ID A0A1X1SZZ9_9MYCO Unreviewed; 905 AA.
AC A0A1X1SZZ9;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Carbonate dehydratase {ECO:0000313|EMBL:ORV37482.1};
GN ORFNames=AWC01_16150 {ECO:0000313|EMBL:ORV37482.1};
OS Mycolicibacterium doricum.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=126673 {ECO:0000313|EMBL:ORV37482.1, ECO:0000313|Proteomes:UP000193564};
RN [1] {ECO:0000313|EMBL:ORV37482.1, ECO:0000313|Proteomes:UP000193564}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44339 {ECO:0000313|EMBL:ORV37482.1,
RC ECO:0000313|Proteomes:UP000193564};
RA Tarcisio F., Conor M., Antonella G., Elisabetta G., Giulia F.S., Sara T.,
RA Anna F., Clotilde B., Roberto B., Veronica D.S., Fabio R., Monica P.,
RA Olivier J., Enrico T., Nicola S.;
RT "The new phylogeny of the genus Mycobacterium.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; 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:ARBA00001836};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {ECO:0000256|ARBA:ARBA00004141}.
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:ORV37482.1}.
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DR EMBL; LQOS01000049; ORV37482.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X1SZZ9; -.
DR STRING; 126673.AWC01_16150; -.
DR Proteomes; UP000193564; Unassembled WGS sequence.
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 CDD; cd02080; P-type_ATPase_cation; 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; 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 PANTHER; PTHR42861:SF156; 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; 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 Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000193564};
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 65..83
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 89..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 252..270
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 282..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 733..751
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 771..794
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 810..830
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 842..863
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 875..894
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 11..85
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 905 AA; 95748 MW; FF9EA3AEA0D610B9 CRC64;
MMQPNLVTSN AHHGLPTHDV VLILQTDPHR GLSTSQAQER RVQFGPNVLP ETVGAGPLLR
ILRQFHHPLI YVLLVAGAVT ALLREYVDAT VIFAVVLVNA VVGFIQESRA EAALQSLRAM
VHTDARVVRD GREISITSEE LVPGDLVLIE AGDKVPADLR ILRETELRVD ESALTGESAP
VVKAEVELPE ATPVADRRNM AYSGTLVTAG TAAGVVVATG AVTEIGQIHR LVGAAEALAT
PLTAKLAQFS QILTVAILGL AAVTFALGLL RGQDPVETFN AAVALAVGAI PEGLPAAVTI
TLAIGVARMA KRRAVIRRLP AVETLGSTTV ICSDKTGTLT ENEMTVRKIW TPENSMEVTG
SGYAPEGTLL ATGGATVSID DDAALRWTLL GGAACNDAAL NRVDGRWQAT GDPTEAAMVV
VAAKAGIPPD RVGAELPRRA TIPFTSERQY MATLHEWGRS EHVVLVKGAV ERMLEICDSQ
MRADGSLRAL DRAAVTEAAD RLAAEGLRVL ACGIRTSVSP DEFGEEAVVG ATAFTGMQAM
LDPPRAAAAP AVTACHSAGI AVKMITGDHA GTARAIASAV GVLDRTDSTS DQVLTGAQLA
VTPADELPEA VQRASVFARV SPEQKLRLVR ALQQRGHVVA MTGDGVNDAP ALRQANIGVA
MGRGGTEVAK DAADMILTDD DFATIEAAVE EGRGVFDNLT KFITWTLPTN IGEGLVILVA
IALGATLPIL PTQILWINMT TAVALGLMLA FEPKEAGIMT RPPRDPDQPL LTSALVGRIL
LVSSLLVAGS WWLFQWELTH GAEVAEARTA ALNLFVVVEG FYLFSCRSLT RSAWRIGLFT
NRWLIVGVGV QAMAQLAITY LPAMNLVFQT APLDAGSWLR IFGIAVAISL VVAAEKWIRA
RRWSP
//
