ID A0A1F8SNJ3_9CHLR Unreviewed; 306 AA.
AC A0A1F8SNJ3;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
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=A2Z36_01760 {ECO:0000313|EMBL:OGO61433.1};
OS Chloroflexi bacterium RBG_19FT_COMBO_48_23.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797666 {ECO:0000313|EMBL:OGO61433.1, ECO:0000313|Proteomes:UP000180540};
RN [1] {ECO:0000313|EMBL:OGO61433.1, ECO:0000313|Proteomes:UP000180540}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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}.
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:OGO61433.1}.
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DR EMBL; MGOH01000020; OGO61433.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8SNJ3; -.
DR Proteomes; UP000180540; 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; 3.30.70.2040; -; 1.
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; IPR022646; SecD/SecF_CS.
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; PF07549; Sec_GG; 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};
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 9..31
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 125..144
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 156..179
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 185..206
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 237..255
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 261..287
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT DOMAIN 101..289
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
SQ SEQUENCE 306 AA; 32817 MW; 6C9EB2F5F70F5B1A CRC64;
MIDLVGKRLW FFLISAIVII PGIISLAVFG LKPGVDFSSG TAMTLSFDKG VELSQLRQEL
TDLGYDRAVV QPAGEEEFFI RLPEISAEEN TRLKEGLETG LDAKLTISSL YSVSPVVAAG
TVRNTIIAIV VASVGILLYI SWAFRKMPNP IRWGTCAVIA LVHDLVVVIA VFSILGWVAG
VEVDALFVTG VLAVVGVSVN NIVVVFDRIR ENVKRGVSRD FEVTANCGIT ESLGRSLNTG
LATLFVIVAL FLLGGTTTHN LVLALLIGIA TGIYSSLCIA GQLLVVWEKG NWGRLSSLRN
QVETSA
//
