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Database: UniProt
Entry: A0A174CTL0_9FIRM
LinkDB: A0A174CTL0_9FIRM
Original site: A0A174CTL0_9FIRM 
ID   A0A174CTL0_9FIRM        Unreviewed;       802 AA.
AC   A0A174CTL0;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   24-JAN-2024, entry version 38.
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=secDF {ECO:0000313|EMBL:CUO15170.1};
GN   Synonyms=secD {ECO:0000256|HAMAP-Rule:MF_01463}, secF
GN   {ECO:0000256|HAMAP-Rule:MF_01464};
GN   ORFNames=DWX77_03480 {ECO:0000313|EMBL:RGS75620.1}, DXB38_09205
GN   {ECO:0000313|EMBL:RGN87427.1}, ERS852394_01577
GN   {ECO:0000313|EMBL:CUO15170.1};
OS   Blautia obeum.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX   NCBI_TaxID=40520 {ECO:0000313|EMBL:CUO15170.1, ECO:0000313|Proteomes:UP000095409};
RN   [1] {ECO:0000313|EMBL:CUO15170.1, ECO:0000313|Proteomes:UP000095409}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=2789STDY5608837 {ECO:0000313|EMBL:CUO15170.1,
RC   ECO:0000313|Proteomes:UP000095409};
RG   Pathogen Informatics;
RL   Submitted (SEP-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000261105, ECO:0000313|Proteomes:UP000284242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AF21-24 {ECO:0000313|EMBL:RGS75620.1,
RC   ECO:0000313|Proteomes:UP000284242}, and OM03-6
RC   {ECO:0000313|EMBL:RGN87427.1, ECO:0000313|Proteomes:UP000261105};
RA   Zou Y., Xue W., Luo G.;
RT   "A genome reference for cultivated species of the human gut microbiota.";
RL   Submitted (AUG-2018) 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; CYZD01000006; CUO15170.1; -; Genomic_DNA.
DR   EMBL; QSUZ01000010; RGN87427.1; -; Genomic_DNA.
DR   EMBL; QRVV01000005; RGS75620.1; -; Genomic_DNA.
DR   RefSeq; WP_005426487.1; NZ_QSRF01000010.1.
DR   AlphaFoldDB; A0A174CTL0; -.
DR   GeneID; 79803550; -.
DR   Proteomes; UP000095409; Unassembled WGS sequence.
DR   Proteomes; UP000261105; Unassembled WGS sequence.
DR   Proteomes; UP000284242; 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; IPR004869; MMPL_dom.
DR   InterPro; IPR005791; SecD.
DR   InterPro; IPR022813; SecD/SecF_arch_bac.
DR   InterPro; IPR022645; SecD/SecF_bac.
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; PF03176; MMPL; 1.
DR   Pfam; PF21760; SecD_1st; 1.
DR   Pfam; PF02355; SecD_SecF; 1.
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:UP000095409};
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        269..290
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        297..317
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        323..347
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        368..390
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        396..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        451..470
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        578..595
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        602..623
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        629..651
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        681..699
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   TRANSMEM        705..730
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01463"
FT   DOMAIN          67..121
FT                   /note="Protein translocase subunit SecDF P1"
FT                   /evidence="ECO:0000259|Pfam:PF21760"
FT   DOMAIN          188..413
FT                   /note="Membrane transport protein MMPL"
FT                   /evidence="ECO:0000259|Pfam:PF03176"
FT   DOMAIN          551..732
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
FT   REGION          746..802
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        748..764
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   802 AA;  86087 MW;  8ECCD73229866094 CRC64;
     MKKSKGIVVL LLTAIITVFL CYTAGIGLGP TGTGSAKNIK TGLDLSGGVS ITYQAKDSNP
     SAEDMSDTVY KLQKRVEQYS TEAQVYKEGS DRIAVEIPGV TDADAILNDL GKPGSLCFIT
     MTDDDGNANF SSTGSGYVLA RSLDEIRESG SVVLEGTDVK DAQGGAFQSD KNSSREYAVS
     LTLTDEGKTK FADATEANVG KQIAIVYDNQ ILSAPKVNEA ITGGQAQITG MSSVEEAQNL
     ASYIRIGSLS IELEELRSSV VAAQLGEEAI STSVMAGLIG LVIVIIFMII MYRLPGVVAG
     VALILYTAIV LITLNAFDIT LTLPGIAGII LGIGMAVDAN VIIYARIQEE IAAGNSVRAS
     IKSGFSKAFS AIFDGNITTL IASLVLMWLG SGTVKGFAYT LALGIVVSMF TALVVSRFVM
     NALYAVGFHD EKFYGRAKQR KVFNVVGKRK VFFIISIILI LSGPVAMAIH HNVDGTALNY
     ALDFSGGTAT TVTFNEDMDI KQIDSEVTPV VEEVTGDKNV QPTKVVGTNQ VVIKTRTLSQ
     EEREKLDNAL VEKFNVDDSL ITTESISSTV SSEMRRDAVV AVIVATLCML AYIWFRFKDI
     RFASSAVLAL LHDVLVVFAF YGISRISVGN TFIACMLTIV GYSINATIVI FDRIRENTKG
     SRSNLEEIVN ESITQTLTRS MYTSFTTFVM VAVLYIMGVS SIREFAAPLM VGVICGAYSS
     VCITGALWLV MKRYYKKPVA QAVAAKNTAA PAKQNNNSQD TKSGKKNSDQ PKKKNRKRVA
     ERLAAQEAAA KENASNDENK DA
//
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