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
//