MSCS_CALS4
ID MSCS_CALS4 Reviewed; 282 AA.
AC Q8R6L9;
DT 07-JUN-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 25-MAY-2022, entry version 97.
DE RecName: Full=Small-conductance mechanosensitive channel;
GN Name=mscS {ECO:0000312|EMBL:AAM25887.1};
GN OrderedLocusNames=TTE2783 {ECO:0000312|EMBL:AAM25887.1};
OS Caldanaerobacter subterraneus subsp. tengcongensis (strain DSM 15242 / JCM
OS 11007 / NBRC 100824 / MB4) (Thermoanaerobacter tengcongensis).
OC Bacteria; Firmicutes; Clostridia; Thermoanaerobacterales;
OC Thermoanaerobacteraceae; Caldanaerobacter.
OX NCBI_TaxID=273068 {ECO:0000312|Proteomes:UP000000555};
RN [1] {ECO:0000312|EMBL:AAM25887.1, ECO:0000312|Proteomes:UP000000555}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15242 / JCM 11007 / NBRC 100824 / MB4
RC {ECO:0000312|Proteomes:UP000000555};
RX PubMed=11997336; DOI=10.1101/gr.219302;
RA Bao Q., Tian Y., Li W., Xu Z., Xuan Z., Hu S., Dong W., Yang J., Chen Y.,
RA Xue Y., Xu Y., Lai X., Huang L., Dong X., Ma Y., Ling L., Tan H., Chen R.,
RA Wang J., Yu J., Yang H.;
RT "A complete sequence of the T. tengcongensis genome.";
RL Genome Res. 12:689-700(2002).
RN [2] {ECO:0007744|PDB:3T9N, ECO:0007744|PDB:3UDC}
RP X-RAY CRYSTALLOGRAPHY (3.35 ANGSTROMS), FUNCTION, SUBCELLULAR LOCATION,
RP TOPOLOGY, SUBUNIT, DOMAIN, AND MUTAGENESIS OF LEU-276 AND GLU-278.
RX PubMed=23074248; DOI=10.1073/pnas.1207977109;
RA Zhang X., Wang J., Feng Y., Ge J., Li W., Sun W., Iscla I., Yu J.,
RA Blount P., Li Y., Yang M.;
RT "Structure and molecular mechanism of an anion-selective mechanosensitive
RT channel of small conductance.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:18180-18185(2012).
CC -!- FUNCTION: Mechanosensitive ion channel that participates in the
CC regulation of osmotic pressure changes within the cell, opening in
CC response to stretch forces in the membrane lipid bilayer, without the
CC need for other proteins. Has high selectivity for anions, and may
CC contribute to resistance to hypoosmotic shock.
CC {ECO:0000269|PubMed:23074248}.
CC -!- SUBUNIT: Homoheptamer. {ECO:0000269|PubMed:23074248}.
CC -!- INTERACTION:
CC Q8R6L9; Q8R6L9: mscS; NbExp=2; IntAct=EBI-16017731, EBI-16017731;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000305|PubMed:23074248}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:23074248}.
CC -!- DOMAIN: The C-terminal cytoplasmic domain is important for channel ion
CC selectivity. {ECO:0000269|PubMed:23074248}.
CC -!- SIMILARITY: Belongs to the MscS (TC 1.A.23) family. {ECO:0000305}.
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DR EMBL; AE008691; AAM25887.1; -; Genomic_DNA.
DR PDB; 3T9N; X-ray; 3.46 A; A/B/C/D/E/F/G=1-282.
DR PDB; 3UDC; X-ray; 3.35 A; A/B/C/D/E/F/G=1-270.
DR PDBsum; 3T9N; -.
DR PDBsum; 3UDC; -.
DR AlphaFoldDB; Q8R6L9; -.
DR SMR; Q8R6L9; -.
DR DIP; DIP-60083N; -.
DR STRING; 273068.TTE2783; -.
DR EnsemblBacteria; AAM25887; AAM25887; TTE2783.
DR KEGG; tte:TTE2783; -.
DR eggNOG; COG0668; Bacteria.
DR HOGENOM; CLU_037945_8_2_9; -.
DR OMA; ITIPNKH; -.
DR Proteomes; UP000000555; 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:0042802; F:identical protein binding; IPI:IntAct.
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; IPR006685; MscS_channel.
DR InterPro; IPR011066; MscS_channel_C.
DR InterPro; IPR011014; MscS_channel_TM-2.
DR InterPro; IPR023408; MscS_dom_sf.
DR InterPro; IPR045276; YbiO_bact.
DR PANTHER; PTHR30460; PTHR30460; 1.
DR Pfam; PF00924; MS_channel; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
DR SUPFAM; SSF82689; SSF82689; 1.
DR SUPFAM; SSF82861; SSF82861; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cell inner membrane; Cell membrane; Ion channel;
KW Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..282
FT /note="Small-conductance mechanosensitive channel"
FT /id="PRO_0000440564"
FT TOPO_DOM 1..23
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:23074248"
FT TRANSMEM 24..46
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:23074248"
FT TOPO_DOM 47..66
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23074248"
FT TRANSMEM 67..87
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:23074248"
FT TOPO_DOM 88..89
FT /note="Periplasmic"
FT /evidence="ECO:0000305|PubMed:23074248"
FT TRANSMEM 90..110
FT /note="Helical"
FT /evidence="ECO:0000269|PubMed:23074248"
FT TOPO_DOM 111..282
FT /note="Cytoplasmic"
FT /evidence="ECO:0000305|PubMed:23074248"
FT MUTAGEN 276
FT /note="L->Y: Loss of channel activity, possibly due to
FT physical obstruction of the ion permeation pathway."
FT /evidence="ECO:0000269|PubMed:23074248"
FT MUTAGEN 278
FT /note="E->A: Reduces channel ion selectivity."
FT /evidence="ECO:0000269|PubMed:23074248"
FT MUTAGEN 278
FT /note="E->R: Loss of channel ion selectivity."
FT /evidence="ECO:0000269|PubMed:23074248"
FT HELIX 17..50
FT /evidence="ECO:0007829|PDB:3UDC"
FT HELIX 60..87
FT /evidence="ECO:0007829|PDB:3UDC"
FT HELIX 92..109
FT /evidence="ECO:0007829|PDB:3UDC"
FT HELIX 111..125
FT /evidence="ECO:0007829|PDB:3UDC"
FT STRAND 134..137
FT /evidence="ECO:0007829|PDB:3UDC"
FT STRAND 140..147
FT /evidence="ECO:0007829|PDB:3UDC"
FT STRAND 149..156
FT /evidence="ECO:0007829|PDB:3UDC"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:3UDC"
FT STRAND 160..165
FT /evidence="ECO:0007829|PDB:3UDC"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:3UDC"
FT STRAND 172..174
FT /evidence="ECO:0007829|PDB:3UDC"
FT STRAND 176..178
FT /evidence="ECO:0007829|PDB:3UDC"
FT STRAND 180..189
FT /evidence="ECO:0007829|PDB:3UDC"
FT HELIX 194..211
FT /evidence="ECO:0007829|PDB:3UDC"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:3UDC"
FT STRAND 220..228
FT /evidence="ECO:0007829|PDB:3UDC"
FT STRAND 231..241
FT /evidence="ECO:0007829|PDB:3UDC"
FT HELIX 245..262
FT /evidence="ECO:0007829|PDB:3UDC"
FT STRAND 271..277
FT /evidence="ECO:0007829|PDB:3T9N"
SQ SEQUENCE 282 AA; 32034 MW; C193404E11BE7B69 CRC64;
MWADIYHKLV EIYDIKAVKF LLDVLKILII AFIGIKFADF LIYRFYKLYS KSKIQLPQRK
IDTLTSLTKN AVRYIIYFLA GASILKLFNI DMTSLLAVAG IGSLAIGFGA QNLVKDMISG
FFIIFEDQFS VGDYVTINGI SGTVEEIGLR VTKIRGFSDG LHIIPNGEIK MVTNLTKDSM
MAVVNIAFPI DEDVDKIIEG LQEICEEVKK SRDDLIEGPT VLGITDMQDS KLVIMVYAKT
QPMQKWAVER DIRYRVKKMF DQKNISFPYP RTTVILSEKK TN
