ID E3E875_PAEPS Unreviewed; 932 AA.
AC E3E875;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 2.
DT 27-MAR-2024, entry version 71.
DE SubName: Full=ATPase {ECO:0000313|EMBL:ADO57267.2};
GN Name=pacL {ECO:0000313|EMBL:ADO57267.2};
GN ORFNames=PPSC2_15490 {ECO:0000313|EMBL:ADO57267.2};
OS Paenibacillus polymyxa (strain SC2) (Bacillus polymyxa).
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=886882 {ECO:0000313|EMBL:ADO57267.2, ECO:0000313|Proteomes:UP000006868};
RN [1] {ECO:0000313|EMBL:ADO57267.2, ECO:0000313|Proteomes:UP000006868}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC2 {ECO:0000313|EMBL:ADO57267.2,
RC ECO:0000313|Proteomes:UP000006868};
RX PubMed=21037012; DOI=10.1128/JB.01234-10;
RA Ma M., Wang C., Ding Y., Li L., Shen D., Jiang X., Guan D., Cao F.,
RA Chen H., Feng R., Wang X., Ge Y., Yao L., Bing X., Yang X., Li J., Du B.;
RT "Complete genome sequence of Paenibacillus polymyxa SC2, a strain of plant
RT growth-promoting Rhizobacterium with broad-spectrum antimicrobial
RT activity.";
RL J. Bacteriol. 193:311-312(2011).
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DR EMBL; CP002213; ADO57267.2; -; Genomic_DNA.
DR RefSeq; WP_014600034.1; NC_014622.2.
DR AlphaFoldDB; E3E875; -.
DR STRING; 1406.LK13_03140; -.
DR KEGG; ppm:PPSC2_15490; -.
DR PATRIC; fig|886882.15.peg.3309; -.
DR eggNOG; COG0474; Bacteria.
DR HOGENOM; CLU_002360_1_0_9; -.
DR OrthoDB; 9813266at2; -.
DR Proteomes; UP000006868; 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, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000006868};
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}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 51..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 80..99
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 247..267
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 273..299
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 791..809
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 815..833
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 854..874
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 889..909
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..79
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 932 AA; 101639 MW; 1C012EFA5EE4E145 CRC64;
MEQAHWHQLS NEQLSTSLEV DPKQGLSEEQ IAERRERTGW NELSEGKRVS AVLLLLNQFK
DFMMLVLMGA TLISGLLGEY LDAITIIAIV VLNGILGFVQ EFRAERSLRA LRQLSAPTAK
VLRGGKRIHV QARELVVGDI VLLESGDRIP ADVRWLSTNG CDVEESALTG ESVPVSKHCR
PIHAAEVPLG DQKNIGFMGT MMTRGTAQGV VIRTGMTTEM GKIADLIENT ESQETPLQHR
LEQLGKILII VALALTVLVV VAGILHGQPA MNMFLAGVSL AVAAIPEGLP AIVTIALALG
VQRMIKRKAI VRKLPSVETL GCASVICSDK TGTLTQNKMT VTKLWLDGRF WGVTGEGYDP
HGHIMDRDLP ADLKNGQSLR RLLQASVLCN NAEIVQADID ELRSKKKTKE PTPSAVWELK
GDPTEGALVT LAAKGGVTRQ GLYELYTRER EFPFDSDRKR MSVLVRHQGG HIVFAKGAPD
VLLGQCSYIL WEGNVVPLTG TLRQKVLAAN EGMASEALRV LGVAYRDIRS HERVSTAEEA
EEQLVFIGLT GMIDPPRREV REAIGKCRRA GIRTVMITGD HGTTAEAIAQ QLGILQRGSH
VLTGQQLSLM DDAALDNVVD TVSVYARVSP EHKLRIVKSL QRRGHVVAMT GDGVNDAPAI
KASDIGIAMG ITGTDVTKEA AALVLSDDNF STIVAAIEEG RNIYENIRKF IRYLLASNVG
EILTMFFAMM AGLPLPLLPI QILWVNLVTD GLPAMALGVD QPEKDLMEHK PRGAKENIFA
RRLGWKIISR GLLIGLCTLA AFWLTLRIAP NDAGQLIKAQ SVAFATLVLA QLIHVFDCRS
SRSVFHRNPF QNSYLVLAVL SSIVLMLVVM YVPVLQPIFK TVPLGLREWA LSIVAAGIPT
FLMGAGSVWG GRRNRRHGGN THFSAGRTKF SA
//
