SECM_SALPA
ID SECM_SALPA Reviewed; 165 AA.
AC Q5PDD0;
DT 27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
DT 27-SEP-2005, sequence version 2.
DT 25-MAY-2022, entry version 68.
DE RecName: Full=Secretion monitor {ECO:0000255|HAMAP-Rule:MF_01332};
DE Flags: Precursor;
GN Name=secM {ECO:0000255|HAMAP-Rule:MF_01332}; OrderedLocusNames=SPA0137;
OS Salmonella paratyphi A (strain ATCC 9150 / SARB42).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Salmonella.
OX NCBI_TaxID=295319;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 9150 / SARB42;
RX PubMed=15531882; DOI=10.1038/ng1470;
RA McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S.,
RA Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R.,
RA Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F.,
RA Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W.,
RA Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M.,
RA Warren W., Florea L., Spieth J., Wilson R.K.;
RT "Comparison of genome degradation in Paratyphi A and Typhi, human-
RT restricted serovars of Salmonella enterica that cause typhoid.";
RL Nat. Genet. 36:1268-1274(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=AAV76170.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; CP000026; AAV76170.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_000014336.1; NC_006511.1.
DR AlphaFoldDB; Q5PDD0; -.
DR EnsemblBacteria; AAV76170; AAV76170; SPA0137.
DR KEGG; spt:SPA0137; -.
DR HOGENOM; CLU_108853_0_0_6; -.
DR Proteomes; UP000008185; 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..165
FT /note="Secretion monitor"
FT /id="PRO_0000042110"
SQ SEQUENCE 165 AA; 18117 MW; E81DAD332F1A366C CRC64;
MSGILTRWRQ LGRRYFWPHL LLGMVAASFG LPALSNAAET NTPARTTAST ASKVNFSHLA
LLEASNRRPN FTVDYWHQHA IRTVIRHLSF AMAPQTLPVA DAPSPLQAHH IALLNTLSAM
LTQEGTPPAI VRRLSLAYFA PQTAFSIPAW ISQAQGIRAG PQRLS