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Database: UniProt
Entry: D4K6H7_9FIRM
LinkDB: D4K6H7_9FIRM
Original site: D4K6H7_9FIRM 
ID   D4K6H7_9FIRM            Unreviewed;       777 AA.
AC   D4K6H7;
DT   18-MAY-2010, integrated into UniProtKB/TrEMBL.
DT   18-MAY-2010, sequence version 1.
DT   24-JAN-2024, entry version 64.
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   ORFNames=FPR_31230 {ECO:0000313|EMBL:CBL03186.1};
OS   Faecalibacterium prausnitzii SL3/3.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Faecalibacterium.
OX   NCBI_TaxID=657322 {ECO:0000313|EMBL:CBL03186.1, ECO:0000313|Proteomes:UP000007059};
RN   [1] {ECO:0000313|EMBL:CBL03186.1, ECO:0000313|Proteomes:UP000007059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL3/3 {ECO:0000313|EMBL:CBL03186.1,
RC   ECO:0000313|Proteomes:UP000007059};
RG   metaHIT consortium -- http://www.metahit.eu/;
RA   Pajon A., Turner K., Parkhill J., Duncan S., Flint H.;
RT   "The genome sequence of Faecalibacterium prausnitzii SL3/3.";
RL   Submitted (MAR-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:CBL03186.1, ECO:0000313|Proteomes:UP000007059}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SL3/3 {ECO:0000313|EMBL:CBL03186.1,
RC   ECO:0000313|Proteomes:UP000007059};
RA   Pajon A.;
RL   Submitted (MAR-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 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; FP929046; CBL03186.1; -; Genomic_DNA.
DR   RefSeq; WP_005925684.1; NC_021020.1.
DR   AlphaFoldDB; D4K6H7; -.
DR   GeneID; 75068892; -.
DR   KEGG; fpa:FPR_31230; -.
DR   PATRIC; fig|657322.3.peg.3003; -.
DR   eggNOG; COG0341; Bacteria.
DR   eggNOG; COG0342; Bacteria.
DR   HOGENOM; CLU_007894_3_0_9; -.
DR   Proteomes; UP000007059; 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; 3.30.70.3400; -; 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; IPR048634; SecD_SecF_C.
DR   InterPro; IPR005665; SecF_bac.
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; 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        267..287
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        294..315
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        327..346
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        367..392
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        418..444
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        483..505
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        636..656
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        662..683
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        715..737
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        743..769
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   DOMAIN          250..391
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
FT   DOMAIN          584..771
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
SQ   SEQUENCE   777 AA;  82720 MW;  6879022C42728B0E CRC64;
     MKTKGKAWQL VVTALLIVVF VYTAFFGVAA KYGDVTTTYI KGAKDIRFGV DIKGGVNVTF
     VPSDGYDATD EQLDAARLVI ENRLVALNVT DYELYVDNNS DSLILEFPWQ SGETDFDPES
     AIQEIGTTAY LTFREGASKD GELILDGSMV ESASAQYGAV SNGGSSEYYV ALKFTTEGAK
     AFGDATTKLA ADKGSISIWL DDENVSTATV NTAITDGQAI ITSSASNPFT QDAVVKMARQ
     INSGALPFAL SVDSYSTVSP SLGENSLGAM VLAGLIAFAL IVVFMTVLYR LPGFLACIAL
     AGQVAATLAF VSGYFPVFES FTLTLPGIAG IILAIGMGVD ANVITAERIK EELKNGKSLD
     GALKSGFARG LTPIIDGNVT IVIVAIVLMG AFGPSDGLFA KALHFVFFAF GPSTAGTIYA
     FGYTLLTGVL LNFVFGVFAT RVMIRGAAAI KALRNPWLYG AAKPGQEKAE KKPVDFVSLR
     KKFLTFSACL MAVILLCAAV FGVHLDTEFT GGAMITLSYE GGFDQAAVQK TAAAALENTG
     LTLQTGENVA TGDQTLKISM PGTETVTTEQ VENLLDSLNE NYPDNQFAQL SLSNVSAAMG
     TKFLQKSLVA VVFALVLILL YIALRFKNIG GLTGGMMAVL ALVNDLMVVF GTFVLLRTAL
     DGNFIAAMLT ILGYSINDTV VVYDRIRENR ALMGKKGSFE ELVNQSVNQS ARRTLITTIT
     TVMALGVMCI VAKLYGLDSI FTFAFPLMMG MISGVYTSLC VSTSAWVLWS ERSKKKN
//
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