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Database: UniProt
Entry: D6Z188_DESAT
LinkDB: D6Z188_DESAT
Original site: D6Z188_DESAT 
ID   D6Z188_DESAT            Unreviewed;       870 AA.
AC   D6Z188;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   24-JAN-2024, entry version 74.
DE   RecName: Full=Multifunctional fusion protein {ECO:0000256|HAMAP-Rule:MF_01463, ECO:0000256|HAMAP-Rule:MF_01464};
DE   Includes:
DE     RecName: Full=Protein translocase subunit SecD {ECO:0000256|HAMAP-Rule:MF_01463};
DE   Includes:
DE     RecName: Full=Protein-export membrane protein SecF {ECO:0000256|HAMAP-Rule:MF_01464};
GN   Name=secF {ECO:0000256|HAMAP-Rule:MF_01464};
GN   Synonyms=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN   OrderedLocusNames=DaAHT2_0637 {ECO:0000313|EMBL:ADH85343.1};
OS   Desulfurivibrio alkaliphilus (strain DSM 19089 / UNIQEM U267 / AHT2).
OC   Bacteria; Thermodesulfobacteriota; Desulfobulbia; Desulfobulbales;
OC   Desulfobulbaceae; Desulfurivibrio.
OX   NCBI_TaxID=589865 {ECO:0000313|EMBL:ADH85343.1, ECO:0000313|Proteomes:UP000001508};
RN   [1] {ECO:0000313|Proteomes:UP000001508}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19089 / UNIQEM U267 / AHT2
RC   {ECO:0000313|Proteomes:UP000001508};
RG   US DOE Joint Genome Institute;
RA   Pitluck S., Chertkov O., Detter J.C., Han C., Tapia R., Larimer F.,
RA   Land M., Hauser L., Kyrpides N., Mikhailova N., Sorokin D.Y., Muyzer G.,
RA   Woyke T.;
RT   "Complete sequence of Desulfurivibrio alkaliphilus AHT2.";
RL   Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Part of the Sec protein translocase complex. Interacts with
CC       the SecYEG preprotein conducting channel. SecDF uses the proton motive
CC       force (PMF) to complete protein translocation after the ATP-dependent
CC       function of SecA. {ECO:0000256|HAMAP-Rule:MF_01463}.
CC   -!- SUBUNIT: Forms a complex with SecD. Part of the essential Sec protein
CC       translocation apparatus which comprises SecA, SecYEG and auxiliary
CC       proteins SecDF. Other proteins may also be involved.
CC       {ECO:0000256|HAMAP-Rule:MF_01464}.
CC   -!- SUBUNIT: Forms a complex with SecF. Part of the essential Sec protein
CC       translocation apparatus which comprises SecA, SecYEG and auxiliary
CC       proteins SecDF. Other proteins may also be involved.
CC       {ECO:0000256|HAMAP-Rule:MF_01463}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01463}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01463}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC       membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the SecD/SecF family. SecD subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01463}.
CC   -!- SIMILARITY: Belongs to the SecD/SecF family. SecF subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01464}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|HAMAP-Rule:MF_01463}.
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DR   EMBL; CP001940; ADH85343.1; -; Genomic_DNA.
DR   RefSeq; WP_013162874.1; NC_014216.1.
DR   AlphaFoldDB; D6Z188; -.
DR   STRING; 589865.DaAHT2_0637; -.
DR   KEGG; dak:DaAHT2_0637; -.
DR   eggNOG; COG0341; Bacteria.
DR   eggNOG; COG0342; Bacteria.
DR   HOGENOM; CLU_007894_3_0_7; -.
DR   InParanoid; D6Z188; -.
DR   OMA; RTVNTGM; -.
DR   OrthoDB; 9805019at2; -.
DR   Proteomes; UP000001508; Chromosome.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015450; F:protein-transporting ATPase activity; IEA:InterPro.
DR   GO; GO:0065002; P:intracellular protein transmembrane transport; IEA:UniProtKB-UniRule.
DR   GO; GO:0006605; P:protein targeting; IEA:UniProtKB-UniRule.
DR   GO; GO:0043952; P:protein transport by the Sec complex; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.30.1360.200; -; 1.
DR   Gene3D; 3.30.70.3400; -; 2.
DR   Gene3D; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 2.
DR   HAMAP; MF_01463_B; SecD_B; 1.
DR   HAMAP; MF_01464_B; SecF_B; 1.
DR   InterPro; IPR005791; SecD.
DR   InterPro; IPR022813; SecD/SecF_arch_bac.
DR   InterPro; IPR022645; SecD/SecF_bac.
DR   InterPro; IPR022646; SecD/SecF_CS.
DR   InterPro; IPR048631; SecD_1st.
DR   InterPro; IPR048634; SecD_SecF_C.
DR   InterPro; IPR005665; SecF_bac.
DR   NCBIfam; TIGR00916; 2A0604s01; 2.
DR   NCBIfam; TIGR01129; secD; 1.
DR   NCBIfam; TIGR00966; transloc_SecF; 1.
DR   PANTHER; PTHR30081:SF1; PROTEIN TRANSLOCASE SUBUNIT SECD; 1.
DR   PANTHER; PTHR30081; PROTEIN-EXPORT MEMBRANE PROTEIN SEC; 1.
DR   Pfam; PF07549; Sec_GG; 2.
DR   Pfam; PF21760; SecD_1st; 1.
DR   Pfam; PF02355; SecD_SecF; 2.
DR   PRINTS; PR01755; SECFTRNLCASE.
DR   SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 2.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01463};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_01463};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01463};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP-
KW   Rule:MF_01463}; Reference proteome {ECO:0000313|Proteomes:UP000001508};
KW   Translocation {ECO:0000256|ARBA:ARBA00023010, ECO:0000256|HAMAP-
KW   Rule:MF_01463};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_01463};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_01463};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01463}.
FT   TRANSMEM        397..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        424..442
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        448..467
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        488..513
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        519..543
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        574..594
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        697..714
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        721..743
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        749..769
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        795..818
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        824..850
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   DOMAIN          154..213
FT                   /note="Protein translocase subunit SecDF P1"
FT                   /evidence="ECO:0000259|Pfam:PF21760"
FT   DOMAIN          377..541
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
FT   DOMAIN          680..850
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
SQ   SEQUENCE   870 AA;  95348 MW;  91951F596983D3E3 CRC64;
     MPSSLKWKIG LLFFMIVFAV VTVLPSLSVP VPGWWKKNLA PEGLRLGLDL QGGMHLVLKV
     DIDQAIANSL DLAAEELRAT MRDERITLVR ARHDDPHIAV FTLPNVEALN TVERAVANDF
     PNLKIRVESE EGTFPRVFLS LDDEQVEFIE QNAVRQSLEI IRNRIDQFGV AEPVIVRQGL
     DEIVVQLPGV RDPDRAIDLI GQTAQLEFKL VDDSGVVDLD RLINQAIEAG QWERGGDRQQ
     LNQALRGQLP EEREIYFHRR VDRETGQERQ EPILLHVTSL MTGEMVRDAR VRVGGTFNEP
     YVSLDLTARG GRLFGQITER NVGRQLAIVL DDVVRSAPVI RERILGGSAQ ISGGFTHGEA
     SDLAIVLRVG ALPAPVDIIQ NLTVGASLGQ DSIQRGIIAG LFGALLVATF MVIYYRLSGV
     IANAALLLNV LFIFTGLAMM QATLTLPGIA GIILAIGMAV DANVLIFERM REEFALGKTV
     KSGVEGGYSK AFSTIIDSQV TTLITALALF LFGTGPIQGF AVTLSLGVTF NLITTLFGTK
     IVYDFLHSKR KLKEIRFLTL LTNPGLDFMR LRRYAFGISG IMLLVGAVAM VEVYRGTANL
     GVDFSGGTMA QYQAQQPFDL AEVRQALSDA GLEGAQPQHV EGENRLIVRI KEDREVVGQI
     TNTITAALDQ YLGDKGFWLE SQSEIGSAIS ETLRNKALQA ILIALLGVLI YLALRFQMRF
     GLAAAGATFH DVIVVLGICW LFNIEITLLI VTALLTIAGY SLNDSVVVFD RIRENIKKRP
     GDDLKVLINR SVNEIISRTV ITSLTTALVL VSLLIYGGVV LHDFSLVLLI GILVGTFSSI
     FVASPLLMML PGSQHEMAKS DEEKVVIEQV
//
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