ID R2SWG9_9ENTE Unreviewed; 876 AA.
AC R2SWG9;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE SubName: Full=Calcium-translocating P-type ATPase, PMCA-type {ECO:0000313|EMBL:EOH99575.1};
GN ORFNames=UAW_00727 {ECO:0000313|EMBL:EOH99575.1};
OS Enterococcus haemoperoxidus ATCC BAA-382.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1158608 {ECO:0000313|EMBL:EOH99575.1, ECO:0000313|Proteomes:UP000013858};
RN [1] {ECO:0000313|EMBL:EOH99575.1, ECO:0000313|Proteomes:UP000013858}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-382 {ECO:0000313|EMBL:EOH99575.1,
RC ECO:0000313|Proteomes:UP000013858};
RG The Broad Institute Genome Sequencing Platform;
RG The Broad Institute Genome Sequencing Center for Infectious Disease;
RA Earl A.M., Gilmore M.S., Lebreton F., Walker B., Young S.K., Zeng Q.,
RA Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Dewar J., Goldberg J., Griggs A.,
RA Gujja S., Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Enterococcus haemoperoxidus BAA-382.";
RL Submitted (FEB-2013) 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:EOH99575.1}.
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DR EMBL; AJAR01000010; EOH99575.1; -; Genomic_DNA.
DR RefSeq; WP_010760937.1; NZ_KE136479.1.
DR AlphaFoldDB; R2SWG9; -.
DR STRING; 155618.RV06_GL002189; -.
DR PATRIC; fig|1158608.3.peg.707; -.
DR eggNOG; COG0474; Bacteria.
DR OrthoDB; 9760364at2; -.
DR Proteomes; UP000013858; 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; 2.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF29; SECRETORY PATHWAY CALCIUM ATPASE, ISOFORM G; 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 50..69
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 75..94
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 242..260
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 272..297
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 674..694
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 706..725
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 746..764
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 776..795
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 815..839
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 845..865
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..74
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 876 AA; 96482 MW; 46F1D9C400F9E781 CRC64;
MTWYKMTAEQ VLTALQSSLN GLDRSVRKAK QEEGSNTLSK EKEASKLKKF FHHFHDLLIY
VLLVSAVLKG VSGDFIDMAI ILLVVIINAV IGYVQEAKAT DSLDSLTSMM SSEAVILIEG
EKETVKAESL VTGDIVYLSP GDIVPADLRV IDAYNLVIDE AILTGESTPV EKSNRTLEEE
EDLGDHINMA YSGTLVNSGT GKGIVIQIGD QTEIGKINQH LKNVGTNETP LIKKMKLLNK
QIFLFLMALI LFLVVFSLFF RELSASELLS SMIALAVSAV PEGLPAVLSI ILSVGVTRMA
RQHAIIKKMP AVETLGSMGV ICSDKTGTLT KNEMAVVALV TAKETIDTTL EEVEVASIRQ
VEKDESVRKM AEIASYCNDT KITYKNGVRE VIGNPTEGAL LDWANHTALV EEEHDISKIP
FDSSYKYMAT LVEIQDKRYI YLKGAPDVLL NMVDYQLADE STETFEEGYW QQKISQQATK
GQRILAAAFK EVTKAQTTLA HEDLQSGMII AGLFGIIDPP KKEAIEAVRN SRKAGISVKM
ITGDHKDTAV AIAKEIGLEN YNNALVGKDI EQLSDDELAD IVLTNDVYAR TTPEHKLRLV
HAIQKNGQIV GMTGDGVNDA PALKQADIGI AMGIKGTEVT KAAADMVLAD DNFATITLAI
KEGRRVYENL KKTIYFSLPT AFAQGLLVVV SLLLDRPLPL TSVQILWLNM VTTITLSFAL
GFEPLAKNGM EQPPRNPREN ILDRYAVFRI VYVSLLLAAL GFLVNVFLEG RNASEAVMQT
TLITTIVFGQ VFYMINCREI YQFSINKSIL SNKVLWLSLL ILFILQALLI VTPIMHLALG
TAVIGWPYIK LALLSGIFVF IVVEFEKQIT RKLKRL
//
