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Database: UniProt
Entry: A0A014PTI1_9GAMM
LinkDB: A0A014PTI1_9GAMM
Original site: A0A014PTI1_9GAMM 
ID   A0A014PTI1_9GAMM        Unreviewed;       290 AA.
AC   A0A014PTI1;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   RecName: Full=Small-conductance mechanosensitive channel {ECO:0000256|RuleBase:RU369025};
GN   ORFNames=BG55_18450 {ECO:0000313|EMBL:EXU74147.1};
OS   Erwinia mallotivora.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Erwiniaceae; Erwinia.
OX   NCBI_TaxID=69222 {ECO:0000313|EMBL:EXU74147.1, ECO:0000313|Proteomes:UP000019918};
RN   [1] {ECO:0000313|EMBL:EXU74147.1, ECO:0000313|Proteomes:UP000019918}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BT-MARDI {ECO:0000313|EMBL:EXU74147.1,
RC   ECO:0000313|Proteomes:UP000019918};
RA   Redzuan R., Abu Bakar N., Badrun R., Mohd Raih M.F., Rozano L.,
RA   Mat Amin N.;
RT   "Draft genome of Erwinia mallotivora strain BT-MARDI, a papaya dieback
RT   pathogen.";
RL   Submitted (FEB-2014) to the EMBL/GenBank/DDBJ databases.
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. {ECO:0000256|RuleBase:RU369025}.
CC   -!- SUBUNIT: Homoheptamer. {ECO:0000256|RuleBase:RU369025}.
CC   -!- SUBCELLULAR LOCATION: Cell inner membrane
CC       {ECO:0000256|RuleBase:RU369025}; Multi-pass membrane protein
CC       {ECO:0000256|RuleBase:RU369025}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the MscS (TC 1.A.23) family.
CC       {ECO:0000256|ARBA:ARBA00008017, ECO:0000256|RuleBase:RU369025}.
CC   -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC       feature annotation. {ECO:0000256|RuleBase:RU369025}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EXU74147.1}.
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DR   EMBL; JFHN01000065; EXU74147.1; -; Genomic_DNA.
DR   RefSeq; WP_034940084.1; NZ_VFIK01000003.1.
DR   AlphaFoldDB; A0A014PTI1; -.
DR   STRING; 69222.BG55_18450; -.
DR   PATRIC; fig|69222.5.peg.3761; -.
DR   OrthoDB; 9809206at2; -.
DR   Proteomes; UP000019918; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008381; F:mechanosensitive monoatomic ion channel activity; IEA:InterPro.
DR   Gene3D; 1.10.287.1260; -; 1.
DR   Gene3D; 2.30.30.60; -; 1.
DR   Gene3D; 3.30.70.100; -; 1.
DR   InterPro; IPR010920; LSM_dom_sf.
DR   InterPro; IPR049142; MS_channel_1st.
DR   InterPro; IPR049278; MS_channel_C.
DR   InterPro; IPR008910; MSC_TM_helix.
DR   InterPro; IPR045275; MscS_archaea/bacteria_type.
DR   InterPro; IPR023408; MscS_beta-dom_sf.
DR   InterPro; IPR006685; MscS_channel_2nd.
DR   InterPro; IPR011066; MscS_channel_C_sf.
DR   InterPro; IPR006686; MscS_channel_CS.
DR   InterPro; IPR011014; MscS_channel_TM-2.
DR   PANTHER; PTHR30221; SMALL-CONDUCTANCE MECHANOSENSITIVE CHANNEL; 1.
DR   PANTHER; PTHR30221:SF1; SMALL-CONDUCTANCE MECHANOSENSITIVE CHANNEL; 1.
DR   Pfam; PF21088; MS_channel_1st; 1.
DR   Pfam; PF05552; MS_channel_1st_1; 1.
DR   Pfam; PF00924; MS_channel_2nd; 1.
DR   Pfam; PF21082; MS_channel_3rd; 1.
DR   SUPFAM; SSF82689; Mechanosensitive channel protein MscS (YggB), C-terminal domain; 1.
DR   SUPFAM; SSF82861; Mechanosensitive channel protein MscS (YggB), transmembrane region; 1.
DR   SUPFAM; SSF50182; Sm-like ribonucleoproteins; 1.
DR   PROSITE; PS01246; UPF0003; 1.
PE   3: Inferred from homology;
KW   Cell inner membrane {ECO:0000256|RuleBase:RU369025};
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Ion channel {ECO:0000256|RuleBase:RU369025};
KW   Ion transport {ECO:0000256|RuleBase:RU369025};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU369025};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019918};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW   ECO:0000256|RuleBase:RU369025};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|RuleBase:RU369025}; Transport {ECO:0000256|RuleBase:RU369025}.
FT   TRANSMEM        24..48
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369025"
FT   TRANSMEM        68..91
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369025"
FT   TRANSMEM        97..125
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU369025"
FT   DOMAIN          72..112
FT                   /note="Mechanosensitive ion channel transmembrane helices
FT                   2/3"
FT                   /evidence="ECO:0000259|Pfam:PF21088"
FT   DOMAIN          114..179
FT                   /note="Mechanosensitive ion channel MscS"
FT                   /evidence="ECO:0000259|Pfam:PF00924"
FT   DOMAIN          186..267
FT                   /note="Mechanosensitive ion channel MscS C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21082"
SQ   SEQUENCE   290 AA;  31043 MW;  D66F21594FE44488 CRC64;
     MEDLNVVDSI NNAGGWLVRN QALLLSYAVN IVAAIAIIIF GMIVARIISN ALNKLLIARH
     IDATVADFLS ALVRYGLIAF TLIAALGRIG VQTASVIAVL GAAGLAVGLA LQGSLSNLAA
     GVLLVTFRPF RTGDFIDIGI MGTVLNVQIF STTLKSADGK IVVVPNGKII AGNIVNYSRE
     PVRRNEFIIG VAYDADVDQV ISLLQGVVDA EPRVLKEMGV QIGLNELAAS SVNFVVRCWS
     NAGDLQNVYW DLMKNFKRAL DANNIGIPYP QMDVHLHHDK SAKSPEAVQE
//
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