(data stored in ACNUC7421 zone)

SWISSPROT: SECF_ECO57

ID   SECF_ECO57              Reviewed;         323 AA.
AC   P0AG95; P19674; P77113;
DT   20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT   20-DEC-2005, sequence version 1.
DT   05-JUL-2017, entry version 82.
DE   RecName: Full=Protein translocase subunit SecF;
GN   Name=secF {ECO:0000255|HAMAP-Rule:MF_01464};
GN   OrderedLocusNames=Z0508, ECs0460;
OS   Escherichia coli O157:H7.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=83334;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX   PubMed=11206551; DOI=10.1038/35054089;
RA   Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D.,
RA   Rose D.J., Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A.,
RA   Posfai G., Hackett J., Klink S., Boutin A., Shao Y., Miller L.,
RA   Grotbeck E.J., Davis N.W., Lim A., Dimalanta E.T., Potamousis K.,
RA   Apodaca J., Anantharaman T.S., Lin J., Yen G., Schwartz D.C.,
RA   Welch R.A., Blattner F.R.;
RT   "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL   Nature 409:529-533(2001).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX   PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA   Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA   Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T.,
RA   Iida T., Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T.,
RA   Kuhara S., Shiba T., Hattori M., Shinagawa H.;
RT   "Complete genome sequence of enterohemorrhagic Escherichia coli
RT   O157:H7 and genomic comparison with a laboratory strain K-12.";
RL   DNA Res. 8:11-22(2001).
CC   -!- FUNCTION: Part of the Sec protein translocase complex. Interacts
CC       with the SecYEG preprotein conducting channel. SecDF uses the
CC       proton motive force (PMF) to complete protein translocation after
CC       the ATP-dependent function of SecA. {ECO:0000255|HAMAP-
CC       Rule:MF_01464}.
CC   -!- SUBUNIT: Forms a complex with SecD. Part of the essential Sec
CC       protein translocation apparatus which comprises SecA, SecYEG and
CC       auxiliary proteins SecDF-YajC and YidC. {ECO:0000255|HAMAP-
CC       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}.
DR   EMBL; AE005174; AAG54756.1; -; Genomic_DNA.
DR   EMBL; BA000007; BAB33883.1; -; Genomic_DNA.
DR   PIR; D90686; D90686.
DR   PIR; H85536; H85536.
DR   RefSeq; NP_308487.1; NC_002695.1.
DR   RefSeq; WP_000046637.1; NZ_MWVM01000009.1.
DR   ProteinModelPortal; P0AG95; -.
DR   STRING; 155864.Z0508; -.
DR   EnsemblBacteria; AAG54756; AAG54756; Z0508.
DR   EnsemblBacteria; BAB33883; BAB33883; BAB33883.
DR   GeneID; 914562; -.
DR   KEGG; ece:Z0508; -.
DR   KEGG; ecs:ECs0460; -.
DR   PATRIC; fig|386585.9.peg.560; -.
DR   eggNOG; ENOG4107RAB; Bacteria.
DR   eggNOG; COG0341; LUCA.
DR   HOGENOM; HOG000245914; -.
DR   KO; K03074; -.
DR   Proteomes; UP000000558; Chromosome.
DR   Proteomes; UP000002519; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005622; C:intracellular; IEA:GOC.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0015450; F:P-P-bond-hydrolysis-driven protein transmembrane transporter activity; IEA:InterPro.
DR   GO; GO:0006886; P:intracellular protein transport; IEA:InterPro.
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   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;
DR   PRODOM; P0AG95.
DR   SWISS-2DPAGE; P0AG95.
KW   Cell inner membrane; Cell membrane; Complete proteome; Membrane;
KW   Protein transport; Translocation; Transmembrane; Transmembrane helix;
KW   Transport.
FT   CHAIN         1    323       Protein translocase subunit SecF.
FT                                /FTId=PRO_0000095977.
FT   TOPO_DOM      1     22       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM     23     43       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01464}.
FT   TOPO_DOM     44    142       Periplasmic. {ECO:0000255}.
FT   TRANSMEM    143    163       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01464}.
FT   TOPO_DOM    164    170       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    171    191       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01464}.
FT   TOPO_DOM    192    196       Periplasmic. {ECO:0000255}.
FT   TRANSMEM    197    217       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01464}.
FT   TOPO_DOM    218    247       Cytoplasmic. {ECO:0000255}.
FT   TRANSMEM    248    270       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01464}.
FT   TOPO_DOM    271    280       Periplasmic. {ECO:0000255}.
FT   TRANSMEM    281    301       Helical. {ECO:0000255|HAMAP-
FT                                Rule:MF_01464}.
FT   TOPO_DOM    302    323       Cytoplasmic. {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
//

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