ID C0DB02_9FIRM Unreviewed; 952 AA.
AC C0DB02;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 67.
DE SubName: Full=Putative calcium-translocating P-type ATPase, PMCA-type {ECO:0000313|EMBL:EEG51490.1};
GN ORFNames=CLOSTASPAR_06457 {ECO:0000313|EMBL:EEG51490.1};
OS [Clostridium] asparagiforme DSM 15981.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae;
OC Enterocloster.
OX NCBI_TaxID=518636 {ECO:0000313|EMBL:EEG51490.1, ECO:0000313|Proteomes:UP000004756};
RN [1] {ECO:0000313|EMBL:EEG51490.1, ECO:0000313|Proteomes:UP000004756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG51490.1,
RC ECO:0000313|Proteomes:UP000004756};
RA Fulton L., Clifton S., Fulton B., Xu J., Minx P., Pepin K.H., Johnson M.,
RA Bhonagiri V., Nash W.E., Mardis E.R., Wilson R.K.;
RL Submitted (JAN-2009) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:EEG51490.1, ECO:0000313|Proteomes:UP000004756}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15981 {ECO:0000313|EMBL:EEG51490.1,
RC ECO:0000313|Proteomes:UP000004756};
RA Sudarsanam P., Ley R., Guruge J., Turnbaugh P.J., Mahowald M., Liep D.,
RA Gordon J.;
RT "Draft genome sequence of Clostridium asparagiforme (DSM 15981).";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {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:EEG51490.1}.
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DR EMBL; ACCJ01000543; EEG51490.1; -; Genomic_DNA.
DR AlphaFoldDB; C0DB02; -.
DR HOGENOM; CLU_002360_3_3_9; -.
DR Proteomes; UP000004756; 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 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; 3.
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; PF00702; Hydrolase; 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 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 102..119
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 125..142
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 306..326
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 332..354
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 753..773
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 851..871
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 891..910
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 922..941
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 49..122
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 952 AA; 103066 MW; 139467C899BC1020 CRC64;
MRREKPEIRR TAAFGRVFGP AGRGRSQGNV TWTHRFRENK RKGETDMADW FRLSKQETMS
QLTTGGQGLG SREAKERLKQ YGENVIEEAG RKQWWQVFLE QFKDLLVIIL IVAAGISMVT
GDPGSAGVIF AVLLLNAVLG TVQHQKAEKS LDSLKSLSSP EARVRRDGRQ LDIPSSQVVP
GDILLLEAGD LVAADARLIE VYGLQVNESS LTGESLNVDK QDTVLGKTRR NGRGAVDKSG
PADDVPLADR VNMVFSGSLV TGGRGVAVVT ATGMDTEIGK IASMMNGTEE HKTPLQISLD
RFSGRLAAAI IAISAVVFAL SLYRKAQVLD ALMFAVALAV AAIPEALSSI VTIVQAMGTQ
KMAREHAIIK DLKAVESLGC VSVICSDKTG TLTQNRMEVE YACLNHRERD MDWMRENAFR
PDVRLLLYGA VLNNDASADP EGQTARDVGE PMELALLHMA AQAGMTPELV RARCPRLGEL
PFDPRRKLMS TKNQVEDGQI IFVKGALDVL LDRCDRIANP GSAKSAVRPG SGGESAALAS
RTLTAQDRRR IADQNMNWSS QGLRVLAFAC KPAEEIPGEK ARAEENLIFL GMVAMMDPPR
SESRAAVQNA RRAGIRTVMI TGDHKVTAMA IARRIGIMDE KTQALTGAEL NAMDDGELSR
RLDSISVYAR VSPEHKIRIV DAWQKRGSIV AMTGDGVNDA PALKKADIGV AMGITGTEVS
KDAASMILAD DNFATIIKAV ANGRNVYRNI KNAIQFLLSG NMAGILCVLY TSLSALPMPF
APVHLLFINL LTDSLPAIAI GMEPPEEGLL KEPPRNPREG ILTRTFVRDI LLQGGLIALA
TMWSYRTGLS TGGAAQASTM AFSTLTLARL FHGFNCRSRH SILHLGFGSN LYSLMAFELG
VVLLAAVLFV PGLQVMFAAA DLGLYQLLTI GFAAFAPTLV IQSFKMFRES VE
//
