ID   SECF_KETVY              Reviewed;         329 AA.
AC   E3F0U0;
DT   21-SEP-2011, integrated into UniProtKB/Swiss-Prot.
DT   21-SEP-2011, sequence version 2.
DT   25-MAY-2022, entry version 46.
DE   RecName: Full=Protein translocase subunit SecF;
GN   Name=secF; OrderedLocusNames=EIO_1371;
OS   Ketogulonicigenium vulgare (strain Y25).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Roseobacteraceae; Ketogulonicigenium.
OX   NCBI_TaxID=880591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Y25;
RX   PubMed=21037005; DOI=10.1128/jb.01189-10;
RA   Xiong X.H., Han S., Wang J.H., Jiang Z.H., Chen W., Jia N., Wei H.L.,
RA   Cheng H., Yang Y.X., Zhu B., You S., He J.Y., Hou W., Chen M.X., Yu C.J.,
RA   Jiao Y.H., Zhang W.C.;
RT   "Complete genome sequence of the bacterium Ketogulonicigenium vulgare
RT   Y25.";
RL   J. Bacteriol. 193:315-316(2011).
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 (By similarity). {ECO:0000250}.
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 (By similarity). {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000250}; Multi-pass
CC       membrane protein {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the SecD/SecF family. SecF subfamily.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=ADO42505.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; CP002224; ADO42505.1; ALT_FRAME; Genomic_DNA.
DR   AlphaFoldDB; E3F0U0; -.
DR   SMR; E3F0U0; -.
DR   EnsemblBacteria; ADO42505; ADO42505; EIO_1371.
DR   KEGG; kvu:EIO_1371; -.
DR   HOGENOM; CLU_129894_0_0_5; -.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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   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; IPR005665; SecF_bac.
DR   PANTHER; PTHR30081; PTHR30081; 1.
DR   Pfam; PF07549; Sec_GG; 1.
DR   Pfam; PF02355; SecD_SecF; 1.
DR   PRINTS; PR01755; SECFTRNLCASE.
DR   TIGRFAMs; TIGR00916; 2A0604s01; 1.
DR   TIGRFAMs; TIGR00966; 3a0501s07; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane; Cell membrane; Membrane; Protein transport;
KW   Translocation; Transmembrane; Transmembrane helix; Transport.
FT   CHAIN           1..329
FT                   /note="Protein translocase subunit SecF"
FT                   /id="PRO_0000412697"
FT   TRANSMEM        27..47
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        149..169
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        177..197
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        204..224
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        256..276
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        279..299
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   329 AA;  35652 MW;  741089EC5567113E CRC64;
     MAFRLKLVPD KTSVNFFKWG GIPTHATFAL ALASLIAVMT IGLNYGIDFL GGTTIRAESS
     ENVAVSEYRS ALDQIELGDV TITEVFDPGF RADQFVKQVR IQAANETEVS NALIGQVEAA
     LQVVDPQVVF TAVETVGPKV SGELIQTAVL AAVLAVAASL LGIMAYVWLR FEWQFGFGAV
     VGLFTDAMIT VGLFSVFQVR FDLTIVAAVL TIVGFSINDK VVVFDRVREI LRRDSTTPLP
     ELMVVALNET LSRTVMTTVT TILALVALYI WGGDVIRGFA FAMLFGSVIA VYSTIFVSAQ
     VVLWLGVKRD WEKKTDTGPS GTQFTTSAE