ID I3C1J3_9FLAO Unreviewed; 705 AA.
AC I3C1J3;
DT 11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT 11-JUL-2012, sequence version 1.
DT 27-MAR-2024, entry version 56.
DE SubName: Full=Copper/silver-translocating P-type ATPase,heavy metal-translocating P-type ATPase, Cd/Co/Hg/Pb/Zn-transporting {ECO:0000313|EMBL:EIJ37486.1};
GN ORFNames=JoomaDRAFT_0432 {ECO:0000313|EMBL:EIJ37486.1};
OS Galbibacter orientalis DSM 19592.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Galbibacter.
OX NCBI_TaxID=926559 {ECO:0000313|EMBL:EIJ37486.1, ECO:0000313|Proteomes:UP000004690};
RN [1] {ECO:0000313|EMBL:EIJ37486.1, ECO:0000313|Proteomes:UP000004690}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19592 {ECO:0000313|EMBL:EIJ37486.1,
RC ECO:0000313|Proteomes:UP000004690};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Peters L., Chertkov O., Ovchinnikova G., Kyrpides N., Mavromatis K.,
RA Detter J.C., Han C., Land M., Hauser L., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Tindall B., Brambilla E., Klenk H.-P.,
RA Eisen J.A.;
RT "Improved High-Quality Draft genome of Joostella marina DSM 19592.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
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; JH651380; EIJ37486.1; -; Genomic_DNA.
DR RefSeq; WP_008616392.1; NZ_JH651380.1.
DR AlphaFoldDB; I3C1J3; -.
DR STRING; 926559.JoomaDRAFT_0432; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_11_2_10; -.
DR OrthoDB; 1521937at2; -.
DR Proteomes; UP000004690; Unassembled WGS sequence.
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 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; 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; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF8; COPPER-TRANSPORTING ATPASE 2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 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 PROSITE; PS00154; ATPASE_E1_E2; 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:UP000004690};
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 70..91
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 103..124
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 131..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 315..340
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 346..373
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 650..669
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 675..695
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT REGION 1..54
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 705 AA; 76849 MW; 948E4E35C4EA78A6 CRC64;
MENHEHHNHD EMDHSKMDHS KMDHSKMKHK KEDHSKMNHK GGDHSGHNPG HGQMGHDHHK
MMIADFRKRF WVTLILTIPI LIISPMIQGF IGYEFLLPGN QYILFGLSSV VYFYGGWPFI
TGFWSEVKKG APGMMTLISM AITVAYVYSS ATVFGLEGVD FFWELATLIA IMLVGHWIEM
KSVLGASKAL QLLVSMMPAE AHRVKGDTIE DIPLEDLLKD DVILVKPGEK VPADGIITEG
TSYLNESMLT GESKPVKKEI DDKVIGGSVN GNGSIKVKVE HTGKDSYLNK VITMVEEAQK
SKSKMQNLSD RAAKWLTYIA LGIGFGTLAV WLILGFPFVY ALERMVTVMI IACPHALGLA
IPLVVAISTA VSAQNGLLIR NRTAFEESRK ITALLFDKTG TLTKGDFGVT RVESVNQKYP
PKEILRLSSA LEQSSEHPIA VGIIKKVKED EVIIPNPENF NAITGKGVEA NVEGKEIKVV
SPGYLRDEKI TIPEDAYSDA AETVVFVLID GKLAGYIALA DEIRPESADA IKIFKKNNIK
VLMATGDNER TAKAVSDKLG LDGYYAEVLP HQKVEIVKEL ESKGEFVAMT GDGVNDAPAL
AQANVGIAVG SGTDVAAETA DIILVNSNPQ DIANLILFGK ATYNKMIQNL VWATGYNVIA
IPLAAGVLYS TGFVLGPAVG AVFMSLSTII VAINAQLLKR KIGKK
//
