ID A0A1Z1WB57_9ACTN Unreviewed; 754 AA.
AC A0A1Z1WB57;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Carbonate dehydratase {ECO:0000313|EMBL:ARX83612.1};
GN Name=copA {ECO:0000313|EMBL:ARX83612.1};
GN ORFNames=SMD44_03035 {ECO:0000313|EMBL:ARX83612.1};
OS Streptomyces alboflavus.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=67267 {ECO:0000313|EMBL:ARX83612.1, ECO:0000313|Proteomes:UP000195880};
RN [1] {ECO:0000313|EMBL:ARX83612.1, ECO:0000313|Proteomes:UP000195880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MDJK44 {ECO:0000313|EMBL:ARX83612.1,
RC ECO:0000313|Proteomes:UP000195880};
RA Wang Y., Du B., Ding Y., Liu H., Hou Q., Liu K., Wang C., Yao L.;
RT "Streptomyces alboflavus Genome sequencing and assembly.";
RL Submitted (MAY-2017) 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}.
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DR EMBL; CP021748; ARX83612.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z1WB57; -.
DR STRING; 67267.GCA_000716675_02416; -.
DR KEGG; salf:SMD44_03035; -.
DR eggNOG; COG2217; Bacteria.
DR OrthoDB; 7059309at2; -.
DR Proteomes; UP000195880; Chromosome.
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; IPR000579; Cation-trans_P-type_ATPase_A/B.
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; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
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; PR00940; CATPATPASEA.
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:UP000195880};
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 102..122
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 128..151
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 163..185
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 205..224
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 359..379
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 385..408
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 708..724
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 730..748
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 4..68
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 68..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 754 AA; 77268 MW; 79F3967CCE7D9BA4 CRC64;
MNTSEVELAI GGMTCASCSA RIEKKLNRIE GVTASVNLAT EKAKVAYADG VEVGQLVATV
ERLGYSAHEI VPPPPDAGPG DDSADRPVTT DLTEADRLLQ RLLVSAALAL PVVVLAMVPS
LQFEYWQWLS LTLAAPVVVW GGLPFHTAAL TNARHGAATM DTLVSLGTLA AFGWSVWALF
LGTAGEPGMR HGFEFTIARG DSSSALYLEV AAGVVTFILL GRYLEARSKR KAGAALRALL
DLGAKDVSVL GPDGTETRIP VGRLAVGDRF VVRPGETVAT DGTVVEGASA VDVSMLTGES
VPADVTVGDA VTGATVNAGG RLVVEATRVG ADTQLARMAR LVEDAQSGKA EVQRLADRVA
AVFVPVVIAL AVATLGFWLG NGVGAAAAFT AAVAVLIIAC PCALGLATPT ALLVGTGRGA
QLGILIKGPE VLESTRRVDT IVLDKTGTVT TGRMALQDVY AAESTDEKEL LRLAGALEHA
SEHPVARAVA AGAAQRLGLD AGALPVPTRF ENVPGAGVRG TVDGREVLAG RERLLAEAGV
TGLAGLAAAR ERAEADGRTA VLVALDGVAA GLLAVADTVK DTSPEAVRRL RELGLDPVLL
TGDNRSVAEA VAAAVGITPD AVHAEVLPED KADVVRRLQE EGRVVAMVGD GVNDAAALAT
ADLGLAMGTG TDAAIEAGDL TLVRGDLRVA ADAIRLARRT LATIKGNLCW AFGYNVAALP
LAAAGLLNPM IAGAAMAFSS VFVVTNSLRL RSFT
//