domain; 1.
DR   Gene3D; 3.30.70.1320; Multidrug efflux transporter AcrB pore domain like; 1.
DR   Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 2.
DR   InterPro; IPR027463; AcrB_DN_DC_subdom.
DR   InterPro; IPR001036; Acrflvin-R.
DR   PANTHER; PTHR32063; -; 1.
DR   PANTHER; PTHR32063:SF0; SWARMING MOTILITY PROTEIN SWRC; 1.
DR   Pfam; PF00873; ACR_tran; 1.
DR   PRINTS; PR00702; ACRIFLAVINRP.
DR   SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 2.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199318};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        330..353
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        360..380
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        386..411
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        431..457
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        463..486
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        522..542
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        856..875
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        882..902
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        908..933
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        954..973
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        985..1011
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1045..1121
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1045..1064
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1098..1121
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1141 AA;  125597 MW;  3AF2B2697CE335E5 CRC64;
     MRNLIKFSIG RPVFTLVTMT LFILLGAVSL TNIPLKLIPE IDPPVAAVVT SYDEAGPQEV
     VDGVSRPMET SLSTIEGLES INSISMEGSS LTLLEFSWTT SIEDVENDII QNMNQTELPS
     GAGSPQFLKF DPSQIPIIQA SISTIDNDND NLTEQVNELE TDLLQVDGVG SIDFMGDAAD
     EAAVRLDQNL LEENNLTQEI VVQTLQSHNV TAPGGVVESG EAEISTRLLF EMNSVEDIEN
     ITLTEDPEDG EDVTVADVAE VSIAPEPTDM ITRTNQDDAI MLSVQQQADA NTADVSRAFI
     NELDSLLEDD QYSDLDASIL FNQGEYVDEA ISNVALALIA GGFIAMAVLF AFLRNFKTPL
     LIGIAIPFSV IVTFVLLYFS NFSLNIMTLG GLALGIGMLV DNSIVVIENI YRHLNMKKDP
     KQAALDGTKE VATAITASTL TTISVFLPVV FIAGIVGNLF REFALTVAFS LLASLLVALT
     VVPMLASKWL RTPRADVETE RRKSRFVKFF DSSARWSLRH RFTIVLLTLL LLVGGGAGVT
     TVGTEFLPAT DEGFFQIDVE NESGTPLEST FEDMEEIEAI LDDENDVAHY TAVTGSSGEQ
     GPMAGQGGSG HEGVVYVSMV PVNERERSTM DFSEDIRTDV ERAAPDAEIS ITMDASFGSD
     PNTFSFDLSD SNPLQLEEVS EDLLEQFEDM SEFTEVTNTL EETVPELQLN IDDDEAREAG
     LTPAEIASQV EQMTGGALAT QIVTEENDVY NVMVRYEEEF TETEEDLENL LLQTQDGDYI
     ALGELAEFDE GESPEEIQRI NQEESVQFDL TFGTDYNLGE INTIVQDEID EYGLPDETSI
     SYTGDQELLE DAVNDLTFAL ILAIVFVYLV MAAQFESLRY PFVIMFSVPL VVIGVAIALT
     LTRTPISVTA FIGLIVLVGI VVNNSIVLVD YINQRKEAGF KSADAIIEGV KDRARPILMT
     ASTTILALVP LALGYGEGSE IQQPLAITVI GGMISATFLT LVLIPVLYSF MDKETRFMNR
     KYVTPDGQLI PAYLMEERYS DETGKTRGRY ISDEKEDMSE YYRPAEDVPE SGQLVDVEED
     RSGEQPNEAS QSDDPFMYDE NVVDRLPSRK EKHRADDLSQ EEILKRLESM IERNKNRRDD
     E
//