ID B0KN94_PSEPG Unreviewed; 750 AA.
AC B0KN94;
DT 18-MAR-2008, integrated into UniProtKB/TrEMBL.
DT 18-MAR-2008, sequence version 1.
DT 27-MAR-2024, entry version 100.
DE SubName: Full=Heavy metal translocating P-type ATPase {ECO:0000313|EMBL:ABZ01075.1};
GN OrderedLocusNames=PputGB1_5192 {ECO:0000313|EMBL:ABZ01075.1};
OS Pseudomonas putida (strain GB-1).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=76869 {ECO:0000313|EMBL:ABZ01075.1, ECO:0000313|Proteomes:UP000002157};
RN [1] {ECO:0000313|EMBL:ABZ01075.1, ECO:0000313|Proteomes:UP000002157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GB-1 {ECO:0000313|EMBL:ABZ01075.1,
RC ECO:0000313|Proteomes:UP000002157};
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., Bruce D., Goodwin L., Chertkov O., Brettin T.,
RA Detter J.C., Han C., Kuske C.R., Schmutz J., Larimer F., Land M.,
RA Hauser L., Kyrpides N., Kim E., McCarthy J.K., Richardson P.;
RT "Complete sequence of Pseudomonas putida GB-1.";
RL Submitted (JAN-2008) 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; CP000926; ABZ01075.1; -; Genomic_DNA.
DR RefSeq; WP_012274688.1; NC_010322.1.
DR AlphaFoldDB; B0KN94; -.
DR KEGG; ppg:PputGB1_5192; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_6_4_6; -.
DR Proteomes; UP000002157; 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; cd07545; P-type_ATPase_Cd-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; 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; PTHR48085; CADMIUM/ZINC-TRANSPORTING ATPASE HMA2-RELATED; 1.
DR PANTHER; PTHR48085:SF5; CADMIUM_ZINC-TRANSPORTING ATPASE HMA2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00941; CDATPASE.
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 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 136..155
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 161..179
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 364..389
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 395..422
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 700..721
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 727..748
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 52..116
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 1..30
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..28
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 750 AA; 79286 MW; A95AE7E465981761 CRC64;
MNQPVSHDHK HSHDHAHGDD DHGHAAHGHS CCGSKAAPSL VQLSETASAQ AQLSRFRIDA
MDCPTEQTLI QDKLGKLAGI EQLEFNLINR VLGVRHTLNG TAEIERAIDS LGMKAEPIAA
EDDGTTSVAQ PAKTRWWPLA LSGIAAITAE IVHFAALAPE WVVAGLALLA ILGCGLGTYK
KGWIALKNRN LNINALMSIA VTGAVLIGQW PEAAMVMVLF TVAELIEARS LDRARNAIGG
LMQLAPDMAT VQQADGLWRE LDVREVAIGA LVRVRPGERI GLDGEVTSGQ SSVDQAPITG
ESLPVEKAVG DKLFAGTINQ AGALEFRVTA AAGQSTLARI IKAVEEAQGA RAPTQRFVDR
FSRIYTPVVF AIALAVAVIP PLFMAGAWFD WVYRALVLLV VACPCALVIS TPVTIVSGLA
AAARKGILIK GGVYLEGGRH LDFLALDKTG TITHGKPVQT DAEVLAPQFE ARAQALAASL
GERSDHPVSR AIAQFGKAQG LALSEVDDFA ALGGRGVRGT IDGEVYHLGN HRLVEELGLC
SPALEAKLDA LERQGKTVVL LLDRSGPLAL FAVADTVKDS SRQAIAELHE LGIKTVMLTG
DNPHTAQAIA AVVGIDRAEG NLLPADKLKT IEALYAEGHR VGMVGDGIND APALARAEIG
FAMAAAGTDT AIETADVALM DDDLRKIPAF VRLSRQSAAI LMQNIVLALG IKAIFLAITF
AGMATMWMAV FADMGVSLLV VFNGLRLLRK
//
