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Database: UniProt
Entry: H1LMI9_9PAST
LinkDB: H1LMI9_9PAST
Original site: H1LMI9_9PAST 
ID   H1LMI9_9PAST            Unreviewed;      1108 AA.
AC   H1LMI9;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Putative potassium efflux system KefA {ECO:0000313|EMBL:EHO48761.1};
GN   ORFNames=HMPREF9096_00484 {ECO:0000313|EMBL:EHO48761.1};
OS   Haemophilus sp. oral taxon 851 str. F0397.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Haemophilus.
OX   NCBI_TaxID=762965 {ECO:0000313|EMBL:EHO48761.1, ECO:0000313|Proteomes:UP000005305};
RN   [1] {ECO:0000313|EMBL:EHO48761.1, ECO:0000313|Proteomes:UP000005305}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=F0397 {ECO:0000313|EMBL:EHO48761.1,
RC   ECO:0000313|Proteomes:UP000005305};
RA   Weinstock G., Sodergren E., Clifton S., Fulton L., Fulton B., Courtney L.,
RA   Fronick C., Harrison M., Strong C., Farmer C., Delahaunty K., Markovic C.,
RA   Hall O., Minx P., Tomlinson C., Mitreva M., Hou S., Chen J., Wollam A.,
RA   Pepin K.H., Johnson M., Bhonagiri V., Zhang X., Suruliraj S., Warren W.,
RA   Chinwalla A., Mardis E.R., Wilson R.K.;
RL   Submitted (SEP-2011) to the EMBL/GenBank/DDBJ databases.
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}.
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:EHO48761.1}.
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DR   EMBL; AGRK01000008; EHO48761.1; -; Genomic_DNA.
DR   RefSeq; WP_009500064.1; NZ_JH591070.1.
DR   AlphaFoldDB; H1LMI9; -.
DR   PATRIC; fig|762965.3.peg.463; -.
DR   HOGENOM; CLU_007829_3_0_6; -.
DR   Proteomes; UP000005305; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR   GO; GO:0055085; P:transmembrane transport; 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; 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; 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   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..26
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           27..1108
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003551143"
FT   TRANSMEM        487..507
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        536..563
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        569..592
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        613..630
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        642..663
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        684..706
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        793..817
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        837..857
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        878..899
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        911..939
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          52..272
FT                   /note="Mechanosensitive ion channel MscS porin"
FT                   /evidence="ECO:0000259|Pfam:PF12795"
FT   DOMAIN          493..823
FT                   /note="Mechanosensitive ion channel inner membrane"
FT                   /evidence="ECO:0000259|Pfam:PF12794"
FT   DOMAIN          884..925
FT                   /note="Mechanosensitive ion channel transmembrane helices
FT                   2/3"
FT                   /evidence="ECO:0000259|Pfam:PF21088"
FT   DOMAIN          927..991
FT                   /note="Mechanosensitive ion channel MscS"
FT                   /evidence="ECO:0000259|Pfam:PF00924"
FT   DOMAIN          1001..1083
FT                   /note="Mechanosensitive ion channel MscS C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21082"
FT   COILED          121..148
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          182..268
FT                   /evidence="ECO:0000256|SAM:Coils"
SQ   SEQUENCE   1108 AA;  126130 MW;  28A2E3177DD83CD6 CRC64;
     MKTSRFFTAL LATALIGWAT VHPTFAANKS KILLPTEQEL SADLADVQKM ADGDVKTALI
     NELQTSLDLL QLIQTQQKNN EDLHDVLAHA DSEIKKNNAD LLAFKKQLEQ SKSVDYQAQN
     LADLQATLSK LNAQQQETQT ALSKANTQLA GQSSISERAQ TSLTENLKRT QEINQQLADS
     NLTKTLRQKN QIELQLIDLK NAYNQDLLKN SDQLTLLYQS RYDLLNARLQ LLQQQIVAIQ
     EVINQKNLAQ TQNQVEQVQQ QQQNSAKNAY IQKELERNAE LSQYLLQQTE KTNILTQDDL
     RMRNVFDSLT QTQHTIEEQI SALQGTLVLS RIIQQQKQKL PTNLNIQGLS KQIADLRVQI
     FDITQKRNEL YDLDAYIAKV ESDEGEKFTY AEKTQLVNLL TERRKMSSDL IKSLNNQLNL
     AISLELTQQQ ITQISDQIQS KLEQQSFWVK SNNPINLDWF TELPRAFIAQ VDGIVKKIGL
     PTNYSNLPYL LMYCLGLFVV GGAIFKFKYR IKQRLSKING EINRLKYDNQ WNTPQALLLT
     AFLTLSGTLW FLAICQMLGF FFMKNPTEFW DWSFSMAGYW WFFTFWLSLF RPNGIFVRHF
     EFSQQSAVRF QSVIKRIVVA VVLLLNTSVF SNVTDYGLAN DVIGQVNTIV SLLFCIIIIA
     PRFKNVLRSY EDEKKSHNHI IVKIVQFGLQ IIPVGLVILV ALGYYYTALN LIQHLINSYI
     AWCVWWLIRQ VIYRGITVSS RRLAHRRLEE KLRQKQAGFN DGSTSDDVVV LNEKEEGLAL
     NEVRSQLLRF ADLFIWTALI GIFYYVWSDL VAVASYLREV TLWQQTTTTE AGTVMESITL
     FNLLVALVIV GITYVLVRNI SGILEVLIFS RVKLSQGTPY TITTLLTYVL VAVGGAWAFA
     TLGMSWSKLQ WLFAALSVGL GFGMQEIFAN FVSGIILLFE RPIRVGDTVT INGVSGTVAK
     IRIRAITLID FDRKEVIVPN KSFVTGQVIN WALSNTMTRL VINVGVAYGS NLELVKKLLL
     QAANEQTTVL KDPEPRAYFL SFGASTLDHE LRVYVAQLAE RTNTIDALNR RINELFAENN
     IDIAFNQLDV FIKNNDTGEE MPFIEVKK
//
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