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Database: UniProt
Entry: A0A101VCW5_9FIRM
LinkDB: A0A101VCW5_9FIRM
Original site: A0A101VCW5_9FIRM 
ID   A0A101VCW5_9FIRM        Unreviewed;       920 AA.
AC   A0A101VCW5;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=ATPase {ECO:0000313|EMBL:KUO52452.1};
GN   ORFNames=APF76_05305 {ECO:0000313|EMBL:KUO52452.1};
OS   Desulfitibacter sp. BRH_c19.
OC   Bacteria; Bacillota; Clostridia; Moorellales; Desulfitibacteraceae;
OC   Desulfitibacter.
OX   NCBI_TaxID=1734395 {ECO:0000313|EMBL:KUO52452.1, ECO:0000313|Proteomes:UP000053015};
RN   [1] {ECO:0000313|EMBL:KUO52452.1, ECO:0000313|Proteomes:UP000053015}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c19 {ECO:0000313|EMBL:KUO52452.1};
RA   Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (OCT-2015) 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:KUO52452.1}.
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DR   EMBL; LOER01000016; KUO52452.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A101VCW5; -.
DR   STRING; 1734395.APF76_05305; -.
DR   Proteomes; UP000053015; Unassembled WGS sequence.
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:InterPro.
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; IPR001757; P_typ_ATPase.
DR   InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR   NCBIfam; TIGR01116; ATPase-IIA1_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   Pfam; PF00702; Hydrolase; 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        57..80
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        86..102
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        250..270
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        276..302
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        710..731
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        737..759
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        787..808
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        814..833
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        845..872
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        884..907
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          8..82
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   920 AA;  101043 MW;  27ACD009CAC8387C CRC64;
     MNIVRNDKWY QLSSQEVLEA LQTNQEQGLE NIIAEKRLSI YGSNTLEEKE QINPWKLFFS
     QFTDFMVLVL LGATMISGIL KEYADAITIL LIVFVNAILG FFQEYKAEKS LEALKSMTAP
     EASVIRNSTR KKIKAAELVP GDIIFLESGD KVPGDARVIE LSNLEVEEAA ITGESHPVKK
     KVDPLNKSEI GLGDRYNMVH MGTVITRGRA VAVVVATGMK TEMGQIAGLI QSVKTEETPL
     QKRLDGLGKW LVALCLIICA VVSITGIVRG EPVYKMFLAG VSLAVAAIPE GLPAIVTVAL
     AIGVQRMIKR NAIIRKLPAV ETLGCATIIC SDKTGTLTQN QMTVREIVTT SKSFTVTGEG
     YDPKGDILEN NLKVDFQKNK ELIKLLKIGV LCNNSRLEKD NLHIDGLMRN NKEKGNWGIN
     GDPTEGSLTV LGAKVGIWKE TIERKEKKIC EIPFDSERKR MTTIYETSDG AKKSYVKGAP
     EIVLQNCSHI LVQDNIVPLT STLRKHILDQ NIRLASKALR VLGLAYKELA YGEDFNEDVA
     EVDLIFVGLA GMIDPPRTSA IKAIAACKQA GIKPVMITGD YKATAEAVAK ELNICSSPDS
     VIDGSQLDKL NDNQLEKRVE GINVYARVSP KHKLRIVRAL KNNGHIVAMT GDGVNDAPAV
     KEADIGVAMG ITGTDVTKEA SAMVLADDNF ATIVAAIEEG RGIYDNIRKF IRYLLSCNVG
     EVMVMFLAAL MGMPLPLIPI QILWVNLVTD GLPAMALGVD NNAKDLMFRK PRHPKESVFS
     GGLGKKILVR GFQIGLATLF VFWLALQLGG GDLVLARTMA FSTLVFSQLF HVFHCKSERY
     SPFEVGVLSN PALIVAVCCS IAMQLTVIYL PFLQPVFQTT SLNWLHWSVI LLVAGWKTYL
     TAIYHYIAKP IRRKLVYLNN
//
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