SECF_ECOLI
ID SECF_ECOLI Reviewed; 323 AA.
AC P0AG93; P19674; P77113; Q2MC17;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Protein translocase subunit SecF;
DE AltName: Full=Sec translocon accessory complex subunit SecF;
GN Name=secF; OrderedLocusNames=b0409, JW0399;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND DISRUPTION PHENOTYPE.
RC STRAIN=K12;
RX PubMed=2170107; DOI=10.1002/j.1460-2075.1990.tb07519.x;
RA Gardel C., Johnson K., Jacq A., Beckwith J.;
RT "The secD locus of E.coli codes for two membrane proteins required for
RT protein export.";
RL EMBO J. 9:3209-3216(1990).
RN [2]
RP ERRATUM OF PUBMED:2170107.
RX PubMed=2249673; DOI=10.1002/j.1460-2075.1990.tb07645.x;
RA Gardel C., Johnson K., Jacq A., Beckwith J.;
RL EMBO J. 9:4205-4206(1990).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RA Chung E., Allen E., Araujo R., Aparicio A.M., Davis K., Duncan M.,
RA Federspiel N., Hyman R., Kalman S., Komp C., Kurdi O., Lew H., Lin D.,
RA Namath A., Oefner P., Roberts D., Schramm S., Davis R.W.;
RT "Sequence of minutes 4-25 of Escherichia coli.";
RL Submitted (JAN-1997) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP TOPOLOGY [LARGE SCALE ANALYSIS].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [7]
RP FUNCTION IN TRANSLOCATION, AND MUTAGENESIS OF ASP-213 AND ARG-247.
RX PubMed=21562494; DOI=10.1038/nature09980;
RA Tsukazaki T., Mori H., Echizen Y., Ishitani R., Fukai S., Tanaka T.,
RA Perederina A., Vassylyev D.G., Kohno T., Maturana A.D., Ito K., Nureki O.;
RT "Structure and function of a membrane component SecDF that enhances protein
RT export.";
RL Nature 474:235-238(2011).
RN [8]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=27435098; DOI=10.1042/bcj20160545;
RA Komar J., Alvira S., Schulze R.J., Martin R., Lycklama a Nijeholt J.A.,
RA Lee S.C., Dafforn T.R., Deckers-Hebestreit G., Berger I., Schaffitzel C.,
RA Collinson I.;
RT "Membrane protein insertion and assembly by the bacterial holo-translocon
RT SecYEG-SecDF-YajC-YidC.";
RL Biochem. J. 473:3341-3354(2016).
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. The large periplasmic domain is thought to have a
CC base and head domain joined by a hinge; movement of the hinge may be
CC coupled to both proton transport and protein export, with the head
CC domain capturing substrate, and a conformational change preventing
CC backward movement and driving forward movement. Expression of
CC V.alginolyticus SecD and SecF in E.coli confers Na(+)-dependent protein
CC export, strongly suggesting SecDF functions via cation-coupled protein
CC translocation. {ECO:0000269|PubMed:21562494}.
CC -!- SUBUNIT: Part of the prokaryotic protein translocation apparatus which
CC is comprised of SecA, SecB, SecD, SecE, SecF, SecG and SecY. The SecDF-
CC YidC-YajC translocase forms a supercomplex with SecYEG, called the
CC holo-translocon (HTL) (PubMed:27435098). The stoichiometry of the super
CC complex may be SecYEG:YidC:SecDF 4:3:1, YajC is in the reconstituted
CC complex (with SecDF) but as no antibody is available it could not be
CC quantified (PubMed:27435098). {ECO:0000269|PubMed:27435098}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- DISRUPTION PHENOTYPE: Disruption of both secD and SecF confers cold-
CC sensitive growth (strain secD1(Cs)). {ECO:0000269|PubMed:2170107}.
CC -!- SIMILARITY: Belongs to the SecD/SecF family. SecF subfamily.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB40165.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; X56175; CAA39635.1; -; Genomic_DNA.
DR EMBL; U82664; AAB40165.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73512.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE76189.1; -; Genomic_DNA.
DR PIR; JQ0697; JQ0697.
DR RefSeq; NP_414943.1; NC_000913.3.
DR RefSeq; WP_000046637.1; NZ_STEB01000007.1.
DR PDB; 5MG3; EM; 14.00 A; F=1-323.
DR PDBsum; 5MG3; -.
DR AlphaFoldDB; P0AG93; -.
DR SMR; P0AG93; -.
DR BioGRID; 4263101; 312.
DR ComplexPortal; CPX-1095; Holo-translocon SecYEG-SecDF-YajC-YidC complex.
DR STRING; 511145.b0409; -.
DR TCDB; 2.A.6.4.1; the resistance-nodulation-cell division (rnd) superfamily.
DR jPOST; P0AG93; -.
DR PaxDb; P0AG93; -.
DR PRIDE; P0AG93; -.
DR EnsemblBacteria; AAC73512; AAC73512; b0409.
DR EnsemblBacteria; BAE76189; BAE76189; BAE76189.
DR GeneID; 67416518; -.
DR GeneID; 949120; -.
DR KEGG; ecj:JW0399; -.
DR KEGG; eco:b0409; -.
DR PATRIC; fig|1411691.4.peg.1868; -.
DR EchoBASE; EB0933; -.
DR eggNOG; COG0341; Bacteria.
DR HOGENOM; CLU_050012_1_0_6; -.
DR InParanoid; P0AG93; -.
DR OMA; AFEWRMA; -.
DR PhylomeDB; P0AG93; -.
DR BioCyc; EcoCyc:SECF; -.
DR BioCyc; MetaCyc:SECF; -.
DR PRO; PR:P0AG93; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0031522; C:cell envelope Sec protein transport complex; IPI:ComplexPortal.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IC:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoCyc.
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:0032978; P:protein insertion into membrane from inner side; IDA:ComplexPortal.
DR GO; GO:0006605; P:protein targeting; IEA:UniProtKB-UniRule.
DR GO; GO:0015031; P:protein transport; IBA:GO_Central.
DR GO; GO:0043952; P:protein transport by the Sec complex; IDA:ComplexPortal.
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 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Membrane;
KW Protein transport; Reference proteome; Translocation; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..323
FT /note="Protein translocase subunit SecF"
FT /id="PRO_0000095976"
FT TOPO_DOM 1..22
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 23..43
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 44..142
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 143..163
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 164..170
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 171..191
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 192..196
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 197..217
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 218..247
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 248..270
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 271..280
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 281..301
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 302..323
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT MUTAGEN 213
FT /note="D->M: Abolishes protein translocation."
FT /evidence="ECO:0000269|PubMed:21562494"
FT MUTAGEN 247
FT /note="R->M: Abolishes protein translocation."
FT /evidence="ECO:0000269|PubMed:21562494"
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
