ID R2PN60_ENTFC Unreviewed; 850 AA.
AC R2PN60;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 42.
DE SubName: Full=Calcium-translocating P-type ATPase, PMCA-type {ECO:0000313|EMBL:EOH57671.1};
GN ORFNames=UA3_00336 {ECO:0000313|EMBL:EOH57671.1};
OS Enterococcus faecium EnGen0263.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Enterococcaceae;
OC Enterococcus.
OX NCBI_TaxID=1158553 {ECO:0000313|EMBL:EOH57671.1, ECO:0000313|Proteomes:UP000013667};
RN [1] {ECO:0000313|EMBL:EOH57671.1, ECO:0000313|Proteomes:UP000013667}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAA1280 {ECO:0000313|EMBL:EOH57671.1,
RC ECO:0000313|Proteomes:UP000013667};
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., Courvalin P., Walker B., Young S.K.,
RA Zeng Q., 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 faecium UAA1280.";
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:EOH57671.1}.
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DR EMBL; AJAD01000005; EOH57671.1; -; Genomic_DNA.
DR RefSeq; WP_010731845.1; NZ_KB946086.1.
DR AlphaFoldDB; R2PN60; -.
DR PATRIC; fig|1158553.3.peg.341; -.
DR HOGENOM; CLU_002360_3_0_9; -.
DR Proteomes; UP000013667; 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 Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
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; 2.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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; 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 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 51..70
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 76..95
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 243..262
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 268..295
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 642..661
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 673..693
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 714..734
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 740..759
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 779..798
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 810..829
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..75
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 850 AA; 93839 MW; 104E79E8208CF564 CRC64;
MNWYKVTVED TLKNYQTSTE GLSQEERQKR LTDQGYNEIE ARQQTKRWKK IAKHFTDLLM
IVLIIASFLK FASSEYIEGS IILFVVIVNG LVSYWQERKA EESLNGLKQL MGQEAIVLSN
GMQEKIPAKE LVKGDVIVLR AGDVVPADVR LIEVHDLLVE ESILTGESEA SEKNHSVLAA
EESIGDQKNM AFSGTLVQSG SAVGVVVETG NTTEIGKINQ ALQSVEQQTT PLIKKINRLN
KQIFQGILCL ILFLVVFTTF RYGMDWHILL SAMIALVVSM VPEGLPAVLT MILSVGVHEM
AKEKAIIKGL PSVETLGSMT VICSDKTGTL TKNEMTVVDV AAKEETRVLS IMKNCQELKT
KEEQKTENLS GNPTELALIR HTETANLPLK KIEAKIPFSS EYKYMATMHA EEKGAVIYVK
GAPEVLLAKS TLSSSEQEAW GQTATAFAKK GQRVLGFAYK KVDSKQELTH ESLTQLTFAG
IAGLIDPPKE SAVKAVKECQ QAGISVKMIT GDHKDTAKAI AEQIGLKHTA KVLEGIDLDL
MSEEELIRQV PKVDVFARTT PEHKLRIVKA LQKNGEIVGM TGDGVNDAPA LKRADIGIAM
GIKGSEVSKQ AADMVLGDDN FHTIAKAVKE GRRILDNLQK TINFFLPTAL AQGLILIWAL
ILNRPLPLSP VQILWVNMVT TITLSYALGF ESPDPEIMKR PPRDPKQGIL SGYHLFRIIY
VALLIMVPAY LLAMQFEGQS LQQTILLQNI VLAQAVYMIN CRELSKPSLN QGLLQNKSLF
LSLGILALLQ GMVIFLPIGQ QLIGTVSLTM TQQLLIGANV ILLFLVVEIE KGIMNKLFRK
KEKTAREFSR
//
