SECM_ECOLI
ID SECM_ECOLI Reviewed; 170 AA.
AC P62395; P10409; P75641;
DT 05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Secretion monitor;
DE Flags: Precursor;
GN Name=secM; Synonyms=srrA, yacA; OrderedLocusNames=b0097, JW5007;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=2824434; DOI=10.1128/jb.169.12.5408-5415.1987;
RA Beall B., Lutkenhaus J.;
RT "Sequence analysis, transcriptional organization, and insertional
RT mutagenesis of the envA gene of Escherichia coli.";
RL J. Bacteriol. 169:5408-5415(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=2841285; DOI=10.1128/jb.170.8.3404-3414.1988;
RA Schmidt M., Rollo E., Grodberg J., Oliver D.;
RT "Nucleotide sequence of the secA gene and secA(Ts) mutations preventing
RT protein export in Escherichia coli.";
RL J. Bacteriol. 170:3404-3414(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
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 SUBCELLULAR LOCATION.
RX PubMed=1834634; DOI=10.1128/jb.173.22.7092-7097.1991;
RA Rajapandi T., Dolan K.M., Oliver D.B.;
RT "The first gene in the Escherichia coli secA operon, gene X, encodes a
RT nonessential secretory protein.";
RL J. Bacteriol. 173:7092-7097(1991).
RN [7]
RP MUTAGENESIS OF 29-LEU--ALA-33 AND 31-LEU--LEU-34.
RC STRAIN=CG155;
RX PubMed=9748461; DOI=10.1128/jb.180.19.5240-5242.1998;
RA Oliver D.B., Norman J., Sarker S.;
RT "Regulation of Escherichia coli secA by cellular protein secretion
RT proficiency requires an intact gene X signal sequence and an active
RT translocon.";
RL J. Bacteriol. 180:5240-5242(1998).
RN [8]
RP IDENTIFICATION OF START CODON, AND MUTAGENESIS.
RX PubMed=10986266; DOI=10.1128/jb.182.19.5592-5595.2000;
RA Sarker S., Rudd K.E., Oliver D.B.;
RT "Revised translation start site for secM defines an atypical signal peptide
RT that regulates Escherichia coli secA expression.";
RL J. Bacteriol. 182:5592-5595(2000).
RN [9]
RP SELF-TRANSLATION ARREST IN THE CYTOSOL.
RC STRAIN=GN40;
RX PubMed=11172723; DOI=10.1016/s1097-2765(01)00166-6;
RA Nakatogawa H., Ito K.;
RT "Secretion monitor, SecM, undergoes self-translation arrest in the
RT cytosol.";
RL Mol. Cell 7:185-192(2001).
RN [10]
RP MUTAGENESIS OF RESIDUES 140-166, IDENTIFICATION OF THE ARREST-CAUSING
RP SEQUENCE, AND ALLEVIATION OF ELONGATION ARREST BY RIBOSOMAL PROTEIN L22
RP MUTATIONS.
RX PubMed=11893334; DOI=10.1016/s0092-8674(02)00649-9;
RA Nakatogawa H., Ito K.;
RT "The ribosomal exit tunnel functions as a discriminating gate.";
RL Cell 108:629-636(2002).
RN [11]
RP MUTAGENESIS OF MET-24.
RC STRAIN=K12 / MC4100 / ATCC 35695 / DSM 6574;
RX PubMed=11948148; DOI=10.1128/jb.184.9.2360-2369.2002;
RA Sarker S., Oliver D.B.;
RT "Critical regions of secM that control its translation and secretion and
RT promote secretion-specific secA regulation.";
RL J. Bacteriol. 184:2360-2369(2002).
RN [12]
RP POSSIBLE MECHANISM FOR THE RELEASE OF TRANSLATIONAL PAUSING.
RX PubMed=14594848; DOI=10.1128/jb.185.22.6719-6722.2003;
RA Butkus M.E., Prundeanu L.B., Oliver D.B.;
RT "Translocon 'pulling' of nascent secM controls the duration of its
RT translational pause and secretion-responsive secA regulation.";
RL J. Bacteriol. 185:6719-6722(2003).
RN [13]
RP REVIEW.
RX PubMed=15063851; DOI=10.1016/j.mib.2004.01.001;
RA Nakatogawa H., Murakami A., Ito K.;
RT "Control of SecA and SecM translation by protein secretion.";
RL Curr. Opin. Microbiol. 7:145-150(2004).
CC -!- FUNCTION: Regulates secA expression by translational coupling of the
CC secM secA operon. Ribosomes translating the C-terminal region of secM
CC can disrupt an RNA repressor helix that normally blocks secA
CC translation initiation, derepressing the expression of secA.
CC Translational pausing of secM at Pro-166 under secretion-limiting
CC conditions increases the duration of the disruption and thus increases
CC secA expression. This is controlled by interaction of the secM signal
CC peptide with secA and the translocon, possibly by secA pulling the
CC paused secM out of the ribosome. The arrest sequence (150-
CC FXXXXWIXXXXGIRAGP-166) is sufficient to cause arrest of unrelated
CC proteins. Elongation arrest can be alleviated by mutations in the 23S
CC rRNA or in ribosomal protein L22.
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:1834634}.
CC Periplasm {ECO:0000269|PubMed:1834634}. Note=The active form is
CC cytosolic, while the periplasmic form is rapidly degraded, mainly by
CC the tail-specific protease.
CC -!- SIMILARITY: Belongs to the SecM family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA24618.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAA83850.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=CAA38874.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M19211; AAA83850.1; ALT_INIT; Genomic_DNA.
DR EMBL; M20791; AAA24618.1; ALT_INIT; Genomic_DNA.
DR EMBL; X55034; CAA38874.1; ALT_INIT; Genomic_DNA.
DR EMBL; U00096; AAC73208.2; -; Genomic_DNA.
DR EMBL; AP009048; BAB96665.2; -; Genomic_DNA.
DR PIR; A64732; QQECAA.
DR RefSeq; NP_414639.2; NC_000913.3.
DR RefSeq; WP_000014321.1; NZ_STEB01000010.1.
DR PDB; 2N62; NMR; -; L=150-166.
DR PDB; 3JBV; EM; 3.32 A; z=150-166.
DR PDBsum; 2N62; -.
DR PDBsum; 3JBV; -.
DR AlphaFoldDB; P62395; -.
DR SMR; P62395; -.
DR BioGRID; 4261885; 277.
DR BioGRID; 849231; 1.
DR IntAct; P62395; 2.
DR STRING; 511145.b0097; -.
DR PaxDb; P62395; -.
DR PRIDE; P62395; -.
DR EnsemblBacteria; AAC73208; AAC73208; b0097.
DR EnsemblBacteria; BAB96665; BAB96665; BAB96665.
DR GeneID; 66671613; -.
DR GeneID; 944831; -.
DR KEGG; ecj:JW5007; -.
DR KEGG; eco:b0097; -.
DR PATRIC; fig|511145.12.peg.101; -.
DR EchoBASE; EB1079; -.
DR eggNOG; ENOG5031JGK; Bacteria.
DR HOGENOM; CLU_108853_0_0_6; -.
DR OMA; NYWQQHA; -.
DR PhylomeDB; P62395; -.
DR BioCyc; EcoCyc:EG11087-MON; -.
DR PRO; PR:P62395; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR GO; GO:0042597; C:periplasmic space; IDA:EcoCyc.
DR GO; GO:0045182; F:translation regulator activity; IDA:EcoCyc.
DR GO; GO:0006417; P:regulation of translation; IMP:EcoCyc.
DR HAMAP; MF_01332; SecM; 1.
DR InterPro; IPR009502; SecM.
DR Pfam; PF06558; SecM; 1.
DR PIRSF; PIRSF004572; SecM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Periplasm; Reference proteome; Signal.
FT SIGNAL 1..37
FT /evidence="ECO:0000255"
FT CHAIN 38..170
FT /note="Secretion monitor"
FT /id="PRO_0000031988"
FT MUTAGEN 1
FT /note="M->V: Protein is not produced, (and therefore
FT neither is SecA) indicating this is the start codon."
FT /evidence="ECO:0000269|PubMed:10986266"
FT MUTAGEN 24
FT /note="M->C: Protein is produced; this is not the start
FT codon."
FT /evidence="ECO:0000269|PubMed:11948148"
FT MUTAGEN 29..33
FT /note="Missing: Loss of the ability to repress SecA-LacZ
FT fusion proteins, translational pausing is very long, with
FT almost no secretion."
FT /evidence="ECO:0000269|PubMed:9748461"
FT MUTAGEN 31..34
FT /note="Missing: Loss of the ability to repress SecA-LacZ
FT fusion proteins."
FT /evidence="ECO:0000269|PubMed:9748461"
FT MUTAGEN 163
FT /note="R->A: Abolishes translation arrest."
FT /evidence="ECO:0000269|PubMed:10986266"
FT MUTAGEN 166..170
FT /note="Missing: Abolishes translation arrest."
FT /evidence="ECO:0000269|PubMed:10986266"
FT MUTAGEN 166
FT /note="P->A: Abolishes translation arrest."
FT /evidence="ECO:0000269|PubMed:10986266"
SQ SEQUENCE 170 AA; 18880 MW; 5F5B3001056CAD22 CRC64;
MSGILTRWRQ FGKRYFWPHL LLGMVAASLG LPALSNAAEP NAPAKATTRN HEPSAKVNFG
QLALLEANTR RPNSNYSVDY WHQHAIRTVI RHLSFAMAPQ TLPVAEESLP LQAQHLALLD
TLSALLTQEG TPSEKGYRID YAHFTPQAKF STPVWISQAQ GIRAGPQRLT
