MSCM_ECOLI
ID MSCM_ECOLI Reviewed; 1107 AA.
AC P39285; P76798; Q2M6E3;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1998, sequence version 3.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Miniconductance mechanosensitive channel MscM;
DE Flags: Precursor;
GN Name=mscM; Synonyms=yjeP; OrderedLocusNames=b4159, JW4120;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7610040; DOI=10.1093/nar/23.12.2105;
RA Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L., Blattner F.R.;
RT "Analysis of the Escherichia coli genome VI: DNA sequence of the region
RT from 92.8 through 100 minutes.";
RL Nucleic Acids Res. 23:2105-2119(1995).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 1015.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-27.
RC STRAIN=K12;
RX PubMed=3042771; DOI=10.1016/s0021-9258(18)37988-2;
RA Li Q.-X., Dowhan W.;
RT "Structural characterization of Escherichia coli phosphatidylserine
RT decarboxylase.";
RL J. Biol. Chem. 263:11516-11522(1988).
RN [5]
RP FUNCTION, SUBUNIT, SUBCELLULAR LOCATION, AND GENE NAME.
RX PubMed=22874652; DOI=10.4161/chan.20998;
RA Edwards M.D., Black S., Rasmussen T., Rasmussen A., Stokes N.R.,
RA Stephen T.L., Miller S., Booth I.R.;
RT "Characterization of three novel mechanosensitive channel activities in
RT Escherichia coli.";
RL Channels 6:272-281(2012).
CC -!- FUNCTION: Mechanosensitive channel that protects cells against
CC hypoosmotic stress when highly overexpressed. Gates spontaneously in
CC response to increased membrane tension. {ECO:0000269|PubMed:22874652}.
CC -!- SUBUNIT: Homoheptamer. {ECO:0000269|PubMed:22874652}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane
CC {ECO:0000269|PubMed:22874652}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:22874652}.
CC -!- SIMILARITY: Belongs to the MscS (TC 1.A.23) family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA83897.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; U14003; AAA97058.1; -; Genomic_DNA.
DR EMBL; U00096; AAC77119.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE78163.1; -; Genomic_DNA.
DR EMBL; J03916; AAA83897.1; ALT_INIT; Genomic_DNA.
DR PIR; E65226; E65226.
DR RefSeq; NP_418583.1; NC_000913.3.
DR RefSeq; WP_001236847.1; NZ_STEB01000014.1.
DR AlphaFoldDB; P39285; -.
DR SMR; P39285; -.
DR BioGRID; 4262029; 305.
DR IntAct; P39285; 3.
DR STRING; 511145.b4159; -.
DR TCDB; 1.A.23.1.3; the small conductance mechanosensitive ion channel (mscs) family.
DR jPOST; P39285; -.
DR PaxDb; P39285; -.
DR PRIDE; P39285; -.
DR EnsemblBacteria; AAC77119; AAC77119; b4159.
DR EnsemblBacteria; BAE78163; BAE78163; BAE78163.
DR GeneID; 948676; -.
DR KEGG; ecj:JW4120; -.
DR KEGG; eco:b4159; -.
DR PATRIC; fig|1411691.4.peg.2539; -.
DR EchoBASE; EB2371; -.
DR eggNOG; COG1511; Bacteria.
DR eggNOG; COG3264; Bacteria.
DR HOGENOM; CLU_007829_2_0_6; -.
DR OMA; MALITFD; -.
DR PhylomeDB; P39285; -.
DR BioCyc; EcoCyc:G7840-MON; -.
DR PRO; PR:P39285; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; 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:0006811; P:ion transport; IEA:UniProtKB-KW.
DR GO; GO:0055085; P:transmembrane transport; 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; IPR006686; MscS_channel_CS.
DR InterPro; IPR011014; MscS_channel_TM-2.
DR InterPro; IPR023408; MscS_dom_sf.
DR InterPro; IPR025692; MscS_IM_dom1.
DR InterPro; IPR024393; MscS_porin.
DR Pfam; PF00924; MS_channel; 1.
DR Pfam; PF12795; MscS_porin; 1.
DR Pfam; PF12794; MscS_TM; 1.
DR SUPFAM; SSF50182; SSF50182; 1.
DR SUPFAM; SSF82689; SSF82689; 1.
DR SUPFAM; SSF82861; SSF82861; 1.
DR PROSITE; PS01246; UPF0003; 1.
PE 1: Evidence at protein level;
KW Cell inner membrane; Cell membrane; Ion channel; Ion transport; Membrane;
KW Reference proteome; Signal; Transmembrane; Transmembrane helix; Transport.
FT SIGNAL 1..19
FT /evidence="ECO:0000255"
FT CHAIN 20..1107
FT /note="Miniconductance mechanosensitive channel MscM"
FT /id="PRO_0000036180"
FT TRANSMEM 467..487
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 522..542
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 551..571
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 600..620
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 628..648
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 674..694
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 698..718
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 785..805
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 828..848
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 875..895
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 910..930
FT /note="Helical"
FT /evidence="ECO:0000255"
FT CONFLICT 1015
FT /note="R -> A (in Ref. 1; AAA97058)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1107 AA; 123968 MW; 5F52A2993B90532B CRC64;
MRLIITFLMA WCLSWGAYAA TAPDSKQITQ ELEQAKAAKP AQPEVVEALQ SALNALEERK
GSLERIKQYQ QVIDNYPKLS ATLRAQLNNM RDEPRSVSPG MSTDALNQEI LQVSSQLLDK
SRQAQQEQER AREIADSLNQ LPQQQTDARR QLNEIERRLG TLTGNTPLNQ AQNFALQSDS
ARLKALVDEL ELAQLSANNR QELARLRSEL AEKESQQLDA YLQALRNQLN SQRQLEAERA
LESTELLAEN SADLPKDIVA QFKINRELSA ALNQQAQRMD LVASQQRQAA SQTLQVRQAL
NTLREQSQWL GSSNLLGEAL RAQVARLPEM PKPQQLDTEM AQLRVQRLRY EDLLNKQPLL
RQIHQADGQP LTAEQNRILE AQLRTQRELL NSLLQGGDTL LLELTKLKVS NGQLEDALKE
VNEATHRYLF WTSDVRPMTI AWPLEIAQDL RRLISLDTFS QLGKASVMML TSKETILPLF
GALILVGCSI YSRRYFTRFL ERSAAKVGKV TQDHFWLTLR TLFWSILVAS PLPVLWMTLG
YGLREAWPYP LAVAIGDGVT ATVPLLWVVM ICATFARPNG LFIAHFGWPR ERVSRGMRYY
LMSIGLIVPL IMALMMFDNL DDREFSGSLG RLCFILICGA LAVVTLSLKK AGIPLYLNKE
GSGDNITNHM LWNMMIGAPL VAILASAVGY LATAQALLAR LETSVAIWFL LLVVYHVIRR
WMLIQRRRLA FDRAKHRRAE MLAQRARGEE EAHHHSSPEG AIEVDESEVD LDAISAQSLR
LVRSILMLIA LLSVIVLWSE IHSAFGFLEN ISLWDVTSTV QGVESLEPIT LGAVLIAILV
FIITTQLVRN LPALLELAIL QHLDLTPGTG YAITTITKYL LMLIGGLVGF SMIGIEWSKL
QWLVAALGVG LGFGLQEIFA NFISGLIILF EKPIRIGDTV TIRDLTGSVT KINTRATTIS
DWDRKEIIVP NKAFITEQFI NWSLSDSVTR VVLTIPAPAD ANSEEVTEIL LTAARRCSLV
IDNPAPEVFL VDLQQGIQIF ELRIYAAEMG HRMPLRHEIH QLILAGFHAH GIDMPFPPFQ
MRLESLNGKQ TGRTLTSAGK GRQAGSL
