MSCS_SHIFL
ID MSCS_SHIFL Reviewed; 286 AA.
AC P0C0S3; P11666;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Small-conductance mechanosensitive channel;
GN Name=mscS; OrderedLocusNames=SF2909, S3109;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
CC -!- FUNCTION: Mechanosensitive channel that participates in the regulation
CC of osmotic pressure changes within the cell, opening in response to
CC stretch forces in the membrane lipid bilayer, without the need for
CC other proteins. Contributes to normal resistance to hypoosmotic shock.
CC Forms an ion channel of 1.0 nanosiemens conductance with a slight
CC preference for anions. The channel is sensitive to voltage; as the
CC membrane is depolarized, less tension is required to open the channel
CC and vice versa. The channel is characterized by short bursts of
CC activity that last for a few seconds. {ECO:0000250|UniProtKB:P0C0S1}.
CC -!- SUBUNIT: Homoheptamer. {ECO:0000250|UniProtKB:P0C0S1}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000250|UniProtKB:P0C0S1}; Multi-pass membrane protein
CC {ECO:0000250|UniProtKB:P0C0S1}.
CC -!- SIMILARITY: Belongs to the MscS (TC 1.A.23) family. {ECO:0000305}.
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DR EMBL; AE005674; AAN44391.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18213.1; -; Genomic_DNA.
DR RefSeq; NP_708684.1; NC_004337.2.
DR RefSeq; WP_000389818.1; NZ_WPGW01000018.1.
DR AlphaFoldDB; P0C0S3; -.
DR SMR; P0C0S3; -.
DR STRING; 198214.SF2909; -.
DR PRIDE; P0C0S3; -.
DR EnsemblBacteria; AAN44391; AAN44391; SF2909.
DR EnsemblBacteria; AAP18213; AAP18213; S3109.
DR GeneID; 1025924; -.
DR GeneID; 66673199; -.
DR KEGG; sfl:SF2909; -.
DR KEGG; sfx:S3109; -.
DR PATRIC; fig|198214.7.peg.3460; -.
DR HOGENOM; CLU_037945_1_1_6; -.
DR OMA; GMQDTLT; -.
DR OrthoDB; 1903165at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008381; F:mechanosensitive ion channel activity; IEA:InterPro.
DR Gene3D; 2.30.30.60; -; 1.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR045275; MscS_archaea/bacteria_type.
DR InterPro; IPR006685; MscS_channel.
DR InterPro; IPR011066; MscS_channel_C.
DR InterPro; IPR006686; MscS_channel_CS.
DR InterPro; IPR011014; MscS_channel_TM-2.
DR InterPro; IPR023408; MscS_dom_sf.
DR InterPro; IPR008910; TM_helix.
DR PANTHER; PTHR30221; PTHR30221; 1.
DR Pfam; PF00924; MS_channel; 1.
DR Pfam; PF05552; TM_helix; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
DR SUPFAM; SSF82689; SSF82689; 1.
DR SUPFAM; SSF82861; SSF82861; 1.
DR PROSITE; PS01246; UPF0003; 1.
PE 3: Inferred from homology;
KW Cell inner membrane; Cell membrane; Ion channel; Ion transport; Membrane;
KW Reference proteome; Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..286
FT /note="Small-conductance mechanosensitive channel"
FT /id="PRO_0000110240"
FT TOPO_DOM 1..30
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0C0S1"
FT TRANSMEM 31..52
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0C0S1"
FT TOPO_DOM 53..67
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0C0S1"
FT TRANSMEM 68..88
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0C0S1"
FT TOPO_DOM 89..90
FT /note="Periplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0C0S1"
FT TRANSMEM 91..111
FT /note="Helical"
FT /evidence="ECO:0000250|UniProtKB:P0C0S1"
FT TOPO_DOM 112..286
FT /note="Cytoplasmic"
FT /evidence="ECO:0000250|UniProtKB:P0C0S1"
SQ SEQUENCE 286 AA; 30896 MW; FF00AD64F795E9FE CRC64;
MEDLNVVDSI NGAGSWLVAN QALLLSYAVN IVAALAIIIV GLIIARMISN AVNRLMISRK
IDATVADFLS ALVRYGIIAF TLIAALGRVG VQTASVIAVL GAAGLAVGLA LQGSLSNLAA
GVLLVMFRPF RAGEYVDLGG VAGTVLSVQI FSTTMRTADG KIIVIPNGKI IAGNIINFSR
EPVRRNEFII GVAYDSDIDQ VKQILTNIIQ SEDRILKDRE MTVRLNELGA SSINFVVRVW
SNSGDLQNVY WDVLERIKRE FDAAGISFPY PQMDVNFKRV KEDKAA
