YNAI_ECOLI
ID YNAI_ECOLI Reviewed; 343 AA.
AC P0AEB5; P77253;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Low conductance mechanosensitive channel YnaI;
GN Name=ynaI; OrderedLocusNames=b1330, JW1323;
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 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 TOPOLOGY [LARGE SCALE ANALYSIS], AND SUBCELLULAR LOCATION.
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=15919996; DOI=10.1126/science.1109730;
RA Daley D.O., Rapp M., Granseth E., Melen K., Drew D., von Heijne G.;
RT "Global topology analysis of the Escherichia coli inner membrane
RT proteome.";
RL Science 308:1321-1323(2005).
RN [5]
RP FUNCTION, SUBUNIT, AND SUBCELLULAR LOCATION.
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.
CC {ECO:0000269|PubMed:22874652}.
CC -!- SUBUNIT: Homoheptamer. {ECO:0000269|PubMed:22874652}.
CC -!- INTERACTION:
CC P0AEB5; P0AEB5: ynaI; NbExp=2; IntAct=EBI-9141361, EBI-9141361;
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000269|PubMed:15919996,
CC ECO:0000269|PubMed:22874652}; Multi-pass membrane protein
CC {ECO:0000269|PubMed:15919996, ECO:0000269|PubMed:22874652}.
CC -!- SIMILARITY: Belongs to the MscS (TC 1.A.23) family. {ECO:0000305}.
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DR EMBL; U00096; AAC74412.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA14923.1; -; Genomic_DNA.
DR PIR; E64882; E64882.
DR RefSeq; NP_415846.1; NC_000913.3.
DR RefSeq; WP_000559900.1; NZ_STEB01000005.1.
DR PDB; 6URT; EM; 3.27 A; A/B/C/D/E/F/G=1-343.
DR PDB; 6ZYD; EM; 3.00 A; A/B/C/D/E/F/G=1-343.
DR PDB; 6ZYE; EM; 4.10 A; A/B/C/D/E/F/G=1-343.
DR PDBsum; 6URT; -.
DR PDBsum; 6ZYD; -.
DR PDBsum; 6ZYE; -.
DR AlphaFoldDB; P0AEB5; -.
DR SMR; P0AEB5; -.
DR BioGRID; 4260142; 225.
DR BioGRID; 850264; 3.
DR DIP; DIP-12740N; -.
DR IntAct; P0AEB5; 4.
DR STRING; 511145.b1330; -.
DR TCDB; 1.A.23.4.3; the small conductance mechanosensitive ion channel (mscs) family.
DR PaxDb; P0AEB5; -.
DR PRIDE; P0AEB5; -.
DR EnsemblBacteria; AAC74412; AAC74412; b1330.
DR EnsemblBacteria; BAA14923; BAA14923; BAA14923.
DR GeneID; 66674841; -.
DR GeneID; 945898; -.
DR KEGG; ecj:JW1323; -.
DR KEGG; eco:b1330; -.
DR PATRIC; fig|1411691.4.peg.947; -.
DR EchoBASE; EB3683; -.
DR eggNOG; COG0668; Bacteria.
DR HOGENOM; CLU_037945_0_0_6; -.
DR InParanoid; P0AEB5; -.
DR OMA; ITQRVEN; -.
DR PhylomeDB; P0AEB5; -.
DR PRO; PR:P0AEB5; -.
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:0042802; F:identical protein binding; IPI:IntAct.
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; IPR045042; YnaI-like.
DR PANTHER; PTHR43634; PTHR43634; 1.
DR Pfam; PF00924; MS_channel; 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 3D-structure; Cell inner membrane; Cell membrane; Ion channel;
KW Ion transport; Membrane; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..343
FT /note="Low conductance mechanosensitive channel YnaI"
FT /id="PRO_0000110242"
FT TOPO_DOM 1..9
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 10..30
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 31..40
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 41..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 62..77
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 78..98
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 99..125
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147
FT /note="Periplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 148..168
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 169..343
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT HELIX 5..11
FT /evidence="ECO:0007829|PDB:6URT"
FT HELIX 13..30
FT /evidence="ECO:0007829|PDB:6URT"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:6URT"
FT HELIX 41..67
FT /evidence="ECO:0007829|PDB:6URT"
FT HELIX 80..107
FT /evidence="ECO:0007829|PDB:6ZYD"
FT HELIX 112..138
FT /evidence="ECO:0007829|PDB:6ZYD"
FT HELIX 142..175
FT /evidence="ECO:0007829|PDB:6ZYD"
FT STRAND 184..187
FT /evidence="ECO:0007829|PDB:6ZYD"
FT STRAND 190..199
FT /evidence="ECO:0007829|PDB:6ZYD"
FT STRAND 201..208
FT /evidence="ECO:0007829|PDB:6ZYD"
FT STRAND 213..217
FT /evidence="ECO:0007829|PDB:6ZYD"
FT HELIX 218..222
FT /evidence="ECO:0007829|PDB:6ZYD"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:6ZYD"
FT STRAND 235..243
FT /evidence="ECO:0007829|PDB:6ZYD"
FT HELIX 245..250
FT /evidence="ECO:0007829|PDB:6ZYD"
FT HELIX 251..262
FT /evidence="ECO:0007829|PDB:6ZYD"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:6URT"
FT STRAND 270..272
FT /evidence="ECO:0007829|PDB:6ZYD"
FT STRAND 274..282
FT /evidence="ECO:0007829|PDB:6ZYD"
FT STRAND 285..295
FT /evidence="ECO:0007829|PDB:6ZYD"
FT HELIX 299..320
FT /evidence="ECO:0007829|PDB:6ZYD"
FT STRAND 328..332
FT /evidence="ECO:0007829|PDB:6ZYD"
SQ SEQUENCE 343 AA; 38755 MW; 469F0B7909480D13 CRC64;
MIAELFTNNA LNLVIIFGSC AALILMSFWF RRGNRKRKGF LFHAVQFLIY TIIISAVGSI
INYVIENYKL KFITPGVIDF ICTSLIAVIL TIKLFLLINQ FEKQQIKKGR DITSARIMSR
IIKITIIVVL VLLYGEHFGM SLSGLLTFGG IGGLAVGMAG KDILSNFFSG IMLYFDRPFS
IGDWIRSPDR NIEGTVAEIG WRITKITTFD NRPLYVPNSL FSSISVENPG RMTNRRITTT
IGLRYEDAAK VGVIVEAVRE MLKNHPAIDQ RQTLLVYFNQ FADSSLNIMV YCFTKTTVWA
EWLAAQQDVY LKIIDIVQSH GADFAFPSQT LYMDNITPPE QGR
