ID A0A1T5I7Q1_9BACT Unreviewed; 1009 AA.
AC A0A1T5I7Q1;
DT 10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2017, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN Synonyms=secF {ECO:0000256|HAMAP-Rule:MF_01464};
GN ORFNames=SAMN06298215_0191 {ECO:0000313|EMBL:SKC35234.1};
OS Bacteroidales bacterium WCE2008.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales.
OX NCBI_TaxID=1945891 {ECO:0000313|EMBL:SKC35234.1, ECO:0000313|Proteomes:UP000190446};
RN [1] {ECO:0000313|EMBL:SKC35234.1, ECO:0000313|Proteomes:UP000190446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WCE2008 {ECO:0000313|EMBL:SKC35234.1,
RC ECO:0000313|Proteomes:UP000190446};
RA Peterson S.W.;
RL Submitted (FEB-2017) 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 membrane {ECO:0000256|HAMAP-Rule:MF_01463};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01463}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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; FUZM01000001; SKC35234.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1T5I7Q1; -.
DR STRING; 1945891.SAMN06298215_0191; -.
DR OrthoDB; 9805019at2; -.
DR Proteomes; UP000190446; Unassembled WGS sequence.
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; 3.30.70.3220; -; 1.
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; 1.
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 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:UP000190446};
KW Signal {ECO:0000256|SAM:SignalP};
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 SIGNAL 1..29
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 30..1009
FT /note="Multifunctional fusion protein"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5012979050"
FT TRANSMEM 520..539
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 548..567
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 573..594
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 615..637
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 643..667
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 701..722
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 842..859
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 871..896
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 902..921
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 952..970
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 976..1000
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 203..257
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 500..665
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
FT DOMAIN 821..1002
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 1009 AA; 109613 MW; A1FCCCA5959C1910 CRC64;
MQSKGAIRLT IIALAIASLW QLSFTAVTAL QEKKADKYAA KAVEAFKQTA DYSNIKADDQ
AFVLDSIAKS RKSWYVDSLS NENVYLGYSF KDVKAKEINL GLDLKGGMNV MLQVQLEDLV
KALAGNNKTP EFENAIALAK QRSVNSRQDF ISLFADAWKE TGNGQRLSSI FGTYEMRDRI
KPESTDDQVI AVIKEDAESA IANSFNVLRN RIDRFGVTQP SIQKLGNSGR ILVELPGVKE
PERVRKLLQG TASLEFWPTF ENSEIQPYLI EANRALAQLI EADNAEVAEI AEEAAVEEAD
SLLSEELQLN AEDAKALENY KKQNPLFAVL QPSQSKTGAC LGFAQSTDTA VVNRYLSMPQ
VRDLFPAEFR PMWSVKPSEY VSGGNWYELV AIKAATRDGK APLDGGAVTD ARVSMNQQSN
GGSPSVSMTM NAEGANVWAR LTKDNIGKQI AIVLDGMVYS YPQVHTEISG GSSEISGHFT
MEEATDLTNV LKSGKLPAPA KIIQEQVVGP SLGSRSIRSG MLSFLIAFLL VLVYMVVFYN
RAGIAADIAL LCNVLLLFGF LTGFGAVLTL PGIAGLILTL GMAVDANVII YERIKEELAA
GKGLGKAIAD GYRNAYSAII DGQLTTIITG FVLFFFGSGP VQGFATTLII GIVTSLLTSI
FVTRLIFEGR LAKGKDITFD RPSTRNFLKN TNIDFLGKRK YSYVISGALI LIAILSICFK
GFTYGVDFQG GRTYVVRFDQ PQTAEGVRAG VEAEFNDGIS SVEVKQFGGP TQMKITTTYK
VNDESSEVDA EVEQKLFNAV KPFFADQSIT LSSFTSTLDN PNGIISSDKV GPTIANDMKR
DAMIAVIIAL LAIFGYIAFR FKGWTWGLGG VVSLAHTAII IIGFFSLFSG ILPFNLDVDQ
TFIAAILTII GYAINDNVVI FDRIREMRGL HPNMDFKEGV NKALNATLTR TVNTSVSTLL
PMLAIAIFGG ESIRGLSVAL CLGIVIGTYA SLMIGTPVMF DATRKASKK
//