ID   SECM_YERPS              Reviewed;         177 AA.
AC   Q66EJ7;
DT   27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT   27-SEP-2005, sequence version 2.
DT   25-MAY-2022, entry version 75.
DE   RecName: Full=Secretion monitor {ECO:0000255|HAMAP-Rule:MF_01332};
DE   Flags: Precursor;
GN   Name=secM {ECO:0000255|HAMAP-Rule:MF_01332}; OrderedLocusNames=YPTB0696;
OS   Yersinia pseudotuberculosis serotype I (strain IP32953).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=273123;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=IP32953;
RX   PubMed=15358858; DOI=10.1073/pnas.0404012101;
RA   Chain P.S.G., Carniel E., Larimer F.W., Lamerdin J., Stoutland P.O.,
RA   Regala W.M., Georgescu A.M., Vergez L.M., Land M.L., Motin V.L.,
RA   Brubaker R.R., Fowler J., Hinnebusch J., Marceau M., Medigue C.,
RA   Simonet M., Chenal-Francisque V., Souza B., Dacheux D., Elliott J.M.,
RA   Derbise A., Hauser L.J., Garcia E.;
RT   "Insights into the evolution of Yersinia pestis through whole-genome
RT   comparison with Yersinia pseudotuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 101:13826-13831(2004).
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=CAH19936.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; BX936398; CAH19936.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_011191738.1; NZ_CP009712.1.
DR   AlphaFoldDB; Q66EJ7; -.
DR   EnsemblBacteria; CAH19936; CAH19936; YPTB0696.
DR   GeneID; 66842883; -.
DR   KEGG; ypo:BZ17_1859; -.
DR   KEGG; yps:YPTB0696; -.
DR   PATRIC; fig|273123.14.peg.1973; -.
DR   OMA; NYWQQHA; -.
DR   Proteomes; UP000001011; 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; Signal.
FT   SIGNAL          1..37
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_01332"
FT   CHAIN           38..177
FT                   /note="Secretion monitor"
FT                   /id="PRO_0000042111"
SQ   SEQUENCE   177 AA;  19805 MW;  7B3C3055A433CBAD CRC64;
     MIGILNRWRQ FGRRYFWPHL LLGMVAASLG VPSNLSGVPD HAALANTSSS QSRQNHGTTN
     FNSLALLHDI HRRPSFSVDY WQQHALRTVI RHLSFALAPQ AAYARVQEVA ETERVAPSKI
     QQLALLDTLN ALLTHEFKPP AIIRYTEQVE RPVLSPYKPG LWLAQVQGIR AGPANLS