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Database: UniProt
Entry: A0A0A1YKJ6_9PSED
LinkDB: A0A0A1YKJ6_9PSED
Original site: A0A0A1YKJ6_9PSED 
ID   A0A0A1YKJ6_9PSED        Unreviewed;       802 AA.
AC   A0A0A1YKJ6;
DT   04-FEB-2015, integrated into UniProtKB/TrEMBL.
DT   04-FEB-2015, sequence version 1.
DT   24-JAN-2024, entry version 41.
DE   SubName: Full=Carbonate dehydratase {ECO:0000313|EMBL:KFX69204.1};
GN   ORFNames=TMS3_0117225 {ECO:0000313|EMBL:KFX69204.1};
OS   Pseudomonas taeanensis MS-3.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1395571 {ECO:0000313|EMBL:KFX69204.1, ECO:0000313|Proteomes:UP000030063};
RN   [1] {ECO:0000313|EMBL:KFX69204.1, ECO:0000313|Proteomes:UP000030063}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MS-3 {ECO:0000313|EMBL:KFX69204.1,
RC   ECO:0000313|Proteomes:UP000030063};
RX   PubMed=24407626;
RA   Lee S.Y., Kim S.H., Lee D.G., Shin S., Yun S.H., Choi C.W., Chung Y.H.,
RA   Choi J.S., Kahng H.Y., Kim S.I.;
RT   "Draft Genome Sequence of Petroleum Oil-Degrading Marine Bacterium
RT   Pseudomonas taeanensis Strain MS-3, Isolated from a Crude Oil-Contaminated
RT   Seashore.";
RL   Genome Announc. 2:0-0(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:KFX69204.1}.
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DR   EMBL; AWSQ01000004; KFX69204.1; -; Genomic_DNA.
DR   RefSeq; WP_025166438.1; NZ_AWSQ01000004.1.
DR   AlphaFoldDB; A0A0A1YKJ6; -.
DR   STRING; 1395571.TMS3_0117225; -.
DR   eggNOG; COG2217; Bacteria.
DR   eggNOG; COG2608; Bacteria.
DR   OrthoDB; 9814270at2; -.
DR   Proteomes; UP000030063; 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; 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; PR00941; CDATPASE.
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:UP000030063};
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..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        213..234
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        246..268
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        274..292
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        430..449
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        455..481
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        750..770
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        776..794
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          93..159
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   802 AA;  86814 MW;  2234AFCB70E26F8C CRC64;
     MASPIPCYHC GLPVPAGSQF HAQVLGEKRL LCCPGCQAVA EAIVAGGLEH YYKHRSERAG
     NPQELPQALP DELALLDRAD VQAPFVEHQG ELSETNLLIE GISCAACAWL IEKHLRGLPG
     VAEANLNLSN HRLQVRWVDS QLPLSQLFKE LRKIGYAGHP WQADAATEQL TRENRRAMRQ
     LGVAGLLWIQ VMMATMATWP EFNIDLSPEL DKILRWVSLF LTTPIVFYCC GQFFRGAMRD
     LRTRHLSMDL SVSLAIGGAY AAGIWSTVTG DGELYFDAVG MFALFLLAGR YLERRARERT
     AAATAQLVQL LPASCLRLDA DGHTQRVLLS ELRKGEQVLV PPGALLPADG RILSGQSSVD
     ESLLTGEYLP QPRGVDDSVT AGTLNVEGPL TVEVEALGDA TRLSAIVRLL ERAQSDKPRL
     AEIAEQTAQW FLLIVLLVAA IVGLVWWQID SSRAFWVVLA LLVATCPCAL ALATPTALTA
     ATGSLHKLGM LLTRGHVLEG LNQIDTVIFD KTGTLTEGRL TLSAIHPLGE LDSDACLALA
     AALEIRSEHP IARAFGRATQ AAERVDNIPG LGLQGWVADR QLRIGQAAFV SELSGQAPPE
     IPADRGQWLL LGDCQGPLAW FVLDDRLRDD APALLAACRE RGWQVLLLSG DSSPMVAEVA
     RQLGIEQARG GLTPDAKLAE LKKLHEQGRR VLMLGDGVND VPVLAGADIS VAMGGATDLA
     KTSADAVLLS NRLTSLIQAF NLARRTRRII IENLTWASLY NGLVLPFAAL GWITPIWAAL
     GMSLSSLLVV LNALRLTRVP KQ
//
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