ID A0A259FN75_9PROT Unreviewed; 905 AA.
AC A0A259FN75;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Carbonate dehydratase {ECO:0000313|EMBL:OZA39851.1};
GN ORFNames=B7X87_02245 {ECO:0000313|EMBL:OZA39851.1};
OS Hydrogenophilales bacterium 17-64-34.
OC Bacteria; Pseudomonadota; Hydrogenophilia; Hydrogenophilales.
OX NCBI_TaxID=1970527 {ECO:0000313|EMBL:OZA39851.1, ECO:0000313|Proteomes:UP000216129};
RN [1] {ECO:0000313|EMBL:OZA39851.1, ECO:0000313|Proteomes:UP000216129}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=17-64-34 {ECO:0000313|EMBL:OZA39851.1};
RA Kantor R.S., Colenbrander Nelson T., Marshall S., Bennett D., Apte S.,
RA Camacho D., Thomas B.C., Warren L.A., Banfield J.F.;
RT "Lifting the veil on microbial sulfur biogeochemistry in mining
RT wastewaters.";
RL Submitted (MAR-2017) to the EMBL/GenBank/DDBJ databases.
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:OZA39851.1}.
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DR EMBL; NCIL01000002; OZA39851.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A259FN75; -.
DR Proteomes; UP000216129; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
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:SF29; SECRETORY PATHWAY CALCIUM ATPASE, ISOFORM G; 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 Pfam; PF08282; Hydrolase_3; 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 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 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 58..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 249..270
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 276..305
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 693..718
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 724..745
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 766..787
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 793..815
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 835..855
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 867..884
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..82
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 905 AA; 96254 MW; CD1A83EA4D3BDCBA CRC64;
MQSRPPVMNW HALSVADTLR HLAATRSGLD TDAVSARRTE HGPNRLPPPL RTPAWKRFLL
QFHNVLIYVL LVAGGITALL AHWVDSGVIF GVVAINALIG FFQEGRAEQA LDAIRELLSP
RAIVTRAGIR HEIDAADLVP GDIVHLASGD RVPADLRLID VRNLRVTEAA LTGESLAVDK
QANPVDPQAP LGDRASMVWA GTLVVIGQGT GIVVATGSRT ELGRISGLLA SVEPLATPLT
RQMTRFGQWL AAVTLLLAAL VFGFGVWVRG YPASEMFLAA VGLAVAAIPE GLPAIMSIAL
AIGVTRMARR HAIIRRLPAV ETLGAVSVIC TDKTGTLTHN EMTVESVLTA DSRYRVSGSG
YAPEGGFRLD DQALDAASQP LLLEAARAAA LCNDADLHES AAGWQLAGDP TEGALLTLAL
KAGLDLPTLR TAYPRLDVIP FESEHRFMAS LHHDHAGHAF LLLKGAPERV LALCVAERNA
SGDRPLDADA WQVRMHATAA AGMRLLALAT RPTGTSAALS FADVEAGGFT LLALLGLADP
PREEAVRAVA DCRAAGIRVK MITGDHVATA RAIASQLGLD ASRALTGADI ERLDEAGLQE
AVLATDVFAR ASPEHKLRLV NALQSRGIVT AMTGDGVNDA PALRRADVGV AMGRKGTEAA
KEAAEMVLAD DNFASIAHAV EEGRTVYGNI RKAIVFTLPT NIGEAAMILV AILFGLTLPI
TPVQILWVNM VTAVTLALAI AFEHAEPDVM RQPPRDPAVP LLTRFLLWRV AFVATLLVAG
SMGLFLWEQA RGMSIEVART AAVNALVAGE IFYLFNCRHL TAPVAGWSDF IGNRVALAAA
GVLIALQGLF TYAPAMHALF KTAPLDAEAW LKIVVFGFVV YGIVEIEKGV FRRRLQGRRS
PARMA
//