GenomeNet

Database: UniProt
Entry: A0A2W7HTU8_9PROT
LinkDB: A0A2W7HTU8_9PROT
Original site: A0A2W7HTU8_9PROT 
ID   A0A2W7HTU8_9PROT        Unreviewed;       325 AA.
AC   A0A2W7HTU8;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 13.
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=C8P66_14410 {ECO:0000313|EMBL:PZW37647.1};
OS   Humitalea rosea.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Humitalea.
OX   NCBI_TaxID=990373 {ECO:0000313|EMBL:PZW37647.1, ECO:0000313|Proteomes:UP000249688};
RN   [1] {ECO:0000313|EMBL:PZW37647.1, ECO:0000313|Proteomes:UP000249688}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 24525 {ECO:0000313|EMBL:PZW37647.1,
RC   ECO:0000313|Proteomes:UP000249688};
RA   Goeker M.;
RT   "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT   (KMG-II): from individual species to whole genera.";
RL   Submitted (JUN-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: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {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:PZW37647.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; QKYU01000044; PZW37647.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2W7HTU8; -.
DR   Proteomes; UP000249688; 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:UP000249688};
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        146..166
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   TRANSMEM        173..193
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   TRANSMEM        199..221
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   TRANSMEM        253..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   TRANSMEM        276..303
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01464"
FT   DOMAIN          122..305
FT                   /note="Protein export membrane protein SecD/SecF C-
FT                   terminal"
FT                   /evidence="ECO:0000259|Pfam:PF02355"
SQ   SEQUENCE   325 AA;  35288 MW;  94EACC3A651B90EF CRC64;
     MIAMFERLSR PLFRLVPDNT HIPFMRGRIA GLAFSALLSV ASVVLAITPG LEKGIDFKGG
     ITMEVRTPGP ADLPTIRTAL ARLPFGDVGV QQFGDPTTLL LRLPTQGEEA QTQAAVAATR
     STIEQVAPGV RILRVEAVGN RVSDELFQGG MIALGLSLLA MMLYIWFRFE WQFGVGAVVT
     LILEVTKVIG FLAVTRIEFN LTTVAAVLTI VGFSVNDKVV VYDRMRENLR RFKTMPLREL
     IDRSINETLN RTLGTSMTLL LAALPLALFG GDTLAGFAWC MLFGIVISAS SSIFIAAPIL
     LFLGENRLRR GTEAVAAPVK AAPRT
//
DBGET integrated database retrieval system