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Database: UniProt
Entry: A0A0A6YCR0_9MICC
LinkDB: A0A0A6YCR0_9MICC
Original site: A0A0A6YCR0_9MICC 
ID   A0A0A6YCR0_9MICC        Unreviewed;       765 AA.
AC   A0A0A6YCR0;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 45.
DE   SubName: Full=Carbonate dehydratase {ECO:0000313|EMBL:KHD97872.1};
GN   ORFNames=GY22_07105 {ECO:0000313|EMBL:KHD97872.1};
OS   Kocuria polaris.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC   Kocuria.
OX   NCBI_TaxID=136273 {ECO:0000313|EMBL:KHD97872.1, ECO:0000313|Proteomes:UP000030466};
RN   [1] {ECO:0000313|EMBL:KHD97872.1, ECO:0000313|Proteomes:UP000030466}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CMS 76or {ECO:0000313|EMBL:KHD97872.1,
RC   ECO:0000313|Proteomes:UP000030466};
RX   PubMed=12656171; DOI=10.1099/ijs.0.02336-0;
RA   Reddy G.S., Prakash J.S., Prabahar V., Matsumoto G.I., Stackebrandt E.,
RA   Shivaji S.;
RT   "Kocuria polaris sp. nov., an orange-pigmented psychrophilic bacterium
RT   isolated from an Antarctic cyanobacterial mat sample.";
RL   Int. J. Syst. Evol. Microbiol. 53:183-187(2003).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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:KHD97872.1}.
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DR   EMBL; JSUH01000005; KHD97872.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0A6YCR0; -.
DR   OrthoDB; 7059309at2; -.
DR   Proteomes; UP000030466; 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   CDD; cd00371; HMA; 1.
DR   CDD; cd02094; P-type_ATPase_Cu-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; 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; TIGR01525; ATPase-IB_hvy; 1.
DR   NCBIfam; TIGR01494; ATPase_P-type; 1.
DR   PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR   PANTHER; PTHR43520:SF8; COPPER-TRANSPORTING ATPASE 2; 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; PS01229; COF_2; 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   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   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        121..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        145..164
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        176..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        219..239
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        373..395
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        401..422
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        717..734
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        740..758
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          17..81
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   765 AA;  79036 MW;  892DBEA21DA7B840 CRC64;
     MPETRTPVPT EVAGPLRTLE LEITGMTCSS CVSRVEKKLG RLDGVDASVN LALETATVHV
     PAGVSDQQVV ETVEKAGYGA VLKNAPGGDD AGGPDGSDAM ARVAGREASS LRSPESLRRR
     LLVAAALSLP VFVISMLPGF QFPHWGWVVA ALSLPVVTWA AWPFHRSAAV NARHLTSTMG
     TLVSLGVSAA YLFSLWNLLR EPGMTAGAML GHAMDMSGHQ LYFETGALVT AFLLLGRYLE
     ARAKARSGEA LRALLELGAK DAVVLRDGVE TSVPAEQLRP GDLVVVRPGE KIAADGVVVD
     GRSAVDTSLL TGESLPVEVE VGDTVTGATI NTNGRLLVEA TRVGADTTLA QMGRMVSRAQ
     ASKAPVARLA DRISGVFVPV VLVIALATLA GWLLLTGDVN ASFVAAVSVL VIACPCALGL
     ATPTALLTGT GRGAQLGILI KGAEVLEDTR TVDTVVLDKT GTVTSGQLSV AAVTPVSGYS
     RDQVLDLAAT VEQHSEHPIA RAVAAATPHR FPVSGFVSAP GGGVRAHVAD GMHSRSVVVG
     RTTWLSENGV RLDGAQLDAL RRAQEGGFTT ILVAVDGALV GFVDLRDTVK DDAREAVARL
     KELGLRPMLL TGDNEPVARA VAAEAGIAAE DVVADVSPEG KVAVVRDLQD DGRVVAMVGD
     GVNDAAALAQ ADLGIAMGAG TDAAIEAADI TVVRSDVGSV PTAIALSRRT LSIIKSNLFW
     AFAYNTVAIP VAAAGLLNPV IAGAAMAFSS VFVVLNSLRL RSFGR
//
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