ID A0A0T5ZFE1_9CHLR Unreviewed; 378 AA.
AC A0A0T5ZFE1;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
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=XU10_C0043G0010 {ECO:0000313|EMBL:KRT61342.1};
OS Chloroflexi bacterium CSP1-4.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1640513 {ECO:0000313|EMBL:KRT61342.1, ECO:0000313|Proteomes:UP000051896};
RN [1] {ECO:0000313|EMBL:KRT61342.1, ECO:0000313|Proteomes:UP000051896}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CSP1-4 {ECO:0000313|EMBL:KRT61342.1};
RA Hug L.A., Thomas B.C., Sharon I., Brown C.T., Sharma R., Hettich R.L.,
RA Wilkins M.J., Williams K.H., Singh A., Banfield J.F.;
RT "Critical biogeochemical functions in the subsurface are associated with
RT bacteria from new phyla and little studied lineages.";
RL Submitted (MAY-2015) 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}.
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:KRT61342.1}.
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DR EMBL; LDXM01000043; KRT61342.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0T5ZFE1; -.
DR STRING; 1640513.XU10_C0043G0010; -.
DR PATRIC; fig|1640513.3.peg.2387; -.
DR Proteomes; UP000051896; 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};
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..31
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 197..216
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 228..251
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 257..278
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 309..327
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT TRANSMEM 333..359
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT DOMAIN 183..361
FT /note="Protein export membrane protein SecD/SecF C-
FT terminal"
FT /evidence="ECO:0000259|Pfam:PF02355"
FT REGION 100..161
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 105..141
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 378 AA; 39613 MW; 69EA751719B8E573 CRC64;
MFDLIGKRRW FFLFSGLITI PGLIFIILTP FSGGKAGLSF SIDYTGGTIW EVHFRDGTPD
PTAVLAVLAD QDLKESAVVL TEGPKGEYVR LTMPPIGLIE AQATPTPGPT LSPGASVSAS
PSVDASGSPS ASASPATSPG AEPSASPSPS PTPASAGIEL PTTGKPGEVA AALEAAFGPI
DDVSQATAVG PVVSRDLINQ ALLLILAGSA GILAWITVRF HDLRMGVAAL VALLHDIIVV
VGVFAILGTF FGVQIDALFV TAMLTIIGFS VHDTIVVFDR VRENRFRHAG EPFSAIVNHS
LLQTLGRSIN TSMTVVLTLT ALLLFGGEAI RVFVLALLIG IVSGTYSSIF NASPLLVVWH
ERDERRRQAQ LTAARAVR
//
