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Database: UniProt
Entry: D2Z512_9BACT
LinkDB: D2Z512_9BACT
Original site: D2Z512_9BACT 
ID   D2Z512_9BACT            Unreviewed;       418 AA.
AC   D2Z512;
DT   23-MAR-2010, integrated into UniProtKB/TrEMBL.
DT   23-MAR-2010, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   SubName: Full=Efflux transporter, RND family, MFP subunit {ECO:0000313|EMBL:EFC90571.1};
GN   ORFNames=Dpep_0541 {ECO:0000313|EMBL:EFC90571.1};
OS   Dethiosulfovibrio peptidovorans DSM 11002.
OC   Bacteria; Synergistota; Synergistia; Synergistales;
OC   Dethiosulfovibrionaceae; Dethiosulfovibrio.
OX   NCBI_TaxID=469381 {ECO:0000313|EMBL:EFC90571.1, ECO:0000313|Proteomes:UP000006427};
RN   [1] {ECO:0000313|EMBL:EFC90571.1, ECO:0000313|Proteomes:UP000006427}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 11002 {ECO:0000313|EMBL:EFC90571.1,
RC   ECO:0000313|Proteomes:UP000006427};
RX   PubMed=21304695;
RA   Labutti K., Mayilraj S., Clum A., Lucas S., Glavina Del Rio T., Nolan M.,
RA   Tice H., Cheng J.F., Pitluck S., Liolios K., Ivanova N., Mavromatis K.,
RA   Mikhailova N., Pati A., Goodwin L., Chen A., Palaniappan K., Land M.,
RA   Hauser L., Chang Y.J., Jeffries C.D., Rohde M., Spring S., Goker M.,
RA   Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA   Kyrpides N.C., Klenk H.P., Lapidus A.;
RT   "Permanent draft genome sequence of Dethiosulfovibrio peptidovorans type
RT   strain (SEBR 4207).";
RL   Stand. Genomic Sci. 3:85-92(2010).
CC   -!- SIMILARITY: Belongs to the membrane fusion protein (MFP) (TC 8.A.1)
CC       family. {ECO:0000256|ARBA:ARBA00009477}.
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:EFC90571.1}.
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DR   EMBL; ABTR02000001; EFC90571.1; -; Genomic_DNA.
DR   RefSeq; WP_005659384.1; NZ_ABTR02000001.1.
DR   AlphaFoldDB; D2Z512; -.
DR   STRING; 469381.Dpep_0541; -.
DR   PaxDb; 469381-Dpep_0541; -.
DR   eggNOG; COG0845; Bacteria.
DR   OrthoDB; 9772050at2; -.
DR   Proteomes; UP000006427; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0022857; F:transmembrane transporter activity; IEA:InterPro.
DR   Gene3D; 2.40.30.170; -; 1.
DR   Gene3D; 2.40.420.20; -; 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   InterPro; IPR006143; RND_pump_MFP.
DR   NCBIfam; TIGR01730; RND_mfp; 1.
DR   PANTHER; PTHR30158; ACRA/E-RELATED COMPONENT OF DRUG EFFLUX TRANSPORTER; 1.
DR   Pfam; PF13533; Biotin_lipoyl_2; 1.
DR   SUPFAM; SSF111369; HlyD-like secretion proteins; 1.
PE   3: Inferred from homology;
KW   Coiled coil {ECO:0000256|SAM:Coils}; Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006427};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          80..125
FT                   /note="Membrane fusion protein biotin-lipoyl like"
FT                   /evidence="ECO:0000259|Pfam:PF13533"
FT   REGION          385..418
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          127..177
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   418 AA;  45295 MW;  FAEAA6B38B685FF9 CRC64;
     MGNVGRRGSA KVVLLILILG AAAFFGREYF VGKAQDEARA QAQAVEQAKP QAPVVVLHVV
     RKADLAVPRE YIGRVEPIQS VSIRPQISGE IAEVHFQEGS MVKEGDLLFS IDDRRFRTTV
     SLRKAELAKA EANYDRASKY LKRLKAADPR SVSASDIDMA QSDLLQAKAQ VQQAKASLSL
     AQIDLSYTKI RAPITGKVGE AFYTKGNYVT PAGSTTLTKI VQMDPIRVSF ALSDREYLDQ
     LDSFKNRDQS VFDATIKLAN GEVYPKKGER DFEDNVMDKG TGTIMVSLRF ENDGGALVPG
     SMVRVEARPS KSKVVPVIPQ ESVMADGQGD FVYVVDEANK VDRRGVVLGD SIGKNCEVLS
     GLEGGERIVF RGIQSVRPGV VVSPIQEETG GDKSPAELAQ ASDYDLKPIV SGDGEIDG
//
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