ID A0A1Q2CVA0_9ACTN Unreviewed; 905 AA.
AC A0A1Q2CVA0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 28-JAN-2026, entry version 33.
DE SubName: Full=Carbonate dehydratase {ECO:0000313|EMBL:AQP50034.1};
GN ORFNames=BW733_03485 {ECO:0000313|EMBL:AQP50034.1};
OS Tessaracoccus flavescens.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Propionibacteriaceae; Tessaracoccus.
OX NCBI_TaxID=399497 {ECO:0000313|EMBL:AQP50034.1, ECO:0000313|Proteomes:UP000188235};
RN [1] {ECO:0000313|EMBL:AQP50034.1, ECO:0000313|Proteomes:UP000188235}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SST-39T {ECO:0000313|EMBL:AQP50034.1,
RC ECO:0000313|Proteomes:UP000188235};
RX PubMed=18398170; DOI=10.1099/ijs.0.64868-0;
RA Lee D.W., Lee S.D.;
RT "Tessaracoccus flavescens sp. nov., isolated from marine sediment.";
RL Int. J. Syst. Evol. Microbiol. 58:785-789(2008).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + phosphate + H(+); Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00049360};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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DR EMBL; CP019607; AQP50034.1; -; Genomic_DNA.
DR RefSeq; WP_152024542.1; NZ_CP019607.1.
DR AlphaFoldDB; A0A1Q2CVA0; -.
DR STRING; 399497.BW733_03485; -.
DR KEGG; tfa:BW733_03485; -.
DR OrthoDB; 9814270at2; -.
DR Proteomes; UP000188235; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR FunFam; 2.70.150.10:FF:000160; Sarcoplasmic/endoplasmic reticulum calcium ATPase 1; 1.
DR FunFam; 3.40.50.1000:FF:000083; Sodium/potassium-transporting ATPase subunit alpha; 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; 1.20.1110.10; Calcium-transporting ATPase, transmembrane domain; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR InterPro; IPR006068; ATPase_P-typ_cation-transptr_C.
DR InterPro; IPR004014; ATPase_P-typ_cation-transptr_N.
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; IPR059000; ATPase_P-type_domA.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00831; Cation_ATPase_N; 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; SSF81660; Metal cation-transporting ATPase, ATP-binding domain N; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Magnesium {ECO:0000256|ARBA:ARBA00022842};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000188235};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 94..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 258..276
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 288..312
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 703..727
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 733..754
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 775..794
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 806..823
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 843..863
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 875..895
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 17..90
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..41
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Low complexity"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 905 AA; 95465 MW; 299D4DB1FCBA5743 CRC64;
MSTSPEPQTP PSSSAPKPWA ASPEEVLASV DSTTDGLAGS EVERRLARDG RNELPTPKPV
PAWRRLLSQF NDILIYILIA AAALKAYSGD WVDFAVIAVV ILATGLIGFI QEGRAASALA
SLQTMQSLDA QVLRDGTWGV VDAATIVPGD VIRVRSGDRV PADVRLLTSS SLQVDEAALT
GESVPAQKEL EPVAAEAGVG DRSSMLFSST IITAGTAEAV VVSTGGNTEI GRISALVADQ
EKLDTPLSRQ LAKLGTQLAI LIGVMAVVML AIGYFVHDFH GDELISAAIG FAVAAVPEGL
PALVTITLAL GVQQMARRNA ITRKMAAVET LGSVTTICSD KTGTLTQNEM TARTVLTSEG
RYVVEGTGYQ PKGHVTDPHG QPAALPDHPD LEALVIAAGA ANDARVEETD EGWRVVGQPT
EGALDVLATK AGADMAHVTR LATVPFESAH KFSATLDDVA SGERRIHVLG APDRLLDRST
TQLGGGGSTE TLDHGFWDAG IDELSEQGLR VLAAASRPAD GVEDLALDDL DTGLTFLGLV
GIVDPPRPEV TDAISLAHTA GIRVKMITGD HAGTAVAISR ELGIAPAEGD VKALTGAELE
AMSDDELAAQ VRDVDIYART SPEHKLRIVK ALQTHDEVVA MTGDGVNDAP SITRADVGVA
MGIKGTEATK EAADIVLADD NFATIERAVE EGRRIYDNIR KSVVFLLPTN GGQGLVILVA
VLLGMALPLS PVQILWVNLV TALTLSLSLS SEPAEPGIMS RPPRSTKEQI LSPRALAQVL
WSSVAIGGAA LLMFMRQNAV VDYDVAQTAA VTMLAFGQIA FLFNCRFLNT SSLTWRVLVG
NRAVWFSIAG LIALQLIFIH APFMNTWFGS SELGWAQWGP ILGLSVGVFL FNELGKFLIN
RVGRR
//
