ID Q6N989_RHOPA Unreviewed; 973 AA.
AC Q6N989;
DT 05-JUL-2004, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 145.
DE SubName: Full=Cation transporting P-type ATPase {ECO:0000313|EMBL:CAE27101.1};
GN OrderedLocusNames=RPA1660 {ECO:0000313|EMBL:CAE27101.1};
OS Rhodopseudomonas palustris (strain ATCC BAA-98 / CGA009).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=258594 {ECO:0000313|EMBL:CAE27101.1, ECO:0000313|Proteomes:UP000001426};
RN [1] {ECO:0000313|EMBL:CAE27101.1, ECO:0000313|Proteomes:UP000001426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-98 / CGA009 {ECO:0000313|Proteomes:UP000001426};
RX PubMed=14704707; DOI=10.1038/nbt923;
RA Larimer F.W., Chain P., Hauser L., Lamerdin J., Malfatti S., Do L.,
RA Land M.L., Pelletier D.A., Beatty T.J., Lang A.S., Tabita F.R.,
RA Gibson J.L., Hanson T.E., Torres y Torres J., Peres C., Harrison F.H.,
RA Gibson J., Harwood C.S.;
RT "Complete genome sequence of the metabolically versatile photosynthetic
RT bacterium Rhodopseudomonas palustris.";
RL Nat. Biotechnol. 22:55-61(2004).
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; BX572598; CAE27101.1; -; Genomic_DNA.
DR AlphaFoldDB; Q6N989; -.
DR STRING; 258594.RPA1660; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_11_3_5; -.
DR PhylomeDB; Q6N989; -.
DR Proteomes; UP000001426; 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:0016491; F:oxidoreductase activity; IEA:InterPro.
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 Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 3.
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; IPR009078; Ferritin-like_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; IPR012348; RNR-like.
DR InterPro; IPR011017; TRASH_dom.
DR InterPro; IPR007029; YHS_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:SF8; COPPER-TRANSPORTING ATPASE 2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF19335; HMBD; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR Pfam; PF04945; YHS; 3.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00943; CUATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00746; TRASH; 3.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF47240; Ferritin-like; 3.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS51257; PROKAR_LIPOPROTEIN; 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:UP000001426};
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 319..340
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 352..370
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 382..402
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 422..440
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 571..597
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 603..626
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 919..938
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 944..966
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 49..87
FT /note="TRASH"
FT /evidence="ECO:0000259|SMART:SM00746"
FT DOMAIN 142..180
FT /note="TRASH"
FT /evidence="ECO:0000259|SMART:SM00746"
FT DOMAIN 215..253
FT /note="TRASH"
FT /evidence="ECO:0000259|SMART:SM00746"
SQ SEQUENCE 973 AA; 101252 MW; 767E811DB2E3CE34 CRC64;
MRDAEHAGHD ASVENTGCCG SAGANAPATS SCCGGAGSVA APNAATAIDP VCGMTVDTAT
AQHRLDHDGQ TYYFCCSGCR DTFSADPADV LAKAAKPFTL PPKPAAKLHQ LTELPAKSSC
CGRQGGDGHQ HGEAPVAIKA IDPVCGMTVD VATSKHSFEH DGTTYHFCCG GCRTKFAADP
QRYLAKAASS SCCGGADDHA DHHHGAAADG GKVIDPVCGM KVDPATSKHR FAYKGTTYHF
CREACQTKFA ADPVSYLDKS KAKPAADVPE GTIYTCPMDP QIRQVGPGTC PICGMALEPE
LVSLDDTPNP ELVDMTRRFW IGLVLALPAI VLEMGGHLVG GHGLIDPVLS NWIQFVSATP
VVLWAGWPFF VRGWQSVMTR NLNMFTLVAM GTGVAYIYSL VATVAPQLFP PAFRGHGSTV
PVYFEAAAVI TVLVLLGQVL ELRAREATSG AIKALLGLAP KTARKIDTDG SEHEVEIDSL
SVGDRLRVRP GEKVPVDGTI LDGRGTLDES LVTGESMPVS RETGGKVVAG TLNQSGGFVM
RADQVGRDTM LSRIVQMVAQ AQRSRAPIQR VADLVAGWFV PAVLLAAIAA FAAWAAFGPE
PRLTFALVAA VSVLIIACPC ALGLATPMSI MVGVGRGAQS GVLIRNAEAL ERMEKVDTLV
IDKTGTLTEG RPSVVAIVAA DGTDETELLR LAASVERASE HPLADAIVRA AKQRNLDLGD
VTDFDAPTGK GATGKIAGRT VVIGNPAYLA SLGIDTASLA PKTEQLRGDG DTVVHVAIDG
RFAGLFAIAD AVKPSTPEAL KALAADGIKV IMLTGDNRVT ANAVARKLGI ADVEAEVLPD
QKSAVVEKLR QQGRVVAMAG DGVNDAPALA AADVGIAMGT GTDVAMESAG VTLLKGDLGG
IVRARKLSQA TIRNIRQNLF FAFVYNSAGI PIAAGILYPS FSLLLSPIIA AAAMSLSSVS
VIGNALRLRR TAL
//
