ID A0A4R4F712_9GAMM Unreviewed; 793 AA.
AC A0A4R4F712;
DT 31-JUL-2019, integrated into UniProtKB/TrEMBL.
DT 31-JUL-2019, sequence version 1.
DT 13-SEP-2023, entry version 17.
DE SubName: Full=Cadmium-translocating P-type ATPase {ECO:0000313|EMBL:TCZ92969.1};
DE EC=3.6.3.3 {ECO:0000313|EMBL:TCZ92969.1};
GN Name=cadA {ECO:0000313|EMBL:TCZ92969.1};
GN ORFNames=EYQ95_02985 {ECO:0000313|EMBL:TCZ92969.1};
OS Lysobacter sp. N42.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Xanthomonadaceae; Lysobacter.
OX NCBI_TaxID=2545719 {ECO:0000313|EMBL:TCZ92969.1, ECO:0000313|Proteomes:UP000294500};
RN [1] {ECO:0000313|EMBL:TCZ92969.1, ECO:0000313|Proteomes:UP000294500}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N42 {ECO:0000313|EMBL:TCZ92969.1,
RC ECO:0000313|Proteomes:UP000294500};
RA Wang T.-J., Du Z.-J.;
RT "Lysobacter caldus sp. nov., isolated from hot spring,.";
RL Submitted (MAR-2019) 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:TCZ92969.1}.
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DR EMBL; SKFB01000001; TCZ92969.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A4R4F712; -.
DR OrthoDB; 9814270at2; -.
DR Proteomes; UP000294500; 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; 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 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; 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 PRINTS; PR00943; CUATPASE.
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; 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 Hydrolase {ECO:0000313|EMBL:TCZ92969.1};
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:UP000294500};
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 181..200
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 212..231
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 243..265
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 271..289
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 427..445
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 451..474
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 743..764
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 770..791
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 93..159
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 793 AA; 88225 MW; 451B83F220729FE7 CRC64;
MTRACFHCHQ PVPEGLNLHV DIMGQSQPMC CYGCQAVAQT IVEQDLESFY KFRQTENNNI
LPLVPDELQK DDLSIYDEPE VQAEFSFSSA NGQEAWLAIE GMTCAACAWL IEKHLQQQPG
IQKVFVNSST DRLRVTWNKE KLLLSTILNE IENIGYRARP FKEGELEEQF QKRRKGLIRR
LGVAGIASMQ TMMVAFGLYY DDIDSTTRLY FWWVSLLFSA PVFVYSCQPF YANAIKALRT
RTLNMDVPVS IAIIFAFFAS MYATITNQGE VYFECVTMFA FFLLTGRYLE LLAKHKAITD
AANLMKLTPS FAEVWHEEQW QTKPVHQLSA GDKVRVKPGS VIPIDGEIET QKVYVNEAQL
TGESHPIPKA KGENVYAGSL NLDTPLQLIV TKPYQDSLLA KIIQLQDDAL ALKPKAIDVA
DRIGRNLVLG TLIIALITYI TWLWVDADRA FWILLSVLVA TCPCALALAS PTAVSSAVSR
LNRLGVLLKN ADASTNVNAI KTICFDKTGT LTEGHFKITD SWFAESEHQN KWLTLACELE
SWSEHPISKA FTARDSETYL QNVENIPGKG LYAEYQAKQI LIGSHAFLAQ HKIPMACTLP
SANVYMAYNG ELVAAWRVDD QLRNDAKSTI SALSQQGYHC VMLTGDNDGR AQEIADKVGI
KEVHAGLTPQ DKLSKLQEMQ RSTPVLMVGD GINDGPVLAG ANVSVTFSAG SELAQASSDV
VILNQKLSSL VYFIQYSKRL ARVIFQNFIW AFGYNGIILP LAAFGFVDPL IAMLGMSASS
LIVITNSLRL IRK
//
