ID A0A0G1TD27_9BACT Unreviewed; 734 AA.
AC A0A0G1TD27;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
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 ECO:0000313|EMBL:KKU43335.1};
GN Synonyms=secD {ECO:0000256|HAMAP-Rule:MF_01463};
GN ORFNames=UX61_C0023G0001 {ECO:0000313|EMBL:KKU43335.1};
OS Parcubacteria group bacterium GW2011_GWA2_46_7.
OC Bacteria.
OX NCBI_TaxID=1618837 {ECO:0000313|EMBL:KKU43335.1, ECO:0000313|Proteomes:UP000034469};
RN [1] {ECO:0000313|EMBL:KKU43335.1, ECO:0000313|Proteomes:UP000034469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(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}.
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:KKU43335.1}.
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DR EMBL; LCMW01000023; KKU43335.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G1TD27; -.
DR PATRIC; fig|1618837.3.peg.381; -.
DR Proteomes; UP000034469; 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; 3.30.70.3400; -; 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; 1.
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};
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 12..35
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 294..311
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 318..338
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 344..365
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 418..445
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 561..580
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 592..618
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 624..645
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 676..693
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT TRANSMEM 699..724
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT DOMAIN 91..148
FT /note="Protein translocase subunit SecDF P1"
FT /evidence="ECO:0000259|Pfam:PF21760"
FT DOMAIN 275..443
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
FT DOMAIN 533..726
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 734 AA; 80972 MW; 18CD93064314B28E CRC64;
MISVLIQEKK KAFALIAAIF VLAIGATVFA FPGLVNTGIS WVSGKIGVSA PSFHVPGFRL
GLDVSGGTSL IYRADVAGLS NNDRITALDG LKDVIERRIN LFGVQEPRIE VSRSGDEWRL
IVELAGIKDI AQAIEMIGQT PFLQFWQEQA GKSSEELFEK YKPEETLLHF EEYFEATELT
GRFLKRAEVV FDQTSSIPAV SLVFDEEGAK VFKDLTTKNL NKPLAITIDG IPLSAPIVGD
VITDGHAQIT GRFSLAQAKD LANNLNQGAL PVPITLISQR SVGATLGNDS LNKMVYAGII
GFITIAVFMV LSYRLGGLFS VVALLIYIPL TLAIFKLVGV TLTLSGIAGF LLSMGMAVDA
NILILERIKE ELRSGKEVVH AIREGFLRAW PSIRDSNVSS IITALVLYFF TASIVRGFAL
TLLIGVVTSM FSAIFVSRTL IMAFLGEKSG HSKFWFGVRM KEMEDSGLKP GIDFTGGALW
EFKFGNPMDK IVLEQQLETI MKTDVLISES SDGIFSARMK EFSEQEHQGF VQELEKSDES
FEELRWETVG PTVGKTLRDK SMVAIVMVVV GISVYIAFAF RKASYPVSSI KYGLITVLTL
FHDVIIPIGA FCALAYFQHV EIDTNFVVAI LVIMGFSVHD TIVVFDRVRE KLMRFNGKDF
GALVNESLNE TLVRSFNTSL TVVFVLLAMF FWGGAVLKYF ILAMLIGMIV GMYSSIFIAS
PLLVDVWKWQ QKRK
//
