ID D2JAJ7_STAAU Unreviewed; 726 AA.
AC D2JAJ7;
DT 09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT 09-FEB-2010, sequence version 1.
DT 27-MAR-2024, entry version 108.
DE RecName: Full=Cd(2+)-exporting ATPase {ECO:0000256|ARBA:ARBA00039103};
DE EC=7.2.2.21 {ECO:0000256|ARBA:ARBA00039103};
GN Name=cadA {ECO:0000313|EMBL:AEH58924.1};
GN ORFNames=SAP054A_034 {ECO:0000313|EMBL:ACZ69004.1}, SAP067A_034
GN {ECO:0000313|EMBL:ACZ69207.1}, SAP075A_034
GN {ECO:0000313|EMBL:ACZ69320.1}, SAP076A_021
GN {ECO:0000313|EMBL:ACZ68846.1}, SAP077A_028
GN {ECO:0000313|EMBL:ACZ68895.1}, SAP078A_034
GN {ECO:0000313|EMBL:ACZ68959.1}, SAP102A_010
GN {ECO:0000313|EMBL:ADA80757.1};
OS Staphylococcus aureus.
OG Plasmid SAP054A {ECO:0000313|EMBL:ACZ69004.1},
OG Plasmid SAP067A {ECO:0000313|EMBL:ACZ69207.1},
OG Plasmid SAP075A {ECO:0000313|EMBL:ACZ69320.1},
OG Plasmid SAP076A {ECO:0000313|EMBL:ACZ68846.1},
OG Plasmid SAP077A {ECO:0000313|EMBL:ACZ68895.1},
OG Plasmid SAP078A {ECO:0000313|EMBL:ACZ68959.1},
OG Plasmid SAP102A {ECO:0000313|EMBL:ADA80757.1}, and
OG Plasmid unnamed {ECO:0000313|EMBL:AEH58924.1}.
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=1280 {ECO:0000313|EMBL:ACZ68846.1};
RN [1] {ECO:0000313|EMBL:ACZ68846.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=49 {ECO:0000313|EMBL:ACZ69004.1}, 879R4RF
RC {ECO:0000313|EMBL:ACZ68895.1}, A78R1 {ECO:0000313|EMBL:ACZ68959.1},
RC B111 {ECO:0000313|EMBL:ACZ69320.1}, PM62
RC {ECO:0000313|EMBL:ACZ69207.1}, PM86 {ECO:0000313|EMBL:ACZ68846.1}, and
RC SK6523 {ECO:0000313|EMBL:ADA80757.1};
RC PLASMID=SAP054A {ECO:0000313|EMBL:ACZ69004.1}, SAP067A
RC {ECO:0000313|EMBL:ACZ69207.1}, SAP075A {ECO:0000313|EMBL:ACZ69320.1},
RC SAP076A {ECO:0000313|EMBL:ACZ68846.1}, SAP077A
RC {ECO:0000313|EMBL:ACZ68895.1}, SAP078A {ECO:0000313|EMBL:ACZ68959.1},
RC and SAP102A {ECO:0000313|EMBL:ADA80757.1};
RA Gill J., Borman J., Shetty J., Hostetler J., Durkin S., Montgomery B.;
RL Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ACZ68846.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=49 {ECO:0000313|EMBL:ACZ69004.1}, 879R4RF
RC {ECO:0000313|EMBL:ACZ68895.1}, A78R1 {ECO:0000313|EMBL:ACZ68959.1},
RC B111 {ECO:0000313|EMBL:ACZ69320.1}, PM62
RC {ECO:0000313|EMBL:ACZ69207.1}, PM86 {ECO:0000313|EMBL:ACZ68846.1}, and
RC SK6523 {ECO:0000313|EMBL:ADA80757.1};
RC PLASMID=SAP054A {ECO:0000313|EMBL:ACZ69004.1}, SAP067A
RC {ECO:0000313|EMBL:ACZ69207.1}, SAP075A {ECO:0000313|EMBL:ACZ69320.1},
RC SAP076A {ECO:0000313|EMBL:ACZ68846.1}, SAP077A
RC {ECO:0000313|EMBL:ACZ68895.1}, SAP078A {ECO:0000313|EMBL:ACZ68959.1},
RC and SAP102A {ECO:0000313|EMBL:ADA80757.1};
RA Summers A.O., Shearer J., Wireman J.;
RL Submitted (DEC-2009) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:AEH58924.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=ATCC 12600 {ECO:0000313|EMBL:AEH58924.1};
RC PLASMID=unnamed {ECO:0000313|EMBL:AEH58924.1};
RA Hoogewerf A.J., Buit T.S., Roukema D.H., Resseguie E.A.;
RT "Cadmium Resistance Cassette in S. aureus ATCC 12600.";
RL Submitted (NOV-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + Cd(2+)(in) + H2O = ADP + Cd(2+)(out) + H(+) + phosphate;
CC Xref=Rhea:RHEA:12132, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:48775,
CC ChEBI:CHEBI:456216; EC=7.2.2.21;
CC Evidence={ECO:0000256|ARBA:ARBA00036510};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362081}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000256|ARBA:ARBA00006024,
CC ECO:0000256|RuleBase:RU362081}.
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DR EMBL; GQ900427; ACZ68846.1; -; Genomic_DNA.
DR EMBL; GQ900428; ACZ68895.1; -; Genomic_DNA.
DR EMBL; GQ900430; ACZ68959.1; -; Genomic_DNA.
DR EMBL; GQ900477; ACZ69004.1; -; Genomic_DNA.
DR EMBL; GQ900483; ACZ69207.1; -; Genomic_DNA.
DR EMBL; GQ900486; ACZ69320.1; -; Genomic_DNA.
DR EMBL; GQ900496; ADA80757.1; -; Genomic_DNA.
DR EMBL; HQ634347; AEH58924.1; -; Genomic_DNA.
DR RefSeq; WP_000378396.1; NZ_WKIY01000085.1.
DR RefSeq; YP_006938426.1; NC_013340.1.
DR RefSeq; YP_006939386.1; NC_018965.1.
DR RefSeq; YP_006940880.1; NC_019009.1.
DR PATRIC; fig|1280.3363.peg.1161; -.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR CDD; cd00371; HMA; 1.
DR CDD; cd07545; P-type_ATPase_Cd-like; 1.
DR Gene3D; 3.30.70.100; -; 1.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 1.
DR Gene3D; 2.70.150.10; Calcium-transporting ATPase, cytoplasmic transduction domain A; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01511; ATPase-IB1_Cu; 1.
DR NCBIfam; TIGR01512; ATPase-IB2_Cd; 1.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR48085; CADMIUM/ZINC-TRANSPORTING ATPASE HMA2-RELATED; 1.
DR PANTHER; PTHR48085:SF5; CADMIUM_ZINC-TRANSPORTING ATPASE HMA2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00941; CDATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF55008; HMA, heavy metal-associated domain; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Cadmium {ECO:0000256|ARBA:ARBA00022539};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475,
KW ECO:0000256|RuleBase:RU362081}; Hydrolase {ECO:0000313|EMBL:ACZ69004.1};
KW Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Plasmid {ECO:0000313|EMBL:ACZ68846.1};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362081}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 106..123
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 129..147
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 331..351
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 363..387
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 673..693
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 699..718
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 11..74
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 726 AA; 78361 MW; E78D9DF405057438 CRC64;
MDSSAKTLTE DKQVYRVEGF SCANCAGKFE KNVKQLAGVQ DAKVNFGASK IDVYGNASVQ
ELEKAGAFEN LKVFPEKLAN SSMQAVKEDT KAPKEEKIPF YKKHSTLLFA TLLIAFGYLS
HFVNGEDNLV TSMLFVGSIV IGGYSLFKVG FQNLIRFDFD MKTLMTVAVI GAAIIGEWAE
ASIVVVLFAI SEALERFSMD RARQSIRSLM DIAPKEALVM RNGQEIMIHV DDIAVGDIMI
VKPGEKIAMD GIIINGVSAV NQAAITGESV PVAKTVDDEV FAGTLNEEGL LEVKITKYVE
DTTISKIIHL VEEAQGERAP AQAFVDKFAK YYTPIIMVIA ALVAVVPPLF FGGSWDTWVY
QGLAVLVVGC PCALVISTPI SIVSAIGNAA KKGVLIKGGV YLEELGAIKA IAFDKTGTLT
KGVPVVTDFK VLNDQVEEKE LFSIITALEY RSQHPLASAI MKKAEQDNIT YSDVRVEDFT
SITGRGIQGN IDGTTYYIGS PRLFKELNVS DFSLEFENKV KVLQNQGKTA MIIGTDQTIL
GVIAVADEVR ETSKNVIQKL HQLGIKQTIM LTGDNQGTAE AIGAHVGVSD IQSELMPQDK
LDYIKKMKAE HGNVAMIGDG VNDAPALAAS TVGIAMGGAG TDTAIETADI ALMGDDLSKL
PFAVRLSRKT LNIIKANITF AIGIKIIALL LVIPGWLTLW IAILSDMGAT ILVALNSLRL
MRVKDK
//
