ID E0REU8_PAEP6 Unreviewed; 932 AA.
AC E0REU8;
DT 02-NOV-2010, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2010, sequence version 1.
DT 27-MAR-2024, entry version 72.
DE SubName: Full=ATPase {ECO:0000313|EMBL:ADM70754.1};
GN OrderedLocusNames=PPE_02929 {ECO:0000313|EMBL:ADM70754.1};
OS Paenibacillus polymyxa (strain E681).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=349520 {ECO:0000313|EMBL:ADM70754.1, ECO:0000313|Proteomes:UP000002227};
RN [1] {ECO:0000313|EMBL:ADM70754.1, ECO:0000313|Proteomes:UP000002227}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E681 {ECO:0000313|EMBL:ADM70754.1,
RC ECO:0000313|Proteomes:UP000002227};
RX PubMed=20851896; DOI=10.1128/JB.00983-10;
RA Kim J.F., Jeong H., Park S.Y., Kim S.B., Park Y.K., Choi S.K., Ryu C.M.,
RA Hur C.G., Ghim S.Y., Oh T.K., Kim J.J., Park C.S., Park S.H.;
RT "Genome sequence of the polymyxin-producing plant-probiotic rhizobacterium
RT Paenibacillus polymyxa E681.";
RL J. Bacteriol. 192:6103-6104(2010).
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DR EMBL; CP000154; ADM70754.1; -; Genomic_DNA.
DR RefSeq; WP_013310900.1; NZ_CP048794.1.
DR AlphaFoldDB; E0REU8; -.
DR KEGG; ppy:PPE_02929; -.
DR eggNOG; COG0474; Bacteria.
DR HOGENOM; CLU_002360_1_0_9; -.
DR Proteomes; UP000002227; Chromosome.
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; PTHR43294:SF22; P-TYPE ATPASE; 1.
DR PANTHER; PTHR43294; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 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 Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989};
KW Transport {ECO:0000256|ARBA:ARBA00022448}.
FT DOMAIN 5..79
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 932 AA; 101469 MW; ED45BBAB2F031339 CRC64;
MEQAHWHQLS NEQLSTSLDV DPKQGLSEEQ LAERRERSGW NELSEGKRVS AILLLLNQFK
DFMMLVLMGA TLISGLLGEY LDAITIIAIV VLNGILGFVQ EFRAERSLRA LRQLSAPTAK
VLRGGKRIQV QARELVPGDI VLLESGDRIP ADVRWLSTNG CDVEESALTG ESVPVSKHSR
PIHAAEVPLG DQKNIGFMGT MMTRGTAQGM VIRTGMSTEM GKIADLIENT ESQETPLQHR
LEQLGKILII VALALTVLVV VAGILHGQPA MSMFLAGVSL AVAAIPEGLP AIVTIALALG
VQRMIKRKAI VRKLPSVETL GCASVICSDK TGTLTQNKMT VTKLWLDGRF WGVTGEGYDP
HGHIMDRDLP ADLKNGQSLR RLLQASVLCN NAEIVQADTE ELRSKKKTKE PTPAAVWELK
GDPTEGALVT LAAKGGVTRQ GLYELYTRER EFPFDSDRKR MSVLVRHQGG HIVFAKGAPD
VLLGQCSYIL WEGNVVPLTG TLRQKVLAAN EGMASEALRV LGVAYRDIRS HERVSTVEEA
EAQLIFIGLT GMIDPPRREV REAIGKCRRA GIRTVMITGD HGTTAEAIAQ QLGILQRGSH
VLTGQELSAM DDPALDKAVD TVSVYARVSP EHKLRIVKSL QRRGHVVAMT GDGVNDAPAI
KASDIGIAMG ITGTDVTKEA AALVLSDDNF STIVAAIEEG RNIYENIRKF IRYLLASNVG
EILTMFFAMM AGLPLPLLPI QILWVNLVTD GLPAMALGVD QPEKDLMEHK PRGAKENIFA
RRLGWKIISR GLLIGLCTLA AFWLTLRIAP DDAGQLTKAQ SVAFATLVLA QLIHVFDCRS
SRSIFHRNPF QNSYLVLAVL SSVVLMLVVM YVPVLQPIFK TVPLGLREWA LSIVAAGIPT
FLMGAGSVWG GRRNRRSGGN THFSAGRTKF SA
//