ID A0A0S7C6I3_9BACT Unreviewed; 1048 AA.
AC A0A0S7C6I3;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 35.
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=TBC1_12636 {ECO:0000313|EMBL:GAP44825.1};
OS Lentimicrobium saccharophilum.
OC Bacteria; Bacteroidota; Bacteroidia; Bacteroidales; Lentimicrobiaceae;
OC Lentimicrobium.
OX NCBI_TaxID=1678841 {ECO:0000313|EMBL:GAP44825.1};
RN [1] {ECO:0000313|EMBL:GAP44825.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TBC1 {ECO:0000313|EMBL:GAP44825.1};
RA Tourlousse D.M., Matsuura N., Sun L., Toyonaga M., Kuroda K., Ohashi A.,
RA Cruz R., Yamaguchi T., Sekiguchi Y.;
RT "Draft Genome Sequence of Bacteroidales Strain TBC1, a Novel Isolate from a
RT Methanogenic Wastewater Treatment System.";
RL Genome Announc. 3:e01168-15(2015).
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; DF968183; GAP44825.1; -; Genomic_DNA.
DR RefSeq; WP_062044697.1; NZ_DF968183.1.
DR AlphaFoldDB; A0A0S7C6I3; -.
DR STRING; 1678841.TBC1_12636; -.
DR PATRIC; fig|1678841.3.peg.3370; -.
DR OrthoDB; 9805019at2; -.
DR Proteomes; UP000053091; 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:UP000053091};
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 550..567
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 574..597
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 603..624
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 645..667
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 673..697
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 732..749
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 868..886
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 898..921
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 927..948
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 979..997
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 1003..1030
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 204..261
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 530..699
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
FT DOMAIN 851..1030
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
FT REGION 298..318
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1048 AA; 115836 MW; C889F350C10B2DD3 CRC64;
MQNKGAIKFF AIALAIVCLF QLSFTFFTKR VEKKAREYSR NEAAISQAKE LAGGNTLLEQ
KLMDSISKSR ERYYLDSMSG QPVFNILVRK YTYQECKERE LNLGLDLKGG MNVTLEVSVV
DIVRALSGYS TNPVFTQAVD MALQKQKNSQ SDFVTLFGES FQEIDPNASL AAIFNTVELK
DRISYNSTNS EVLDVIRQET KGAIDRTFNI LRTRIDRFGV AQPNIQQLQT AGRILVELPG
IKEPERVRKL LQGTAQLEFW ETYQFAELVP YFEEANKRLA SITSEGAMAD STVADTTTTA
AGEVPQTEQT TPADTTATAQ ADTAQSTLLD KISDTTAADQ QKESFEKYAK ENPLFAYLNP
AIFPNAQGQY FPGEGATVGF ATIKDTARVN RMLRQTASIF PRDLKMAWTV KPEKDRPEIL
ELIALKVTSR DGLAPLGGDA VVDARQDYDQ NGRVEITMLM NAEGAKTWKR LTADNIGNQI
AIVLDDYVYS APRVNSEIPN GRSSITGNFS IEEAQDLANI LKAGKLPAPA RIVQEEVVGP
SLGRESINSG LTSFVIAFVL VLIYMVLYYN RAGWVADLAL VTNIFFIFGV LTSLGAVLTL
PGIAGIVLTL GMAVDSNVII YERVREELRA GKGLRLAITD GYNNAYSAII DGNVTTLLTG
IVLNIFGSGP VQGFATTLII GIITSLFTSI FISRIIFEWQ LRKNRNIPFD NQYTRYAFTK
VNFDFIGLRK KMYIASGIVI LIGIISLATK GLNFGVDFSG GRTYVIRFDK EVGTNEVRSL
LADEFGEAPE VKTFGSSNQV KITTKYMIEE DTQAADSIVE AKIFNGVKGL YDTPMNFNDF
TADDETKVLG RLSSQKVGPT IADDIKQGAV LAVFFALLII FIYIAIRFKK WQYGMGGLVA
LAHDTMITIS LYSIFSGILP FNLEVDQAFI AALLTIIGYS INDTVIIFDR IREYVGLYPK
RVISDNMNHA MNSTLGRTFN TAGTTLVVLI AIFIFGGEVI RGFVFALMVG IAIGTYSSIF
VASPIAYDFI TNSQKRRKRK EEAKKLQK
//
