ID K6ZVL1_9ALTE Unreviewed; 780 AA.
AC K6ZVL1;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=Cu2+-exporting ATPase {ECO:0000313|EMBL:GAC32823.1};
DE EC=3.6.3.4 {ECO:0000313|EMBL:GAC32823.1};
GN Name=copA {ECO:0000313|EMBL:GAC32823.1};
GN ORFNames=GPLA_1916 {ECO:0000313|EMBL:GAC32823.1};
OS Paraglaciecola polaris LMG 21857.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Paraglaciecola.
OX NCBI_TaxID=1129793 {ECO:0000313|EMBL:GAC32823.1, ECO:0000313|Proteomes:UP000006322};
RN [1] {ECO:0000313|EMBL:GAC32823.1, ECO:0000313|Proteomes:UP000006322}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21857 {ECO:0000313|EMBL:GAC32823.1,
RC ECO:0000313|Proteomes:UP000006322};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
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:GAC32823.1}.
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DR EMBL; BAER01000044; GAC32823.1; -; Genomic_DNA.
DR AlphaFoldDB; K6ZVL1; -.
DR STRING; 1129793.GPLA_1916; -.
DR Proteomes; UP000006322; 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 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 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:GAC32823.1};
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 Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362081}.
FT TRANSMEM 167..186
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 198..220
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 232..254
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 260..278
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 412..433
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 439..470
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 736..755
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 79..145
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 780 AA; 85635 MW; A7FEBBED11AE12B8 CRC64;
MNGDKYCTII LDHNRIMCCP GCQAVAQAIV ENGLDDYYRF RTEPSVKADD NLQETLDQLA
IFDEQSIQQD FVIHQGDVSE IQLSLSGISC AACGWLIEKQ LSKVKGIKQV SVNVTANRAL
VSWYSDVVTL SQIMASIERI GYHPSPFQQE QHEALFQQSH KTQLKRIGLA GLMTMQVMML
AVGVYFDLFG DLERETSSFF SWVSLILSTP VVFYSGAGFY HSAYKALKGR TVNMDVPVSI
ALLATYFSGV WATVFEQGQV YFESVCMFIF LLLVSRFIEH QARHKAAQIS ANMLQYIPLT
ANLLIEEQLQ PTLAKSLQLD DVILVKAGET VPIDGVVLSG SAQIDESLLT GEFYPVDKNP
DDSVYGGTIN KSGTLTIRVT SAFKYALVNQ IARLQEQAMA NKPKIATMAD QFSQYFVMAV
LFFSLGSFIF WWWQGNPEAF WIAISVLIAT CPCALGLATP SALSFAMANL NKQGVLLKRS
DVLEQLTQID HVVLDKTGTL TQGKISIAAM NNISDLSDET LLRYAHSVEQ FSEHPIARAF
NNSLAFPDVT EFSFTLGEGV SGKVNQKWVE LLGTHTLSST TNAVPRALTG SSIVMRIGGQ
FVCGFTLSDT LRPDASDMLR RLSRKDISLL SGDNKTNVQQ IADSLGISNW LAEQSPRDKL
AFVQNLQSEQ HSVLMIGDGI NDAPVLAQAD VAVTLGAGAD LAKSSADIIL LKNALGKLPN
LFTIAHRCKQ KIRQNMAWAL GYNILVLPLA VSGVLTPWMA VIGMSLSSII VVINSVRLLK
//
