ID   SILP_SALTM              Reviewed;         824 AA.
AC   Q9ZHC7;
DT   27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 123.
DE   RecName: Full=Silver exporting P-type ATPase;
DE            EC=7.2.2.15 {ECO:0000269|PubMed:9930866};
GN   Name=silP;
OS   Salmonella typhimurium.
OG   Plasmid pMG101.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Salmonella.
OX   NCBI_TaxID=90371;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND CATALYTIC ACTIVITY.
RX   PubMed=9930866; DOI=10.1038/5545;
RA   Gupta A., Matsui K., Lo J.-F., Silver S.;
RT   "Molecular basis for resistance to silver cations in Salmonella.";
RL   Nat. Med. 5:183-188(1999).
CC   -!- FUNCTION: Component of the sil cation-efflux system that confers
CC       resistance to silver.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Ag(+)(in) + ATP + H2O = ADP + Ag(+)(out) + H(+) + phosphate;
CC         Xref=Rhea:RHEA:14733, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:49468,
CC         ChEBI:CHEBI:456216; EC=7.2.2.15;
CC         Evidence={ECO:0000269|PubMed:9930866};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC       family. Type IB subfamily. {ECO:0000305}.
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DR   EMBL; AF067954; AAD11750.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q9ZHC7; -.
DR   SMR; Q9ZHC7; -.
DR   TCDB; 3.A.3.5.4; the p-type atpase (p-atpase) superfamily.
DR   KEGG; ag:AAD11750; -.
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:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0015445; F:P-type silver transporter activity; IEA:UniProtKB-EC.
DR   Gene3D; 3.40.1110.10; -; 1.
DR   Gene3D; 3.40.50.1000; -; 1.
DR   InterPro; IPR023299; ATPase_P-typ_cyto_dom_N.
DR   InterPro; IPR018303; ATPase_P-typ_P_site.
DR   InterPro; IPR023298; ATPase_P-typ_TM_dom_sf.
DR   InterPro; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR045800; HMBD.
DR   InterPro; IPR027256; P-typ_ATPase_IB.
DR   InterPro; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   InterPro; IPR011017; TRASH_dom.
DR   InterPro; IPR007029; YHS_dom.
DR   Pfam; PF19335; HMBD; 1.
DR   Pfam; PF04945; YHS; 1.
DR   SFLD; SFLDF00027; p-type_atpase; 1.
DR   SMART; SM00746; TRASH; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   SUPFAM; SSF81653; SSF81653; 1.
DR   SUPFAM; SSF81665; SSF81665; 1.
DR   TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 1.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Cell membrane; Membrane; Metal-binding; Nucleotide-binding;
KW   Phosphoprotein; Plasmid; Translocase; Transmembrane; Transmembrane helix.
FT   CHAIN           1..824
FT                   /note="Silver exporting P-type ATPase"
FT                   /id="PRO_0000046331"
FT   TRANSMEM        167..187
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        200..220
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        234..254
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        268..288
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        427..447
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        455..475
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        764..784
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        785..805
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          89..112
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        511
FT                   /note="4-aspartylphosphate intermediate"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   824 AA;  88221 MW;  56A983D256C9AD1C CRC64;
     MLQICIRRVT VKNDNAVEHN NQDCFLSRTS SRDESHALHK VRESVCGMVI LPDKAHSSIR
     YQDHQLYFCS ASCESKFKAH PDHYFTEDAS EHHHHHDHHE VSPDKIKQSH RQAEKEISEG
     VWTCPMHPEI RRSGPGSCPV CGMALEPLVA TASTGTSDEL RDMTRRFWLG LLLAFPVLIL
     EMGSHLFPAL RNTVPPQYNT WLQLLLASPV VLWCGWPFFA RAGMSLRNRS LNMFTLVAMG
     TGVAWVYSVI ATVFPSWFPA SFRNMDGLVA IYFEAAAVIT VLVLLGQVLE LRAREQTSGA
     ITALLNLAPK TARRLDQDGH ETDINAEDVL PGDKLRIRPG ESIPVDGIVV EGKTTVDESM
     VTGESMPVTK TEGEPVIGGT INQTGSLIIR AEKVGDETML SRIVQMVADA QRSRAPIQRM
     ADSVSGWFVP LVILIAVVAF MIWSVWGPEP RMAHGLIAAV SVLIIACPCA LGLATPMSIM
     VGVGKGAQAG VLIKNAEALE RLEKVDTLVV DKTGTLTEGS PTVTGIISLN PGGETSLLRV
     TAAVDKGSQH PLGMAVVKAA QEKGIAIPAV THFNAPSGKG VSGDVEGQRV VIGNELAMQE
     NSIVIDNQKA VADTLRMEGT TVIYVATDGH LAGLIAISDP VKATTPDALK ALRQAGIRIV
     MLTGDNQLTA EAVARKLGID EVEAGILPDG KKAVITRLKA SGHVVAMAGD GVNDAPALAA
     ADVGIAMGTG TDVAIESAGV TLLKGDLMIL NRARHLSEIT MKNIRQNLFF AFIYNALGVP
     VAAGLLYPVY GILLSPVIAA AAMALSSVSV IVNALRLKSV RLGK