ID A8LSW9_DINSH Unreviewed; 781 AA.
AC A8LSW9;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 114.
DE SubName: Full=Heavy metal translocating P-type ATPase {ECO:0000313|EMBL:ABV95336.1};
DE EC=3.6.3.- {ECO:0000313|EMBL:ABV95336.1, ECO:0000313|EMBL:ABV95669.1};
DE SubName: Full=Heavy metal transporting P-type ATPase {ECO:0000313|EMBL:ABV95669.1};
GN OrderedLocusNames=Dshi_3603 {ECO:0000313|EMBL:ABV95336.1}, Dshi_3941
GN {ECO:0000313|EMBL:ABV95669.1};
OS Dinoroseobacter shibae (strain DSM 16493 / NCIMB 14021 / DFL 12).
OG Plasmid pDSHI01 {ECO:0000313|EMBL:ABV95336.1,
OG ECO:0000313|Proteomes:UP000006833}, and
OG Plasmid pDSHI03 {ECO:0000313|EMBL:ABV95669.1,
OG ECO:0000313|Proteomes:UP000006833}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Dinoroseobacter.
OX NCBI_TaxID=398580 {ECO:0000313|EMBL:ABV95336.1, ECO:0000313|Proteomes:UP000006833};
RN [1] {ECO:0000313|EMBL:ABV95336.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DFL 12 {ECO:0000313|EMBL:ABV95336.1};
RC PLASMID=pDSHI01 {ECO:0000313|EMBL:ABV95336.1}, and pDSHI03
RC {ECO:0000313|EMBL:ABV95669.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Thompson L.S., Brettin T., Bruce D., Detter J.C.,
RA Han C., Tapia R., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Kim E., Richardson P.;
RT "Complete sequence of chromosome of Dinoroseobacter shibae DFL 12.";
RL Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:ABV95336.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=DFL 12 {ECO:0000313|EMBL:ABV95336.1};
RC PLASMID=pDSHI01 {ECO:0000313|EMBL:ABV95336.1}, and pDSHI03
RC {ECO:0000313|EMBL:ABV95669.1};
RA Liesegang H., Wagner-Doebler I.;
RT "The Roseobacter - microalgae symbiosis: Adaptation to viral pressure,
RT horizontal gene transfer, and ability to synthesize vitamine B12 under all
RT conditions are revealed by the genome sequence.";
RL Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|Proteomes:UP000006833}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16493 / NCIMB 14021 / DFL 12
RC {ECO:0000313|Proteomes:UP000006833};
RC PLASMID=Plasmid pDSHI01 {ECO:0000313|Proteomes:UP000006833}, and
RC Plasmid pDSHI03 {ECO:0000313|Proteomes:UP000006833};
RX PubMed=19741735; DOI=10.1038/ismej.2009.94;
RA Wagner-Dobler I., Ballhausen B., Berger M., Brinkhoff T., Buchholz I.,
RA Bunk B., Cypionka H., Daniel R., Drepper T., Gerdts G., Hahnke S., Han C.,
RA Jahn D., Kalhoefer D., Kiss H., Klenk H.P., Kyrpides N., Liebl W.,
RA Liesegang H., Meincke L., Pati A., Petersen J., Piekarski T.,
RA Pommerenke C., Pradella S., Pukall R., Rabus R., Stackebrandt E., Thole S.,
RA Thompson L., Tielen P., Tomasch J., von Jan M., Wanphrut N., Wichels A.,
RA Zech H., Simon M.;
RT "The complete genome sequence of the algal symbiont Dinoroseobacter shibae:
RT a hitchhiker's guide to life in the sea.";
RL ISME J. 4:61-77(2010).
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; CP000831; ABV95336.1; -; Genomic_DNA.
DR EMBL; CP000833; ABV95669.1; -; Genomic_DNA.
DR AlphaFoldDB; A8LSW9; -.
DR KEGG; dsh:Dshi_3603; -.
DR KEGG; dsh:Dshi_3941; -.
DR HOGENOM; CLU_001771_11_3_5; -.
DR Proteomes; UP000006833; Plasmid pDSHI01.
DR Proteomes; UP000006833; Plasmid pDSHI03.
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; cd02094; P-type_ATPase_Cu-like; 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; 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; IPR013087; Znf_C2H2_type.
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:SF8; COPPER-TRANSPORTING ATPASE 2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF19335; HMBD; 2.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00943; CUATPASE.
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.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Cell membrane {ECO:0000256|RuleBase:RU362081};
KW Hydrolase {ECO:0000313|EMBL:ABV95336.1};
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 Plasmid {ECO:0000313|EMBL:ABV95336.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000006833};
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 125..148
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 160..178
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 190..213
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 383..405
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 411..434
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 727..749
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 755..774
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 32..54
FT /note="C2H2-type"
FT /evidence="ECO:0000259|PROSITE:PS00028"
SQ SEQUENCE 781 AA; 82940 MW; 10FD8F0C79F62720 CRC64;
MSTPDSSETT AASSVFVCPM HPEVRQDEPG NCPKCGMHLV PESELEVHSA HDHHEHHAGA
TPADGRYDLV PTGHDGPIFT CPMHPQVRQP DPGACPICGM GLELESGVPG DEGPNPELVD
FTRRFWVGTV LTIPLLVLTM GPFVGFPAVR TFFGESTTQW IELILATPVV LWCGWPFLER
GWISFRTLNL NMFSLIGMGV LAAWLFSVVA VLAPDIFPDG FRDSEGHVGV YFEAAAVIVT
LVLLGQVMEL RAREGTGKAI RALLDMAAKT ARVIRDDGSE EEIPLEDVQV GDRLRVRPGD
KVPVDGVVLD GRSSVDESMI SGEPVPVEKT EGDPLTGATI NGTGSLVMEA TRVGSDTMLA
QIVEMVSNAQ RSRAPIQKYA DKVAGYFVPA VIGIAVLSFI AWAIWGPAPA LSYALISAVA
VLIIACPCAL GLATPMSIMT ATGRGAQAGV LIKNAEALER FEKVDTLIVD KTGTLTEGKP
RLVDVLPQPG HDEAEVLRLA ASLERGSEHP LAEAIVRGAE ERDVKMDEAR DFEAVTGKGV
KGVVDGKAVA LGNLAMIREL GLEAGALTAK ANARRDEGET VMFVVLDGEI AGLVAVADPV
KETTPEAIED LHELGFRVIM ATGDNERTAK AIGTRLGIDE IRADVLPEDK ARIILELQEA
GHKVAMAGDG VNDAPALAQA DVGIAMGTGA DVAIESAGVT LVKGNLDGIV RARRLARATM
RNIRQNLFFA LIYNASGVPV AAGVLFPFFG ILISPMFAAF AMSASSISVV LNSLRLRGVR
I
//
