ID A3WG84_9SPHN Unreviewed; 707 AA.
AC A3WG84;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 104.
DE SubName: Full=E1-E2 type cation ATPase {ECO:0000313|EMBL:EAQ29084.1};
GN ORFNames=NAP1_15833 {ECO:0000313|EMBL:EAQ29084.1};
OS Erythrobacter sp. NAP1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae; Erythrobacter/Porphyrobacter group; Erythrobacter.
OX NCBI_TaxID=237727 {ECO:0000313|EMBL:EAQ29084.1, ECO:0000313|Proteomes:UP000002995};
RN [1] {ECO:0000313|EMBL:EAQ29084.1, ECO:0000313|Proteomes:UP000002995}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NAP1 {ECO:0000313|EMBL:EAQ29084.1,
RC ECO:0000313|Proteomes:UP000002995};
RX PubMed=21952547; DOI=10.1128/JB.05845-11;
RA Koblizek M., Janouskovec J., Obornik M., Johnson J.H., Ferriera S.,
RA Falkowski P.G.;
RT "Genome Sequence of the Marine Photoheterotrophic Bacterium Erythrobacter
RT sp. Strain NAP1.";
RL J. Bacteriol. 193:5881-5882(2011).
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EAQ29084.1}.
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DR EMBL; AAMW01000002; EAQ29084.1; -; Genomic_DNA.
DR RefSeq; WP_007166290.1; NZ_CH672390.1.
DR AlphaFoldDB; A3WG84; -.
DR STRING; 237727.NAP1_15833; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_6_2_5; -.
DR OrthoDB; 9813266at2; -.
DR Proteomes; UP000002995; 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 GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR CDD; cd00371; HMA; 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; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 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 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; 2.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF5; CATION-TRANSPORTING P-TYPE ATPASE-RELATED; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00943; CUATPASE.
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 Cell membrane {ECO:0000256|RuleBase:RU362081};
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 Reference proteome {ECO:0000313|Proteomes:UP000002995};
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 101..123
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 130..147
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 167..185
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 191..209
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 347..368
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 374..400
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 660..679
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 685..704
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 16..81
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 707 AA; 74276 MW; 274EBF7D7CBEBB78 CRC64;
MNAPQLSIDR GETPTKGTRF TVPGMRCAGC IAKIERELPK TDGIVAARVN FSSKRVAIEH
DPAIGEDALT DALLKLGFEA RPIDENPLGT EAAERKQLTR ALGVAGFGMM NVMLLSVSIW
SGAEGFTREL FHWLSALIAM PVIAYSGRPF FSSAWMALKY RRTNMDVPIS IGVILATALS
LYETITGGEH AYFESAVMLL FFLLAGRALD AEMRTRTRAG IGALLGRMGK SASVIAPDGS
TRRVPANALE PGMLVLVAAG EALAADGEIE EGRTTIDNSM LTGESAPESV GEGAVVHAGA
INLGSPFRMR LTRTADDTAI AEIARLMDEA GQSRSTYVRI ADRASRAYAP IVHTLAALAF
VGWMIAGAGW HQSLVIAIAV LIITCPCAMG LAVPTAQVVA SGALLKRGLL VKDGSALERL
AEVDVALFDK TGTLTLGEPR PDIGALNATE RKVALGLAQS SRHPLSQGLA KRLLDEGVEP
AAIVSVEEIS GQGVSGECAG VRVALERPEI ETDRLAVTLK IGTEQTTLTF EDPLRPDASR
TLAMLRGENI EASILSGDRN APVEEIANQL GIPARAEASP HDKLATLEAL RDSGRYPLMV
GDGLNDGPAL AAAHASIAPG TASDASQQAA DAVFIGEKLM PVALAVRVAK RTMVIVRQNF
GFAIGYNALA VPLALFGFVT PLIAAIAMSL SSLVVVANSL RLAGSAK
//
