ID   SECM_SALTY              Reviewed;         165 AA.
AC   Q8ZRT8;
DT   05-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 2.
DT   25-MAY-2022, entry version 82.
DE   RecName: Full=Secretion monitor {ECO:0000255|HAMAP-Rule:MF_01332};
DE   Flags: Precursor;
GN   Name=secM {ECO:0000255|HAMAP-Rule:MF_01332}; OrderedLocusNames=STM0135;
OS   Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=99287;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LT2 / SGSC1412 / ATCC 700720;
RX   PubMed=11677609; DOI=10.1038/35101614;
RA   McClelland M., Sanderson K.E., Spieth J., Clifton S.W., Latreille P.,
RA   Courtney L., Porwollik S., Ali J., Dante M., Du F., Hou S., Layman D.,
RA   Leonard S., Nguyen C., Scott K., Holmes A., Grewal N., Mulvaney E.,
RA   Ryan E., Sun H., Florea L., Miller W., Stoneking T., Nhan M., Waterston R.,
RA   Wilson R.K.;
RT   "Complete genome sequence of Salmonella enterica serovar Typhimurium LT2.";
RL   Nature 413:852-856(2001).
CC   -!- FUNCTION: Regulates secA expression by translational coupling of the
CC       secM secA operon. Translational pausing at a specific Pro residue 5
CC       residues before the end of the protein may allow disruption of a mRNA
CC       repressor helix that normally suppresses secA translation initiation.
CC       {ECO:0000255|HAMAP-Rule:MF_01332}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000255|HAMAP-
CC       Rule:MF_01332}. Periplasm {ECO:0000255|HAMAP-Rule:MF_01332}. Note=The
CC       active form is cytosolic, while the periplasmic form is rapidly
CC       degraded, mainly by the tail-specific protease. {ECO:0000255|HAMAP-
CC       Rule:MF_01332}.
CC   -!- SIMILARITY: Belongs to the SecM family. {ECO:0000255|HAMAP-
CC       Rule:MF_01332}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAL19099.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE006468; AAL19099.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; NP_459140.3; NC_003197.2.
DR   AlphaFoldDB; Q8ZRT8; -.
DR   STRING; 99287.STM0135; -.
DR   PaxDb; Q8ZRT8; -.
DR   EnsemblBacteria; AAL19099; AAL19099; STM0135.
DR   GeneID; 1251653; -.
DR   KEGG; stm:STM0135; -.
DR   PATRIC; fig|99287.12.peg.141; -.
DR   HOGENOM; CLU_108853_0_0_6; -.
DR   OMA; NYWQQHA; -.
DR   PhylomeDB; Q8ZRT8; -.
DR   Proteomes; UP000001014; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:UniProtKB-SubCell.
DR   GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell.
DR   GO; GO:0045182; F:translation regulator activity; IEA:InterPro.
DR   HAMAP; MF_01332; SecM; 1.
DR   InterPro; IPR009502; SecM.
DR   Pfam; PF06558; SecM; 1.
DR   PIRSF; PIRSF004572; SecM; 1.
PE   3: Inferred from homology;
KW   Cytoplasm; Periplasm; Reference proteome; Signal.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01332"
FT   CHAIN           38..165
FT                   /note="Secretion monitor"
FT                   /id="PRO_0000031992"
SQ   SEQUENCE   165 AA;  18151 MW;  DEC6C513A53294E6 CRC64;
     MSGILTRWRQ LGRRYFWPHL LLGMVAASFG LPALSNAAET NTPARTTAST ASKVNFSHFA
     LLEASNRRPN FTVDYWHQHA IRTVIRHLSF AMAPQTLPVA DAPSPLQAHH IALLNTLSAM
     LTQEGTPPAI VRRLSLAYFA PQTAFSIPAW ISQAQGIRAG PQRLS