ID   H1G300_9GAMM            Unreviewed;       415 AA.
AC   H1G300;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 25.
DE   SubName: Full=RND family efflux transporter MFP subunit {ECO:0000313|EMBL:EHQ52187.1};
GN   ORFNames=ECTPHS_05816 {ECO:0000313|EMBL:EHQ52187.1};
OS   Ectothiorhodospira sp. PHS-1.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC   Ectothiorhodospiraceae; Ectothiorhodospira.
OX   NCBI_TaxID=519989 {ECO:0000313|EMBL:EHQ52187.1, ECO:0000313|Proteomes:UP000005314};
RN   [1] {ECO:0000313|EMBL:EHQ52187.1, ECO:0000313|Proteomes:UP000005314}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PHS-1 {ECO:0000313|EMBL:EHQ52187.1,
RC   ECO:0000313|Proteomes:UP000005314};
RA   Saltikov C.W., Zargar K., Conrad A., Bernick D., Lowe T.M., Stolc V.,
RA   Hoeft S., Oremland R.S., Stolz J.;
RT   "ArxA, a new clade of arsenite oxidase within the DMSO family of molybdenum
RT   oxidoreductases.";
RL   Submitted (JAN-2012) to the EMBL/GenBank/DDBJ databases.
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:EHQ52187.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AGBG01000009; EHQ52187.1; -; Genomic_DNA.
DR   AlphaFoldDB; H1G300; -.
DR   STRING; 519989.ECTPHS_05816; -.
DR   eggNOG; COG0845; Bacteria.
DR   OrthoDB; 8524475at2; -.
DR   Proteomes; UP000005314; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   Gene3D; 2.40.30.170; -; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   Gene3D; 1.10.287.470; Helix hairpin bin; 1.
DR   InterPro; IPR039562; MFP_biotin_lipoyl_2.
DR   PANTHER; PTHR30469; MULTIDRUG RESISTANCE PROTEIN MDTA; 1.
DR   PANTHER; PTHR30469:SF36; SLL0180 PROTEIN; 1.
DR   Pfam; PF13533; Biotin_lipoyl_2; 1.
DR   Pfam; PF13437; HlyD_3; 1.
DR   SUPFAM; SSF111369; HlyD-like secretion proteins; 2.
PE   4: Predicted;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        10..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          75..117
FT                   /note="Membrane fusion protein biotin-lipoyl like"
FT                   /evidence="ECO:0000259|Pfam:PF13533"
FT   COILED          110..158
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          190..217
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   415 AA;  45791 MW;  21875CBBC0D40483 CRC64;
     MPLPPRIKRL LPLILLAIGI GGFVLLLITR PSEPPRQVAE RVWRVTAEEI TPRTLPPQVT
     LHGHVTSPRA AGLRAAVEAD VARVPVEEGR QVQAGDTLVI LDDRELELLV RQRQADLDDL
     RAQLRALERS HARDREALDR ERTLLALAER AVNRAQDLLN RNLGSPATLE EAQRNREQQA
     LAVANRQLAL DDYDARREQL RARTRRAEAQ LAQAALDLER SHVRAPFDGR IARVNVAPGD
     RVRVGDALVT LFDTQALEVR APIPAVHLPA VRQALDMASP PVAQARVDGL PLTLELSRLA
     GETGAGSAGV EGLFRIVSDT QDVPLGRFVS LRLSLPPREH VVALPFEALY GLDRIYRLED
     GRMQGLAVRR VGEWVDEDGR ERILVSGEAL RAGDRIITTR LPNAIDGLRV SAEAD
//