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Database: UniProt
Entry: A0A101NI07_9ACTN
LinkDB: A0A101NI07_9ACTN
Original site: A0A101NI07_9ACTN 
ID   A0A101NI07_9ACTN        Unreviewed;       749 AA.
AC   A0A101NI07;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Carbonate dehydratase {ECO:0000313|EMBL:KUM93673.1};
GN   ORFNames=AQI88_24990 {ECO:0000313|EMBL:KUM93673.1};
OS   Streptomyces cellostaticus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=67285 {ECO:0000313|EMBL:KUM93673.1, ECO:0000313|Proteomes:UP000054241};
RN   [1] {ECO:0000313|EMBL:KUM93673.1, ECO:0000313|Proteomes:UP000054241}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40189 {ECO:0000313|EMBL:KUM93673.1,
RC   ECO:0000313|Proteomes:UP000054241};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces cellostaticus DSM 40189, type strain
RT   for the species Streptomyces cellostaticus.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
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:KUM93673.1}.
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DR   EMBL; LMWL01000044; KUM93673.1; -; Genomic_DNA.
DR   RefSeq; WP_067003294.1; NZ_KQ948028.1.
DR   AlphaFoldDB; A0A101NI07; -.
DR   STRING; 67285.AQI88_24990; -.
DR   OrthoDB; 7059309at2; -.
DR   Proteomes; UP000054241; 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; 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: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   Reference proteome {ECO:0000313|Proteomes:UP000054241};
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        110..128
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        134..150
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        171..190
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        210..229
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        366..387
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        393..415
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        702..719
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        725..743
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          18..82
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   REGION          79..101
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   749 AA;  77940 MW;  CFF875D7499420CB CRC64;
     MTSTTAETGT TSAIGGTSEV ELLIGGMTCA SCAARVEKKL NRMDGVSATV NFATEKAKVS
     YTGGVQVADL IATVVKTGYT AEEPPPPEPE PETPQTSGQD PELAALRHRL LVSALLAAPV
     VLLAMVPSLQ FDNWQWLSLT LAAPVVVWGG RPFHQAAWTN LRHGAATMDT LVSVGTLAAF
     GWSLWALFFG DAGMPGMHDE FRFTVSRMDG ASTIYLEVAA GVVALILLGR YLEARSKRRA
     GAALRALMEL GAKDVAVLRA GREERVPVAS LTVGDRFVVR PGEKIATDGT VVEGVSAVDA
     SMLTGESVPV DVGPGDQVTG ATVNAGGRLV VEATRVGADT QLARMARLVE DAQNGKAEVQ
     RLADRISAVF VPVVMLIAVA TFGAWLGVTG DSVAAFTAAV AVLIIACPCA LGLATPTALM
     VGTGRGAQLG ILIKGPEVLE STRRVDTVVL DKTGTVTSGR MTLQEVYAAD GEDAKEVLRL
     AGALEHASEH PVARAIAAGA EERTGALPGA EHFENVPGRG VRGRVEGREV AVGRLFDALP
     EELAQARRQA EQEGRTAVTV GWDGRARGVL AVADAVKETS AEAVRELRAL GLTPVLLTGD
     NRTVAEAVAQ AVGIDEVIAE VLPEDKVDVV RRLQGEGRTV AMVGDGVNDA AALATADLGL
     AMGTGTDAAI EAGDLTLVRG DLRVAADAIR LSRRTLATIK GNLVWAFGYN VAALPLAAAG
     LLNPMIAGAA MAFSSVFVVT NSLRLRRFR
//
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