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
//