ID   SECF_ECOL6              Reviewed;         323 AA.
AC   P0AG94; P19674; P77113;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   25-MAY-2022, entry version 95.
DE   RecName: Full=Protein translocase subunit SecF;
GN   Name=secF {ECO:0000255|HAMAP-Rule:MF_01464}; OrderedLocusNames=c0519;
OS   Escherichia coli O6:H1 (strain CFT073 / ATCC 700928 / UPEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=199310;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CFT073 / ATCC 700928 / UPEC;
RX   PubMed=12471157; DOI=10.1073/pnas.252529799;
RA   Welch R.A., Burland V., Plunkett G. III, Redford P., Roesch P., Rasko D.,
RA   Buckles E.L., Liou S.-R., Boutin A., Hackett J., Stroud D., Mayhew G.F.,
RA   Rose D.J., Zhou S., Schwartz D.C., Perna N.T., Mobley H.L.T.,
RA   Donnenberg M.S., Blattner F.R.;
RT   "Extensive mosaic structure revealed by the complete genome sequence of
RT   uropathogenic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:17020-17024(2002).
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:0000255|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:0000255|HAMAP-Rule:MF_01464}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_01464}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_01464}.
CC   -!- SIMILARITY: Belongs to the SecD/SecF family. SecF subfamily.
CC       {ECO:0000255|HAMAP-Rule:MF_01464}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAN78997.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE014075; AAN78997.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_000046637.1; NC_004431.1.
DR   AlphaFoldDB; P0AG94; -.
DR   SMR; P0AG94; -.
DR   STRING; 199310.c0519; -.
DR   EnsemblBacteria; AAN78997; AAN78997; c0519.
DR   GeneID; 67416518; -.
DR   KEGG; ecc:c0519; -.
DR   eggNOG; COG0341; Bacteria.
DR   HOGENOM; CLU_050012_1_0_6; -.
DR   OMA; AFEWRMA; -.
DR   Proteomes; UP000001410; Chromosome.
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..323
FT                   /note="Protein translocase subunit SecF"
FT                   /id="PRO_0000095978"
FT   TOPO_DOM        1..22
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        23..43
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT   TOPO_DOM        44..142
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        143..163
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT   TOPO_DOM        164..170
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        171..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT   TOPO_DOM        192..196
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        197..217
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT   TOPO_DOM        218..247
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        248..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT   TOPO_DOM        271..280
FT                   /note="Periplasmic"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        281..301
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01464"
FT   TOPO_DOM        302..323
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   323 AA;  35382 MW;  9662196085448643 CRC64;
     MAQEYTVEQL NHGRKVYDFM RWDYWAFGIS GLLLIAAIVI MGVRGFNWGL DFTGGTVIEI
     TLEKPAEIDV MRDALQKAGF EEPMLQNFGS SHDIMVRMPP AEGETGGQVL GSQVLKVINE
     STNQNAAVKR IEFVGPSVGA DLAQTGAMAL MAALLSILVY VGFRFEWRLA AGVVIALAHD
     VIITLGILSL FHIEIDLTIV ASLMSVIGYS LNDSIVVSDR IRENFRKIRR GTPYEIFNVS
     LTQTLHRTLI TSGTTLMVIL MLYLFGGPVL EGFSLTMLIG VSIGTASSIY VASALALKLG
     MKREHMLQQK VEKEGADQPS ILP