ID   MSCL_BORPD              Reviewed;         148 AA.
AC   A9HW97;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-FEB-2008, sequence version 1.
DT   25-MAY-2022, entry version 79.
DE   RecName: Full=Large-conductance mechanosensitive channel {ECO:0000255|HAMAP-Rule:MF_00115};
GN   Name=mscL {ECO:0000255|HAMAP-Rule:MF_00115}; OrderedLocusNames=Bpet0123;
OS   Bordetella petrii (strain ATCC BAA-461 / DSM 12804 / CCUG 43448).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=340100;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-461 / DSM 12804 / CCUG 43448;
RX   PubMed=18826580; DOI=10.1186/1471-2164-9-449;
RA   Gross R., Guzman C.A., Sebaihia M., Martin dos Santos V.A.P., Pieper D.H.,
RA   Koebnik R., Lechner M., Bartels D., Buhrmester J., Choudhuri J.V.,
RA   Ebensen T., Gaigalat L., Herrmann S., Khachane A.N., Larisch C., Link S.,
RA   Linke B., Meyer F., Mormann S., Nakunst D., Rueckert C.,
RA   Schneiker-Bekel S., Schulze K., Voerholter F.-J., Yevsa T., Engle J.T.,
RA   Goldman W.E., Puehler A., Goebel U.B., Goesmann A., Bloecker H., Kaiser O.,
RA   Martinez-Arias R.;
RT   "The missing link: Bordetella petrii is endowed with both the metabolic
RT   versatility of environmental bacteria and virulence traits of pathogenic
RT   Bordetellae.";
RL   BMC Genomics 9:449-449(2008).
CC   -!- FUNCTION: Channel that opens in response to stretch forces in the
CC       membrane lipid bilayer. May participate in the regulation of osmotic
CC       pressure changes within the cell. {ECO:0000255|HAMAP-Rule:MF_00115}.
CC   -!- SUBUNIT: Homopentamer. {ECO:0000255|HAMAP-Rule:MF_00115}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC       Rule:MF_00115}; Multi-pass membrane protein {ECO:0000255|HAMAP-
CC       Rule:MF_00115}.
CC   -!- SIMILARITY: Belongs to the MscL family. {ECO:0000255|HAMAP-
CC       Rule:MF_00115}.
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DR   EMBL; AM902716; CAP40454.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9HW97; -.
DR   STRING; 94624.Bpet0123; -.
DR   EnsemblBacteria; CAP40454; CAP40454; Bpet0123.
DR   KEGG; bpt:Bpet0123; -.
DR   eggNOG; COG1970; Bacteria.
DR   OMA; AWIIFLM; -.
DR   Proteomes; UP000001225; Chromosome.
DR   GO; GO:0005887; C:integral component of plasma membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0008381; F:mechanosensitive ion channel activity; IEA:UniProtKB-UniRule.
DR   Gene3D; 1.10.1200.120; -; 1.
DR   HAMAP; MF_00115; MscL; 1.
DR   InterPro; IPR001185; MS_channel.
DR   InterPro; IPR037673; MSC/AndL.
DR   InterPro; IPR036019; MscL_channel.
DR   PANTHER; PTHR30266; PTHR30266; 1.
DR   Pfam; PF01741; MscL; 1.
DR   PRINTS; PR01264; MECHCHANNEL.
DR   SUPFAM; SSF81330; SSF81330; 1.
DR   TIGRFAMs; TIGR00220; mscL; 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..148
FT                   /note="Large-conductance mechanosensitive channel"
FT                   /id="PRO_1000094879"
FT   TRANSMEM        21..41
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00115"
FT   TRANSMEM        45..65
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00115"
FT   TRANSMEM        92..112
FT                   /note="Helical"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00115"
SQ   SEQUENCE   148 AA;  15876 MW;  6E94C9DD4944815A CRC64;
     MSKASGFLKE FRDFAVKGNA IDLAVGVIIG AAFGKIVDSV VKDLIMPLVN YILGGSVDFS
     NKFLVLSAPD GYAGPMTYAD LTKAGAIVLA WGNFLTILIN FILLALVVFI IVKAINAARR
     KEEEAPAEPA APPEDVVVLR EIRDLLKK