ID B7MDY7_ECO45 Unreviewed; 1120 AA.
AC B7MDY7;
DT 10-FEB-2009, integrated into UniProtKB/TrEMBL.
DT 10-FEB-2009, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Mechanosensitive channel {ECO:0008006|Google:ProtNLM};
GN Name=kefA {ECO:0000313|EMBL:CAR01809.1};
GN OrderedLocusNames=ECS88_0462 {ECO:0000313|EMBL:CAR01809.1};
OS Escherichia coli O45:K1 (strain S88 / ExPEC).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=585035 {ECO:0000313|EMBL:CAR01809.1, ECO:0000313|Proteomes:UP000000747};
RN [1] {ECO:0000313|Proteomes:UP000000747}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S88 / ExPEC {ECO:0000313|Proteomes:UP000000747};
RX PubMed=19165319; DOI=10.1371/journal.pgen.1000344;
RA Touchon M., Hoede C., Tenaillon O., Barbe V., Baeriswyl S., Bidet P.,
RA Bingen E., Bonacorsi S., Bouchier C., Bouvet O., Calteau A., Chiapello H.,
RA Clermont O., Cruveiller S., Danchin A., Diard M., Dossat C., Karoui M.E.,
RA Frapy E., Garry L., Ghigo J.M., Gilles A.M., Johnson J., Le Bouguenec C.,
RA Lescat M., Mangenot S., Martinez-Jehanne V., Matic I., Nassif X., Oztas S.,
RA Petit M.A., Pichon C., Rouy Z., Ruf C.S., Schneider D., Tourret J.,
RA Vacherie B., Vallenet D., Medigue C., Rocha E.P.C., Denamur E.;
RT "Organised genome dynamics in the Escherichia coli species results in
RT highly diverse adaptive paths.";
RL PLoS Genet. 5:E1000344-E1000344(2009).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the MscS (TC 1.A.23) family.
CC {ECO:0000256|ARBA:ARBA00008017}.
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DR EMBL; CU928161; CAR01809.1; -; Genomic_DNA.
DR RefSeq; WP_000177749.1; NC_011742.1.
DR AlphaFoldDB; B7MDY7; -.
DR KEGG; ecz:ECS88_0462; -.
DR HOGENOM; CLU_007829_3_0_6; -.
DR Proteomes; UP000000747; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0022857; F:transmembrane transporter activity; IEA:UniProt.
DR Gene3D; 1.10.287.1260; -; 1.
DR Gene3D; 2.30.30.60; -; 1.
DR Gene3D; 3.30.70.100; -; 1.
DR InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR InterPro; IPR010920; LSM_dom_sf.
DR InterPro; IPR049142; MS_channel_1st.
DR InterPro; IPR049278; MS_channel_C.
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 InterPro; IPR025692; MscS_IM_dom1.
DR InterPro; IPR024393; MscS_porin.
DR PANTHER; PTHR30347:SF8; MECHANOSENSITIVE CHANNEL MSCK; 1.
DR PANTHER; PTHR30347; POTASSIUM CHANNEL RELATED; 1.
DR Pfam; PF21088; MS_channel_1st; 1.
DR Pfam; PF00924; MS_channel_2nd; 1.
DR Pfam; PF21082; MS_channel_3rd; 1.
DR Pfam; PF12795; MscS_porin; 1.
DR Pfam; PF12794; MscS_TM; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 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 membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000000747};
KW Signal {ECO:0000256|SAM:SignalP};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..33
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 34..1120
FT /note="Mechanosensitive channel"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002860377"
FT TRANSMEM 499..522
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 560..579
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 585..606
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 630..646
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 658..679
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 691..716
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 728..747
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 796..820
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 840..860
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 881..902
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 914..942
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 50..289
FT /note="Mechanosensitive ion channel MscS porin"
FT /evidence="ECO:0000259|Pfam:PF12795"
FT DOMAIN 509..826
FT /note="Mechanosensitive ion channel inner membrane"
FT /evidence="ECO:0000259|Pfam:PF12794"
FT DOMAIN 887..928
FT /note="Mechanosensitive ion channel transmembrane helices
FT 2/3"
FT /evidence="ECO:0000259|Pfam:PF21088"
FT DOMAIN 930..995
FT /note="Mechanosensitive ion channel MscS"
FT /evidence="ECO:0000259|Pfam:PF00924"
FT DOMAIN 1004..1086
FT /note="Mechanosensitive ion channel MscS C-terminal"
FT /evidence="ECO:0000259|Pfam:PF21082"
FT COILED 130..164
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1120 AA; 127219 MW; 5FF04A046E2A1CC1 CRC64;
MTMFQYYKRS RHFVFSAFIA FVFVLLCQNT AFARASSNGD LPTKADLQAQ LDSLNKQKDL
SAQDKLVQQD LTDTLATLDK IDRVKEETVQ LRQKVAEAPE KMRQATAALT ALSDVDNDEE
TRKILSTLSL RQLETRVAQA LDDLQNAQND LASYNSQLVS LQTQPERVQN AMYNASQQLQ
QIRSRLDGTD VGETALRPSQ KVLMQAQQAL LNAEIDQQRK SLEGNTVLQD TLQKQRDYVT
ANSARLEHQL QLLQEAVNSK RLTLTEKTAQ EAVSPDEAAR IQANPLVKQE LEINQQLSQR
LITATENGNQ LMQQNIKVKN WLERALQSER NIKEQIAVLK GSLLLSRILY QQQQTLPSAD
ELENMTNRIA DLRLEQFEVN QQRDALFQSD AFVSKLEEGH TNEVNSEVHD ALLQVVDMRR
ELLDQLNKQL GNQLMMAINL QINQQQLMSV SKNLKSILTQ QIFWVNSNRP MDWDWIKAFP
QTLKDEFKSM KITVNWEKAW PAVFIAFLAG LPLLLIAGLI HWRLGWLKAY QQKLASAVGS
LRNDSQLNTP KAILIDLIRA LPVCLIILAV GLILLTMQLN ISELLWSFSK KLAIFWLVFG
LCWKVLEKNG VAVRHFGMPE QQTSHWRRQI VRISLALLPI HFWSVVAELS PLHLMDDVLG
QAMIFFNLLL IAFLVWPMCR ESWRDKESHT MRLVTITVLS IIPIALMVLT ATGYFYTTLR
LSGRWIETVY LVIIWNLLYQ TVLRGLSVAA RRIAWRRALA RRQNLVKEGA EGAEPPEEPT
IALEQVNQQT LRITMLLMFA LFGVMFWAIW SDLITVFSYL DSITLWHYNA TEAGAAVVKN
VTMGSLLFAI IASMVAWALI RNLPGLLEVL VLSRLNMRQG ASYAITTILN YIIIAVGAMT
VFGSLGVSWD KLQWLAAALS VGLGFGLQEI FGNFVSGLII LFERPVRIGD TVTIGSFSGT
VSKIRIRATT ITDFDRKEVI IPNKAFVTER LINWSLTDTT TRLVIRLGVA YGSDLEKVRK
VLLKAATEHP RVMHEPMPEV FFTAFGASTL DHELRLYVRE LRDRSRTVDE LNRTIDQLCR
ENDINIAFNQ LEVHLHNEKG DEVTEVKRDY KGDDPTPAVG
//
