ID A0A0M8VSJ9_9ACTN Unreviewed; 780 AA.
AC A0A0M8VSJ9;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Carbonate dehydratase {ECO:0000313|EMBL:KOV71440.1};
GN ORFNames=ADL00_07700 {ECO:0000313|EMBL:KOV71440.1};
OS Streptomyces sp. AS58.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519489 {ECO:0000313|EMBL:KOV71440.1, ECO:0000313|Proteomes:UP000037758};
RN [1] {ECO:0000313|EMBL:KOV71440.1, ECO:0000313|Proteomes:UP000037758}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS58 {ECO:0000313|EMBL:KOV71440.1,
RC ECO:0000313|Proteomes:UP000037758};
RA Noorani M.;
RL Submitted (JUL-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:KOV71440.1}.
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DR EMBL; LGDU01000047; KOV71440.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0M8VSJ9; -.
DR PATRIC; fig|1519489.3.peg.1804; -.
DR OrthoDB; 7059309at2; -.
DR Proteomes; UP000037758; 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 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; PR00120; HATPASE.
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:UP000037758};
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 105..123
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 129..146
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 166..187
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 207..227
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 362..383
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 389..411
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 702..721
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 727..746
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 10..74
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 73..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 748..780
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 79..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 780 AA; 80110 MW; 774DACFF1BB65681 CRC64;
MATEPAPPLL TTDLTVGGMT CAACVRRVEK KLAKLEGVTA AVNLATGSAR VSHPPEVSPA
QLVATVEQAG YTAALPEPPK ARRPEETDPE ADPDAEGVRR ERDRVLITAL LAVPVLALSM
VPAWQFRNWQ WLCFALAAPV AVWSAWPFHL RALRGLRHST ATMDTLVSLG VVASFSWSVY
ALFLGGAGEP GMRMPFSLLP SASDGVAHVY LEAAVAVPLF VLAGRFLEAR ARHGTGAALR
SLAGLAAKEV AVRGDDGSER LVAIEELTVG QVFVVRPGER VATDGQVVKG SSAVDLSLVT
GESEPVEVGS GSPVVGGAVN AGGLLLVRAT AVGADTQLAR ITRLVTEAQA GKAKAQRLAD
SVAGVFVPVV LALAVTVLGY WLGAGADPQA AVTACVAVLV VACPCALGLA TPTALMAATG
RGAQLGVLVR GPQSLEGLEH IDTVVLDKTG TLTTGHMTVA RVTAVPDGPG RDEVLRLAAA
VEQGSEHPLG RAIVGYAKRE SPGSPLPEPA DFTATAGRGV RGRVEGRVVE VVAPDDELPA
ALADALAAAE SAARTPVLVR VDGETLALIE VGDVLRSGSY RTVDRLRRLG VEPVLATGDR
EAPARAVADA LGIEEVHTRC TPEDKAGLVK ELRESGRRVA VVGDGVNDAA ALAGADLGIA
MGSGTDAAIG AADVTLVRGD IEALADAVLL ARRTLSTIHA NLMWAFGYNA VTVPLAMVGL
LNPMLAAAAM SASSVLVVGN SLRLRAWQPS PARGRRPAAT GPTPGNRPSP VPSPAGSSDR
//
