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Database: UniProt
Entry: A0A4R6UM53_9BURK
LinkDB: A0A4R6UM53_9BURK
Original site: A0A4R6UM53_9BURK 
ID   A0A4R6UM53_9BURK        Unreviewed;       316 AA.
AC   A0A4R6UM53;
DT   31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT   31-JUL-2019, sequence version 1.
DT   24-JAN-2024, entry version 11.
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=DFR43_10358 {ECO:0000313|EMBL:TDQ44314.1};
OS   Tepidicella xavieri.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales; Tepidicella.
OX   NCBI_TaxID=360241 {ECO:0000313|EMBL:TDQ44314.1, ECO:0000313|Proteomes:UP000295510};
RN   [1] {ECO:0000313|EMBL:TDQ44314.1, ECO:0000313|Proteomes:UP000295510}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 19605 {ECO:0000313|EMBL:TDQ44314.1,
RC   ECO:0000313|Proteomes:UP000295510};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT   most valuable type-strain genomes for metagenomic binning, comparative
RT   biology and taxonomic classification.";
RL   Submitted (MAR-2019) 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:TDQ44314.1}.
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DR   EMBL; SNYL01000003; TDQ44314.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A4R6UM53; -.
DR   OrthoDB; 9774769at2; -.
DR   Proteomes; UP000295510; 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   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.
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:UP000295510};
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        137..154
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   TRANSMEM        161..182
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   TRANSMEM        188..212
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   TRANSMEM        248..266
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   TRANSMEM        272..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   DOMAIN          108..291
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
SQ   SEQUENCE   316 AA;  35075 MW;  5C1C2E30B7105F81 CRC64;
     MEFFRIKKDI PFMRHAVLLN AISITAFVLA VFFLVTRGLN LSVEFTGGTV IEVAYEQPAD
     LPAIRQVIAG LGYTEVPVQN FGTSRDVLMR LPLMEGQTSG QQSEIVLAAL RAHDPTVELR
     RTEYVGPQVG RELAEDGLMA LAFVILGIMV YLAFRFEWKY AVAAIVANLH DVVIVLGFFA
     FFQWEFSLAV LAAVLAVLGY SVNESVVIFD RIRETFRRQR KMTTREVIDH AITRTMSRTA
     ITHGSTEVMV VSMLLFGGPT LFYFALALTI GILFGIYSSI FVASAVAMWL GVRREDLVKP
     TRKVEDPDDP NAGAAV
//
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