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Database: UniProt
Entry: R6YZL8_9FIRM
LinkDB: R6YZL8_9FIRM
Original site: R6YZL8_9FIRM 
ID   R6YZL8_9FIRM            Unreviewed;       986 AA.
AC   R6YZL8;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 47.
DE   SubName: Full=Cation-transporting ATPase P-type {ECO:0000313|EMBL:CDD23702.1};
GN   ORFNames=BN617_01389 {ECO:0000313|EMBL:CDD23702.1};
OS   Firmicutes bacterium CAG:345.
OC   Bacteria; Bacillota.
OX   NCBI_TaxID=1263020 {ECO:0000313|EMBL:CDD23702.1, ECO:0000313|Proteomes:UP000018232};
RN   [1] {ECO:0000313|EMBL:CDD23702.1, ECO:0000313|Proteomes:UP000018232}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MGS:345 {ECO:0000313|Proteomes:UP000018232};
RA   Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA   Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA   Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA   Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA   Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA   Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA   Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA   Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA   Wang J., Brunak S., Ehrlich S.D.;
RT   "Dependencies among metagenomic species, viruses, plasmids and units of
RT   genetic variation.";
RL   Submitted (NOV-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   -!- 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:CDD23702.1}.
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DR   EMBL; CBGR010000038; CDD23702.1; -; Genomic_DNA.
DR   AlphaFoldDB; R6YZL8; -.
DR   STRING; 1263020.BN617_01389; -.
DR   Proteomes; UP000018232; 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; 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:SF31; PLASMA MEMBRANE ATPASE-RELATED; 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   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:UP000018232};
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        220..243
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        249..267
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        395..413
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        447..471
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        792..812
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        824..842
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        854..873
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        893..913
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        925..946
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        958..979
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          182..238
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00690"
FT   REGION          1..62
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..55
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   986 AA;  109607 MW;  4B7F6C7EF7F11C97 CRC64;
     MAKDKKNFVE DEQSKEPQFS EIKETIIDEN IPEEGKEKKK KKFRDLFKSK EDDEEDKEPI
     EFTEETINPI DEESRFSNTS DIKKSEVLER LGKKSRSIKE ANSILEDIKD EEDISDKSQE
     NIEGIKKKAA EALRLADDET IELKVIRKIA ADDEKRKKYF SFLKFKKKNT PVQPKLDLSK
     ATRYEVDVET GLNDEQIKER FQNNYTNVDR NNHSKSIGRI FVDNIFTFFN VLLTIIAIAL
     IIVGSYTDLF FMVIAILNTG IGIFQEIRAK LTMDKLRLVT APTASVVRNG NTETIPTEQL
     VLDDIVLLSI GNQVPSDSIV QKGTIEVNES LLTGESLPIK KGPGDLIYAG SFVVSGSCAA
     KVEKIGDANY SSSIQNVAKQ YSKPKSELVK ALNRIIHVIS IVIIPLGIIS FYLNFTNAGN
     INPNIDLFDK ISDAIGKTAG SLIGKTAGSL ICMIPAGMYL LTSFALMSGV LRITKRNTVV
     RELYSIEMLA RVNVLCLDKT GTLTDGTMNV QEVVILKKNY DIKKVMGSYL SAFEDNNQTS
     IALQQAFRYN NDYHVIDSIP FSSVRKYSAA SFENMGTFIM GAPEFIYRQD NPELSKLIAE
     KQSHGLRVVM LAHTNAMIKN QKINGVVAPI ALFVLMDHIR DEAPETIKWF VENGVDIKII
     SGDSPLTASE IADNCGVPNA KNWISLDGLS INEVQEVANK YTVFGRVSPE QKAALVKAFK
     SSQKIVGMTG DGVNDIIAMK TSDCSIAMAS GADAAKNVAN LVLLDSNFAS MPKVVEEGRR
     VINNIQRSSS MFLMKTLFTI FLTLFVIFSN IFGSKMSYPF TPKHLMIMET FCIGIPSAIL
     ALQPNKSQIK GHFLRNVICS SLPGSCLLLL SLLCTLFPGR LGFFEINGNI DSQLSIISMA
     VIGMVICSLS MLYQISRPMD AYRTVLLIFM IICSVLTVFL APQNLIGINP FILNKIQWLV
     LGIILFASIP VSSGLTYIFN RFKQNN
//
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