ID K4KHW9_SIMAS Unreviewed; 781 AA.
AC K4KHW9;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 2.
DT 27-MAR-2024, entry version 70.
DE RecName: Full=Copper-exporting P-type ATPase {ECO:0000256|ARBA:ARBA00015102};
DE EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
DE AltName: Full=Copper-exporting P-type ATPase A {ECO:0000256|ARBA:ARBA00029719};
DE AltName: Full=Cu(+)-exporting ATPase {ECO:0000256|ARBA:ARBA00033239};
GN OrderedLocusNames=M5M_02815 {ECO:0000313|EMBL:AFU97780.2};
OS Simiduia agarivorans (strain DSM 21679 / JCM 13881 / BCRC 17597 / SA1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales;
OC Cellvibrionaceae; Simiduia.
OX NCBI_TaxID=1117647 {ECO:0000313|EMBL:AFU97780.2, ECO:0000313|Proteomes:UP000000466};
RN [1] {ECO:0000313|EMBL:AFU97780.2, ECO:0000313|Proteomes:UP000000466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21679 / JCM 13881 / BCRC 17597 / SA1
RC {ECO:0000313|Proteomes:UP000000466};
RX PubMed=23405302; DOI=10.1128/genomeA.00039-12;
RA Lin S.Y., Shieh W.Y., Chen J.S., Tang S.L.;
RT "Complete genome sequence of Simiduia agarivorans SA1(T), a marine
RT bacterium able to degrade a variety of polysaccharides.";
RL Genome Announc. 1:E00039-E00039(2013).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003746; AFU97780.2; -; Genomic_DNA.
DR AlphaFoldDB; K4KHW9; -.
DR STRING; 1117647.M5M_02815; -.
DR KEGG; saga:M5M_02815; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_5_1_6; -.
DR Proteomes; UP000000466; Chromosome.
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 GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR CDD; cd00371; HMA; 1.
DR CDD; cd02094; P-type_ATPase_Cu-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; 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; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF6; COPPER-EXPORTING P-TYPE ATPASE; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
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; PS50846; HMA_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Cell membrane {ECO:0000256|RuleBase:RU362081};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000000466};
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}.
FT TRANSMEM 132..149
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 161..178
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 199..221
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 227..246
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 380..402
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 408..431
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 724..743
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 749..767
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 40..103
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..18
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 781 AA; 82644 MW; 18251BD8461C9319 CRC64;
MSTMKTESGD VSCHEGGTTT TPHDHHAHKA HHHSSENNPG PQELIIEGAG CASCVGKIES
ALKAVPGVEN AEMNFAQRTV SVTGNVDAAD LVKAVEKSGY NAKIAAAESE DDALAEKEQA
DWAYYKRLMR EMTIALSLGV PLMIYSVVVG EMTVSTTGER IAWLAVGLLT LGVMVFSGKH
FFVGAWQSFK NHSANMDTLI ALGTGTAWVY SMVVVFVPYA VPEMARHVYF EATAMIIGLI
DLGLALELKA RGRTSEAIKR LIGLQAKTAR VIRDEKELDV AIEQVLMDDV VRVRPGEKIP
VDGEVIEGHT AIDESMLTGE PMPVEKTVGD TVAAGTINKT GSILFKATRV GKDTALAQII
NMVKRAQNSK PPIGRLADVI SAYFVPVVMI IAVTSALVWL NFGPDPAVAF AIVSATTVLI
IACPCALGLA TPMSVMVGVG KAAEAGVLIR NGEALQTASK ISAMILDKTG TITLGAPKVT
DILVAGEQHE DTILKLAATL ESGSEHPLAL AIVESAQEKG IETGKVSNFN AIAGHGVQAE
VDGKTLLFGN EKLMRERNIE LGDFVEKAQG LAAEAKTPMY FAVDNQLSAI IAVADPIKED
SIAAIKRLQH NGIRVVMLTG DNRATAKAVA EKAGIKEFFA EVLPEEKSKK VQELQMEGEV
VGMTGDGIND APALAIANVG FAIGTGTDVA IESADITLMR GSLHGLADAI AVSKATLRNI
KQNLFGAFIY NVAGVPFAAG VLYPFFGLLL SPVIAGAAMA FSSLTVVTNA NRLRFFKAQE
H
//
