ID K9DTI4_9BURK Unreviewed; 818 AA.
AC K9DTI4;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, sequence version 1.
DT 24-JAN-2024, entry version 60.
DE SubName: Full=Heavy metal translocating P-type ATPase {ECO:0000313|EMBL:EKU82007.1};
GN ORFNames=HMPREF9710_02700 {ECO:0000313|EMBL:EKU82007.1};
OS Massilia timonae CCUG 45783.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Telluria group; Massilia.
OX NCBI_TaxID=883126 {ECO:0000313|EMBL:EKU82007.1, ECO:0000313|Proteomes:UP000009874};
RN [1] {ECO:0000313|EMBL:EKU82007.1, ECO:0000313|Proteomes:UP000009874}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CCUG 45783 {ECO:0000313|EMBL:EKU82007.1,
RC ECO:0000313|Proteomes:UP000009874};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Massilia timonae CCUG 45783.";
RL Submitted (SEP-2012) 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}.
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:EKU82007.1}.
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DR EMBL; AGZI01000033; EKU82007.1; -; Genomic_DNA.
DR RefSeq; WP_005667204.1; NZ_JH992923.1.
DR AlphaFoldDB; K9DTI4; -.
DR STRING; 47229.LO55_3391; -.
DR PATRIC; fig|883126.3.peg.2725; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_0_3_4; -.
DR OrthoDB; 8552908at2; -.
DR Proteomes; UP000009874; 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 CDD; cd02079; P-type_ATPase_HM; 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; IPR021993; ATPase-cat-bd.
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 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; PF12156; ATPase-cat_bd; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
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 Reference proteome {ECO:0000313|Proteomes:UP000009874};
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 190..210
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 222..239
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 259..277
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 283..301
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 439..458
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 470..493
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 773..789
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 795..813
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 102..168
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 818 AA; 86124 MW; 9346D2F226563382 CRC64;
MSAVLEEAVR AAGGAATAAA RNAPAGCFHC GLPVPRDSAW QATIGGEVRR MCCPGCAAAA
QAIVDGGFAD YYATRTAYAA QADIEAANAP ELDLVDDGDA DGAASFTVEG IRCAACVWLI
ERRLHDLPGV LDVGLNVATE RLFVRWDPSG CRASAILRTL RAIGYVAYPY DARRHGEQLE
RARKQLFRQL FVAGLSMMQV MMYAVPVYMA DEGTMDAAMT ALMHWAALFL TLPAVLYSAQ
PFFKGAWRDL RRGMPGMDVP VALGIGAAFA GSLQALVTGN GDVYFDSVTM FVFLLLGSRY
LELGARRKAA GALERLQQGL PPSALRLRGD PQLRDTELVT AGSLRVDDLV LVRAGQAAPA
DGMIVEGDTD VDLALLTGES RTQRRGVGDL VPGGALNAGG AIVLRVTSTA HDSTLSMLVR
LVERAGQGKP ALALWADRVA AWFVLGLLAL TVLAYFAWLQ VDPGKAWQVA IAVLVVSCPC
ALSLATPTAL AAATDRLLRR GVLSVQPHTL ETFDRATHVV FDKTGTLTHG RPVLRQTLPV
GSLTGFDCLR IAAALEADNP HPLALGIREA VIASPAEAAR AERTQFTIGQ GVEGWVDGRY
YRLGNVAWVA GVAGGVARVA APVGATSVWL GSSEGWLARF DLADGLRADA AEVVRRIRAS
GKTVILLSGD EQHAAQAVAA RLGISTAIGG KLPQEKLAYV RRLQQDGAIV AMVGDGINDA
AVLRGADVSF AMGRGAELAQ LHADGVLMGD SLAPLADTLD TARRTLAVIR QNLAWATVYN
VAAIPAAATG LLNPWLAGIG MAASSAVVVL NALRLRRD
//
