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Database: UniProt
Entry: A0A3R8TD24_9BURK
LinkDB: A0A3R8TD24_9BURK
Original site: A0A3R8TD24_9BURK 
ID   A0A3R8TD24_9BURK        Unreviewed;       338 AA.
AC   A0A3R8TD24;
DT   10-APR-2019, integrated into UniProtKB/TrEMBL.
DT   10-APR-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
DE   RecName: Full=Protein-export membrane protein SecF {ECO:0000256|HAMAP-Rule:MF_01464};
GN   Name=secF {ECO:0000256|HAMAP-Rule:MF_01464,
GN   ECO:0000313|EMBL:RRS04924.1};
GN   ORFNames=EIP75_08095 {ECO:0000313|EMBL:RRS04924.1};
OS   Aquabacterium soli.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Aquabacterium.
OX   NCBI_TaxID=2493092 {ECO:0000313|EMBL:RRS04924.1, ECO:0000313|Proteomes:UP000269265};
RN   [1] {ECO:0000313|EMBL:RRS04924.1, ECO:0000313|Proteomes:UP000269265}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SJQ9 {ECO:0000313|EMBL:RRS04924.1,
RC   ECO:0000313|Proteomes:UP000269265};
RA   Sun L., Gao X., Chen W., Huang K.;
RT   "The whole draft genome of Aquabacterium sp. SJQ9.";
RL   Submitted (DEC-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_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-YajC and YidC. {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:RRS04924.1}.
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DR   EMBL; RSED01000005; RRS04924.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A3R8TD24; -.
DR   OrthoDB; 9774769at2; -.
DR   Proteomes; UP000269265; 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; IPR022646; SecD/SecF_CS.
DR   InterPro; IPR048634; SecD_SecF_C.
DR   InterPro; IPR005665; SecF_bac.
DR   InterPro; IPR000731; SSD.
DR   NCBIfam; TIGR00916; 2A0604s01; 1.
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.
DR   PROSITE; PS50156; SSD; 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:UP000269265};
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..35
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   TRANSMEM        159..176
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   TRANSMEM        183..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   TRANSMEM        210..231
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   TRANSMEM        262..279
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   TRANSMEM        285..314
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   DOMAIN          179..311
FT                   /note="SSD"
FT                   /evidence="ECO:0000259|PROSITE:PS50156"
SQ   SEQUENCE   338 AA;  37397 MW;  FD07830CFF654CD8 CRC64;
     MEFFRIKRDI PFMRHALVFN IISFLTFAAA VFFLVTRGLH FSIEFTGGSV LEMQYAQSAD
     LAKTRHAVET LNFGEVQVQN FGTSRDVLVR VPLREGMKQS EVVSKVFDAV CKAENGTVSQ
     LKTDHGDKPV CQAGASEPVS LQRSEFVGPQ VGSELARDGA LALLVTVVGI MAYLAFRFEW
     KFAVAGVIAN LHDVVIILGF FAYFQWEFSL SVLAAILAVL GYSVNESVVI FDRIREAFRR
     FRKLNTSEVI DHAITSTMSR TIITHLSTQM MVTSMLIFGG PTLHYFALAL TIGILFGIYS
     SVFVAAALAM WLGVKREDLM KNTKKETDPN DPNAGAVV
//
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