SECG_ECOLI
ID SECG_ECOLI Reviewed; 110 AA.
AC P0AG99; P33582; Q2M937;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Protein-export membrane protein SecG;
DE AltName: Full=P12;
DE AltName: Full=Preprotein translocase band 1 subunit;
GN Name=secG; OrderedLocusNames=b3175, JW3142;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 95-110, AND
RP CHARACTERIZATION.
RX PubMed=8253068; DOI=10.1002/j.1460-2075.1993.tb06015.x;
RA Nishiyama K., Mizushima S., Tokuda H.;
RT "A novel membrane protein involved in protein translocation across the
RT cytoplasmic membrane of Escherichia coli.";
RL EMBO J. 12:3409-3415(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8244950; DOI=10.1128/jb.175.23.7743-7744.1993;
RA Dallas W.S., Dev I.K., Ray P.H.;
RT "The dihydropteroate synthase gene, folP, is near the leucine tRNA gene,
RT leuU, on the Escherichia coli chromosome.";
RL J. Bacteriol. 175:7743-7744(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RA Wang R., Kushner S.R.;
RL Submitted (SEP-1993) 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 CHARACTERIZATION.
RX PubMed=8045257; DOI=10.1002/j.1460-2075.1994.tb06628.x;
RA Nishiyama K., Hanada M., Tokuda H.;
RT "Disruption of the gene encoding p12 (SecG) reveals the direct involvement
RT and important function of SecG in the protein translocation of Escherichia
RT coli at low temperature.";
RL EMBO J. 13:3272-3277(1994).
RN [7]
RP CHARACTERIZATION.
RX PubMed=8034620; DOI=10.1016/s0021-9258(17)32220-2;
RA Douville K., Leonard M., Brundage L., Nishiyama K., Tokuda H.,
RA Mizushima S., Wickner W.;
RT "Band 1 subunit of Escherichia coli preportein translocase and integral
RT membrane export factor P12 are the same protein.";
RL J. Biol. Chem. 269:18705-18707(1994).
RN [8]
RP MUTANTS.
RX PubMed=7556084; DOI=10.1002/j.1460-2075.1995.tb00120.x;
RA Bost S., Belin D.;
RT "A new genetic selection identifies essential residues in SecG, a component
RT of the Escherichia coli protein export machinery.";
RL EMBO J. 14:4412-4421(1995).
RN [9]
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 [10]
RP COMPLEX DEGRADATION.
RC STRAIN=K12 / MC4100;
RX PubMed=19661432; DOI=10.1126/science.1172221;
RA van Stelten J., Silva F., Belin D., Silhavy T.J.;
RT "Effects of antibiotics and a proto-oncogene homolog on destruction of
RT protein translocator SecY.";
RL Science 325:753-756(2009).
RN [11]
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).
RN [12]
RP STRUCTURE BY ELECTRON MICROSCOPY (14.9 ANGSTROMS) OF 1-77 IN COMPLEX WITH
RP THE RIBOSOME, AND A NASCENT POLYPEPTIDE CHAIN.
RC STRAIN=MRE-600;
RX PubMed=16292303; DOI=10.1038/nature04133;
RA Mitra K., Schaffitzel C., Shaikh T., Tama F., Jenni S., Brooks C.L. III,
RA Ban N., Frank J.;
RT "Structure of the E. coli protein-conducting channel bound to a translating
RT ribosome.";
RL Nature 438:318-324(2005).
RN [13]
RP REVIEW.
RX PubMed=18078384; DOI=10.1146/annurev.biochem.77.061606.160747;
RA Driessen A.J., Nouwen N.;
RT "Protein translocation across the bacterial cytoplasmic membrane.";
RL Annu. Rev. Biochem. 77:643-667(2008).
CC -!- FUNCTION: Subunit of the protein translocation channel SecYEG.
CC Overexpression of some hybrid proteins has been thought to jam the
CC protein secretion apparatus resulting in cell death; while this may be
CC true it also results in FtsH-mediated degradation of SecY. Treatment
CC with antibiotics that block translation elongation such as
CC chloramphenicol also leads to degradation of SecY and SecE but not
CC SecG.
CC -!- SUBUNIT: Component of the Sec protein translocase complex. Heterotrimer
CC consisting of SecY, SecE and SecG subunits. The heterotrimers can form
CC oligomers, although 1 heterotrimer is thought to be able to translocate
CC proteins. The SecDF-YidC-YajC translocase forms a supercomplex with
CC SecYEG, called the holo-translocon (HTL) (PubMed:27435098). The
CC stoichiometry of the super complex may be SecYEG:YidC:SecDF 4:3:1, YajC
CC is in the reconstituted complex (with SecDF) but as no antibody is
CC available it could not be quantified (PubMed:27435098). SecG probably
CC contacts ribosomal protein L23 and/or L29 when the translocation
CC complex is docked with the ribosome. {ECO:0000269|PubMed:27435098}.
CC -!- INTERACTION:
CC P0AG99; P10408: secA; NbExp=3; IntAct=EBI-6404248, EBI-543213;
CC P0AG99; P0AGA2: secY; NbExp=3; IntAct=EBI-6404248, EBI-761422;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane; Multi-pass membrane protein.
CC -!- PTM: The N-terminus is blocked.
CC -!- SIMILARITY: Belongs to the SecG family. {ECO:0000305}.
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DR EMBL; D16463; BAA03930.1; -; Genomic_DNA.
DR EMBL; L12968; -; NOT_ANNOTATED_CDS; Unassigned_DNA.
DR EMBL; U01376; AAA97511.1; -; Genomic_DNA.
DR EMBL; U18997; AAA57976.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76207.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77219.1; -; Genomic_DNA.
DR PIR; S40402; S40402.
DR RefSeq; NP_417642.1; NC_000913.3.
DR RefSeq; WP_001295556.1; NZ_SSZK01000007.1.
DR PDB; 2AKH; EM; 14.90 A; A/X=1-77.
DR PDB; 2AKI; EM; 14.90 A; A/X=1-77.
DR PDB; 3J45; EM; 9.50 A; G=9-73.
DR PDB; 3J46; EM; 10.10 A; G=9-73.
DR PDB; 5MG3; EM; 14.00 A; G=1-110.
DR PDB; 5NCO; EM; 4.80 A; j=1-71.
DR PDBsum; 2AKH; -.
DR PDBsum; 2AKI; -.
DR PDBsum; 3J45; -.
DR PDBsum; 3J46; -.
DR PDBsum; 5MG3; -.
DR PDBsum; 5NCO; -.
DR AlphaFoldDB; P0AG99; -.
DR SMR; P0AG99; -.
DR BioGRID; 4259584; 379.
DR BioGRID; 852033; 1.
DR ComplexPortal; CPX-1095; Holo-translocon SecYEG-SecDF-YajC-YidC complex.
DR ComplexPortal; CPX-1096; Protein-conducting channel SecYEG complex.
DR DIP; DIP-47480N; -.
DR IntAct; P0AG99; 4.
DR MINT; P0AG99; -.
DR STRING; 511145.b3175; -.
DR TCDB; 3.A.5.1.1; the general secretory pathway (sec) family.
DR jPOST; P0AG99; -.
DR PaxDb; P0AG99; -.
DR PRIDE; P0AG99; -.
DR EnsemblBacteria; AAC76207; AAC76207; b3175.
DR EnsemblBacteria; BAE77219; BAE77219; BAE77219.
DR GeneID; 60901971; -.
DR GeneID; 947720; -.
DR KEGG; ecj:JW3142; -.
DR KEGG; eco:b3175; -.
DR PATRIC; fig|1411691.4.peg.3557; -.
DR EchoBASE; EB2019; -.
DR eggNOG; COG1314; Bacteria.
DR HOGENOM; CLU_094156_2_2_6; -.
DR InParanoid; P0AG99; -.
DR OMA; MYEVLMV; -.
DR PhylomeDB; P0AG99; -.
DR BioCyc; EcoCyc:SECG; -.
DR BioCyc; MetaCyc:SECG; -.
DR EvolutionaryTrace; P0AG99; -.
DR PRO; PR:P0AG99; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0031522; C:cell envelope Sec protein transport complex; IDA:EcoCyc.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0016020; C:membrane; IDA:ComplexPortal.
DR GO; GO:0005886; C:plasma membrane; IDA:EcoliWiki.
DR GO; GO:0008320; F:protein transmembrane transporter activity; IDA:EcoCyc.
DR GO; GO:0015450; F:protein-transporting ATPase activity; IEA:InterPro.
DR GO; GO:0065002; P:intracellular protein transmembrane transport; IDA:EcoliWiki.
DR GO; GO:0006886; P:intracellular protein transport; IDA:EcoliWiki.
DR GO; GO:0032978; P:protein insertion into membrane from inner side; IDA:EcoCyc.
DR GO; GO:0009306; P:protein secretion; IEA:InterPro.
DR GO; GO:0043952; P:protein transport by the Sec complex; IDA:ComplexPortal.
DR GO; GO:0006616; P:SRP-dependent cotranslational protein targeting to membrane, translocation; IDA:EcoCyc.
DR InterPro; IPR004692; SecG.
DR PANTHER; PTHR34182; PTHR34182; 1.
DR Pfam; PF03840; SecG; 1.
DR PRINTS; PR01651; SECGEXPORT.
DR TIGRFAMs; TIGR00810; secG; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane;
KW Direct protein sequencing; Membrane; Protein transport; Reference proteome;
KW Translocation; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..110
FT /note="Protein-export membrane protein SecG"
FT /id="PRO_0000157225"
FT TOPO_DOM 1..13
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 14..25
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 26..50
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT TRANSMEM 51..66
FT /note="Helical"
FT /evidence="ECO:0000305"
FT TOPO_DOM 67..110
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:15919996"
FT REGION 81..110
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MUTAGEN 41
FT /note="T->P: Affects activity."
FT MUTAGEN 42
FT /note="L->P: Affects activity."
FT MUTAGEN 43
FT /note="F->S,Y: Affects activity."
SQ SEQUENCE 110 AA; 11365 MW; 8DC7663F94D32F2F CRC64;
MYEALLVVFL IVAIGLVGLI MLQQGKGADM GASFGAGASA TLFGSSGSGN FMTRMTALLA
TLFFIISLVL GNINSNKTNK GSEWENLSAP AKTEQTQPAA PAKPTSDIPN
