ID L0FBZ7_DESDL Unreviewed; 913 AA.
AC L0FBZ7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
DE RecName: Full=P-type Ca(2+) transporter {ECO:0000256|ARBA:ARBA00012790};
DE EC=7.2.2.10 {ECO:0000256|ARBA:ARBA00012790};
GN OrderedLocusNames=Desdi_2757 {ECO:0000313|EMBL:AGA70171.1};
OS Desulfitobacterium dichloroeliminans (strain LMG P-21439 / DCA1).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Desulfitobacteriaceae;
OC Desulfitobacterium.
OX NCBI_TaxID=871963 {ECO:0000313|EMBL:AGA70171.1, ECO:0000313|Proteomes:UP000010797};
RN [1] {ECO:0000313|Proteomes:UP000010797}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG P-21439 / DCA1 {ECO:0000313|Proteomes:UP000010797};
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA Peters L., Ovchinnikova G., Teshima H., Detter J.C., Han C., Tapia R.,
RA Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Kruse T.,
RA de Vos W.M., Boon N., Smidt H., Woyke T.;
RT "Complete sequence of Desulfitobacterium dichloroeliminans LMG P-21439.";
RL Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP003344; AGA70171.1; -; Genomic_DNA.
DR RefSeq; WP_015263137.1; NC_019903.1.
DR AlphaFoldDB; L0FBZ7; -.
DR STRING; 871963.Desdi_2757; -.
DR KEGG; ddl:Desdi_2757; -.
DR eggNOG; COG0474; Bacteria.
DR HOGENOM; CLU_002360_1_0_9; -.
DR OrthoDB; 9760364at2; -.
DR Proteomes; UP000010797; Chromosome.
DR GO; GO:0016020; C: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 GO; GO:0005388; F:P-type calcium transporter activity; IEA:UniProtKB-EC.
DR CDD; cd02089; P-type_ATPase_Ca_prok; 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; IPR005782; P-type_ATPase_IIA.
DR InterPro; IPR006413; P-type_ATPase_IIA_PMR1.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01116; ATPase-IIA1_Ca; 1.
DR NCBIfam; TIGR01522; ATPase-IIA2_Ca; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 3.
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:UP000010797};
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 52..77
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 83..102
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 273..299
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 780..800
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 845..864
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 876..899
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..79
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 913 AA; 99034 MW; EAA2777CB860FBF8 CRC64;
MRQQAWHVLP WLDVVKALGV HPGKGLTPRE VSRRLGEVGT NILESKKGVH PVFLFLGQFK
DFMVLVLLAA TIVSALLGEI ADAVTIMAIL VLNAVLGFIQ EYRAERSIES LKSLTAPEAR
VLRDGLESRI PATELVPGDI VLLEAGDRIP ADLRWIQAVN VEVEESALTG ESHPVAKRVA
PLTDELTPMA DRANMGYMGT ALVAGRGAGV IVATGMETEM GIIAGMIQSV EEEETPLQKR
LAQLGKYLVV ISIAVCGIVV LTGILRGEGV YKMFLAGVSL AVAAIPEGLP AIVTVALAIG
VQRMVKRKAI IRKLPAVETL GCATVICSDK TGTLTQNEMT VRQIYTDRKM IVVTGQGYDP
KGEFHGADPL KEKGPLQNAL KIASLCNNSS LTRKGVQVAG MFRSAGKEAP WGIEGDPTEG
ALLVAAAKAG IWRETLERKE ERVGEIPFDS DRKRMSVIYK GRREKNAYVK GAPDEILRRC
THELTGDGVV ELSEIRRRAI FRANDEMAKK ALRVLALAQK PLKEYERVDE RVEEDLVFVS
LMGMIDPPRT SAGKAIVVCR KAGIKPVMIT GDHRLTAEAV ARELGILKGN NGGILTGVEL
DKMSDEELEK EVMDVSVYAR VTPKDKLRIV RALKKNNQIV AMTGDGVNDA PAVKEADIGI
SMGKTGTDVT KEASAMVLAD DNFATIVAAV EEGRAIYDNI RKFIRYLLSC NIGEVLVMFL
AALIGLPLPL LAIQILWVNL VTDGLPAMAL GVDGMDKDIM NRKPREPGES IFARGLARKI
LTRGVIIGVG TLVVFVVALL LGVNMLVART MAFTTLVFSQ LFHVFDCKSE TRGIFEVNLF
SNPYLIAAVA GSTIMQLSVI YFPPLQAIFK TTALLGWQWG LILLVAGGPS ILIGLYRLVR
NTWHGKRTMV GAK
//
