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Database: UniProt
Entry: A0A1M6K4P2_9FIRM
LinkDB: A0A1M6K4P2_9FIRM
Original site: A0A1M6K4P2_9FIRM 
ID   A0A1M6K4P2_9FIRM        Unreviewed;       318 AA.
AC   A0A1M6K4P2;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   24-JAN-2024, entry version 17.
DE   RecName: Full=Protein-export membrane protein SecF {ECO:0000256|HAMAP-Rule:MF_01464};
GN   Name=secF {ECO:0000256|HAMAP-Rule:MF_01464};
GN   ORFNames=SAMN05444373_10688 {ECO:0000313|EMBL:SHJ53875.1};
OS   Thermoclostridium caenicola.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Thermoclostridium.
OX   NCBI_TaxID=659425 {ECO:0000313|EMBL:SHJ53875.1, ECO:0000313|Proteomes:UP000324781};
RN   [1] {ECO:0000313|EMBL:SHJ53875.1, ECO:0000313|Proteomes:UP000324781}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19027 {ECO:0000313|EMBL:SHJ53875.1,
RC   ECO:0000313|Proteomes:UP000324781};
RA   Varghese N., Submissions S.;
RL   Submitted (NOV-2016) 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_01464}.
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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_01464};
CC       Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01464}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the SecD/SecF family. SecF subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_01464}.
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DR   EMBL; FQZP01000068; SHJ53875.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M6K4P2; -.
DR   OrthoDB; 9805019at2; -.
DR   Proteomes; UP000324781; 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; 1.20.1640.10; Multidrug efflux transporter AcrB transmembrane domain; 1.
DR   HAMAP; MF_01464_B; SecF_B; 1.
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:SF8; PROTEIN TRANSLOCASE SUBUNIT SECF; 1.
DR   PANTHER; PTHR30081; PROTEIN-EXPORT MEMBRANE PROTEIN SEC; 1.
DR   Pfam; PF02355; SecD_SecF; 1.
DR   PRINTS; PR01755; SECFTRNLCASE.
DR   SUPFAM; SSF82866; Multidrug efflux transporter AcrB transmembrane domain; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_01464};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01464};
KW   Protein transport {ECO:0000256|ARBA:ARBA00022927, ECO:0000256|HAMAP-
KW   Rule:MF_01464}; Reference proteome {ECO:0000313|Proteomes:UP000324781};
KW   Translocation {ECO:0000256|ARBA:ARBA00023010, ECO:0000256|HAMAP-
KW   Rule:MF_01464};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW   Rule:MF_01464};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW   Rule:MF_01464};
KW   Transport {ECO:0000256|ARBA:ARBA00022448, ECO:0000256|HAMAP-Rule:MF_01464}.
FT   TRANSMEM        12..30
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   TRANSMEM        144..161
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   TRANSMEM        168..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   TRANSMEM        199..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   TRANSMEM        255..273
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   TRANSMEM        279..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   DOMAIN          126..306
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
SQ   SEQUENCE   318 AA;  34859 MW;  9CC06F360B68E530 CRC64;
     MTRFDFVKNR KIFFTISGVL LLIFLVLYLI NGAVLDITFR GGTRMSIECE QMVDANLAAV
     RLEAALNKKV NTSVMETVSG SQGTAKKTIM LRIDVASQTP LTPDEEQLVR DTLVKEGFPV
     ILDSPNNEVV SIEPSIGKET LGKGLLAVLI SSVLILIYVA WRFSIMSGFS AAVCAVIALL
     HDCAVMLGVY VAFRLPFNDV FIAAILTIIG YSINDTIIVY DRIRENAKVM QKSEIGTIVN
     VSIWQTLSRT INTTLTTLLS VAVLYIFSAA NNITSLKGFS FSLIIGCISG TYSSVFIAAN
     LWHWLRTIRL KAKTASAK
//
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