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Database: UniProt
Entry: A4GAC4_HERAR
LinkDB: A4GAC4_HERAR
Original site: A4GAC4_HERAR 
ID   A4GAC4_HERAR            Unreviewed;       422 AA.
AC   A4GAC4;
DT   17-APR-2007, integrated into UniProtKB/TrEMBL.
DT   17-APR-2007, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   SubName: Full=MscS mechanosensitive ion channel {ECO:0000313|EMBL:CAL63461.1};
GN   OrderedLocusNames=HEAR3359 {ECO:0000313|EMBL:CAL63461.1};
OS   Herminiimonas arsenicoxydans.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herminiimonas.
OX   NCBI_TaxID=204773 {ECO:0000313|EMBL:CAL63461.1, ECO:0000313|Proteomes:UP000006697};
RN   [1] {ECO:0000313|EMBL:CAL63461.1, ECO:0000313|Proteomes:UP000006697}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ULPAs1 {ECO:0000313|Proteomes:UP000006697};
RX   PubMed=17432936; DOI=10.1371/journal.pgen.0030053;
RA   Muller D., Medigue C., Koechler S., Barbe V., Barakat M., Talla E.,
RA   Bonnefoy V., Krin E., Arsene-Ploetze F., Carapito C., Chandler M.,
RA   Cournoyer B., Cruveiller S., Dossat C., Duval S., Heymann M., Leize E.,
RA   Lieutaud A., Lievremont D., Makita Y., Mangenot S., Nitschke W., Ortet P.,
RA   Perdrial N., Schoepp B., Siguier N., Simeonova D.D., Rouy Z., Segurens B.,
RA   Turlin E., Vallenet D., Van Dorsselaer A., Weiss S., Weissenbach J.,
RA   Lett M.C., Danchin A., Bertin P.N.;
RT   "A tale of two oxidation states: bacterial colonization of arsenic-rich
RT   environments.";
RL   PLoS Genet. 3:518-530(2007).
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; CU207211; CAL63461.1; -; Genomic_DNA.
DR   AlphaFoldDB; A4GAC4; -.
DR   STRING; 204773.HEAR3359; -.
DR   KEGG; har:HEAR3359; -.
DR   eggNOG; COG0668; Bacteria.
DR   HOGENOM; CLU_037945_0_2_4; -.
DR   OrthoDB; 9775207at2; -.
DR   Proteomes; UP000006697; Chromosome.
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; IPR011014; MscS_channel_TM-2.
DR   PANTHER; PTHR30566:SF25; INNER MEMBRANE PROTEIN-RELATED; 1.
DR   PANTHER; PTHR30566; YNAI-RELATED MECHANOSENSITIVE ION CHANNEL; 1.
DR   Pfam; PF21088; MS_channel_1st; 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.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006697};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        61..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        115..133
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        139..155
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        186..204
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        210..230
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          187..227
FT                   /note="Mechanosensitive ion channel transmembrane helices
FT                   2/3"
FT                   /evidence="ECO:0000259|Pfam:PF21088"
FT   DOMAIN          228..296
FT                   /note="Mechanosensitive ion channel MscS"
FT                   /evidence="ECO:0000259|Pfam:PF00924"
FT   DOMAIN          302..385
FT                   /note="Mechanosensitive ion channel MscS C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF21082"
SQ   SEQUENCE   422 AA;  47030 MW;  1AAE660B77FE3BBD CRC64;
     MPQSICIFAC RKHLRTIQLL RPLIFRARTA GKSQQAARNR RNRHMAVLQN WMVFGISLES
     WLYALITTCL IYLLLDVLTR STVHLAKRRI ALPPKAASRR INQVVVGMAP GSKRYLYFLF
     ALLIGLQTLL LPATLELRLF QAGVIVVGIQ ALLWINRGIN TWLEDLDISG INPDLRKRAT
     TTTMVFLLRL AVMLTVVLTV LANLGVNITA FVASLGIGGI AIALALQTIL SDLFASLSIG
     LDKPFEVGDF IIVDEVMLGT VEYIGVKTTR LRSLGGEQLV RSNTELLKSV IRNYKRMAER
     RIVFSFGIRY ETPLAKVGQL GSVLGEIISA IDNTRFDRAH FVKFGASSLD FEVVYYVLSS
     DYNTYMDIQQ RINLELMQAC AQRGILFARP TSILHFGSEV RLASAEIEAV NKDAATLQDM
     PG
//
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