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Database: UniProt
Entry: A0A0X3XP06_9ACTN
LinkDB: A0A0X3XP06_9ACTN
Original site: A0A0X3XP06_9ACTN 
ID   A0A0X3XP06_9ACTN        Unreviewed;       761 AA.
AC   A0A0X3XP06;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 39.
DE   SubName: Full=Carbonate dehydratase {ECO:0000313|EMBL:KUL73484.1};
GN   ORFNames=ADL34_20220 {ECO:0000313|EMBL:KUL73484.1};
OS   Streptomyces sp. NRRL WC-3605.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=1609103 {ECO:0000313|EMBL:KUL73484.1, ECO:0000313|Proteomes:UP000052945};
RN   [1] {ECO:0000313|EMBL:KUL73484.1, ECO:0000313|Proteomes:UP000052945}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL WC-3605 {ECO:0000313|EMBL:KUL73484.1,
RC   ECO:0000313|Proteomes:UP000052945};
RA   Gilbert D.G.;
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:KUL73484.1}.
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DR   EMBL; LLZN01000062; KUL73484.1; -; Genomic_DNA.
DR   RefSeq; WP_062670153.1; NZ_LLZN01000062.1.
DR   AlphaFoldDB; A0A0X3XP06; -.
DR   OrthoDB; 7059309at2; -.
DR   Proteomes; UP000052945; 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; SFLDG00002; C1.7:_P-type_atpase_like; 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:UP000052945};
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        119..139
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        145..167
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        179..199
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        219..238
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        375..397
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        403..424
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        714..731
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        737..755
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          24..88
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          85..114
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   761 AA;  78828 MW;  678BB26B1179BDD8 CRC64;
     MPRTTTGEPA ITEAPATSEA PPASEVELLI GGMTCASCAA RVEKKLNRMD GVTASVNYAT
     EKAKVSHPAE VSVADLIAVV ERTGYTAHEP EPPRPAPEEP AAAPEGTEDS GPDSYRQRLT
     VSALLSLPVV LLSMVPALQF DNWQWLALTL ASPVVVWGGL PFHRAAFTNA RHGAATMDTL
     VSVGTLAAYG WSLWALFLGD AGMSGMRDGF TFTVSRGDGA SQIYLEVASG VITFILLGRH
     LEARAKRRAG DALRALMELG AKDVGVLRDG REVRVPVDRL AVGDRFVVRP GEKIATDGTV
     VEGAAAVDAA LLTGESAPVD VGVGDAVTGA TVNAGGRLVV EATRVGADTR LARMARLVEE
     AQSGKAEAQR LADRVSAVFV PVVIALAVAT FGVWFGATDD TAAAFTAAVA VLIIACPCAL
     GLATPTALMV GTGRGAQLGI LIKGPEVLES TRRVDTVLLD KTGTVTTGRM TLQGVYAADG
     VDEETLLRLA GAVEHASEHP VARAVAAGAE ERAGLLPSVE DFTNVPGKGV RGRVEGHEVA
     VGRLAENTTA LPPELASAAE EAEREGRTAV VVGWDGVARG VLAVADTVKE SSAEAVRALR
     ALGLTPVLLT GDNRRVAESV AHTVGIDQVI AEVLPEDKVE AVRRLQREGR SVAVVGDGVN
     DAAALATADL GLSMGTGTDA AIEASDLTLV RGDLRVAADA IRLSRRTLAV IKGNLVWAFG
     YNVAALPLAA AGLLNPMIAG AAMAFSSVFV VTNSLRLRTF R
//
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