ID F4GWK3_PUSST Unreviewed; 713 AA.
AC F4GWK3;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 27-MAR-2024, entry version 73.
DE SubName: Full=Heavy metal translocating P-type ATPase {ECO:0000313|EMBL:AEC18876.1};
GN OrderedLocusNames=PT7_0336 {ECO:0000313|EMBL:AEC18876.1};
OS Pusillimonas sp. (strain T7-7).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Pusillimonas.
OX NCBI_TaxID=1007105 {ECO:0000313|EMBL:AEC18876.1, ECO:0000313|Proteomes:UP000008737};
RN [1] {ECO:0000313|EMBL:AEC18876.1, ECO:0000313|Proteomes:UP000008737}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=T7-7 {ECO:0000313|EMBL:AEC18876.1,
RC ECO:0000313|Proteomes:UP000008737};
RX PubMed=21622753; DOI=10.1128/JB.05242-11;
RA Cao B., Ma T., Ren Y., Ren Y., Li G., Li P., Guo X., Ding P., Feng L.;
RT "Complete genome sequence of Pusillimonas sp. T7-7, a cold-tolerant diesel
RT oil-degrading bacterium isolated from the Bohai Sea in China.";
RL J. Bacteriol. 193:4021-4022(2011).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=T7-7;
RA Cao B., Ma T., Li P., Jiang L., Li Y., Guo X., Feng L.;
RT "Genome Announcement Complete Genome Sequence of Pusillimonas sp. T7-7, a
RT novel species isolated from the Bohai Sea, China.";
RL Submitted (APR-2011) 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; CP002663; AEC18876.1; -; Genomic_DNA.
DR RefSeq; WP_013741425.1; NC_015458.1.
DR AlphaFoldDB; F4GWK3; -.
DR STRING; 1007105.PT7_0336; -.
DR KEGG; put:PT7_0336; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_6_4_4; -.
DR OrthoDB; 8552908at2; -.
DR Proteomes; UP000008737; 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; cd00371; HMA; 1.
DR CDD; cd07546; P-type_ATPase_Pb_Zn_Cd2-like; 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; 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; TIGR01512; ATPase-IB2_Cd; 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; PF00403; HMA; 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; PS01229; COF_2; 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 99..116
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 122..140
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 322..342
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 354..379
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 662..687
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 1..66
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 713 AA; 74314 MW; 6BE6D8DBE9EECA57 CRC64;
MQFHIEGMDC ASCVGKIEAA LVRMPGISDV RLNFATEKLE LTLASGSATQ PGDIETIIKS
LGFGVSVAAD QSATAGSVSE IPAASASLRW WQTRRGRQVV GLGILMGTAY AMALFFPDYG
QWVFAAAVLA GVFPFVRQAL TLARAGSPFS IEMLMSVAAL GALFIGEAEE AAAVVFLFSV
GELLESVAAG RARAGIRALA SLVPQSAVLL DPQGGQRNVP VAMLHVNDRV LVRPGDRLPA
DGVIIEGASS LDESPITGES IPCAKALGDS VFAGSINIEG VLQVRVGKTT ADNTISRIIH
LVEQAQASKS PTARFIEQFS RYYTPAVMAI AALTVLVPPL AMGADWDTWI YRGLALLLIA
CPCALVLSTP AAIASGLAAG TRRGLLVKGG NALEIIGRVN AIAFDKTGTL TEGKPRVTDV
VAFGQQNHDE ILSLAASVES GSSHPLAQAI VNHARAANIL IPAAAQASAT AGKAVHATVA
GRMLAVGSPV YAVGVATLSS EQFAQIETLQ NQGKTVSVLL DEQNRAALGL LALRDEPRQD
AQQALSRLKA MGVRTIMLTG DNSRTAQAIA HRLGMAYKAE LLPQDKLRLL DEMKYKDKVA
MVGDGINDAP ALATADVGIA MGGGTDVALE TADAALLKNR VTDVAHLVAL SRATMANIHQ
NVVFALGLKG VFLLTTVFGF TGLWVAVLAD TGATALVTLN ALRLLRFKGT PGI
//
