ID Q03XK2_LEUMM Unreviewed; 896 AA.
AC Q03XK2;
DT 14-NOV-2006, integrated into UniProtKB/TrEMBL.
DT 14-NOV-2006, sequence version 1.
DT 27-MAR-2024, entry version 117.
DE SubName: Full=Cation transport ATPase {ECO:0000313|EMBL:ABJ62070.1};
GN OrderedLocusNames=LEUM_0964 {ECO:0000313|EMBL:ABJ62070.1};
OS Leuconostoc mesenteroides subsp. mesenteroides (strain ATCC 8293 / DSM
OS 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO 523 / NBRC 100496 / NCIMB
OS 8023 / NCTC 12954 / NRRL B-1118 / 37Y).
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Leuconostoc.
OX NCBI_TaxID=203120 {ECO:0000313|EMBL:ABJ62070.1, ECO:0000313|Proteomes:UP000000362};
RN [1] {ECO:0000313|EMBL:ABJ62070.1, ECO:0000313|Proteomes:UP000000362}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 8293 / DSM 20343 / BCRC 11652 / CCM 1803 / JCM 6124 / NCDO
RC 523 / NBRC 100496 / NCIMB 8023 / NCTC 12954 / NRRL B-1118 / 37Y
RC {ECO:0000313|Proteomes:UP000000362};
RX PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA Makarova K., Slesarev A., Wolf Y., Sorokin A., Mirkin B., Koonin E.,
RA Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA Baldwin K., Lee J.H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J., Hutkins R.,
RA O'Sullivan D., Steele J., Unlu G., Saier M., Klaenhammer T., Richardson P.,
RA Kozyavkin S., Weimer B., Mills D.;
RT "Comparative genomics of the lactic acid bacteria.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
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DR EMBL; CP000414; ABJ62070.1; -; Genomic_DNA.
DR RefSeq; WP_011679722.1; NC_008531.1.
DR AlphaFoldDB; Q03XK2; -.
DR EnsemblBacteria; ABJ62070; ABJ62070; LEUM_0964.
DR KEGG; lme:LEUM_0964; -.
DR eggNOG; COG0474; Bacteria.
DR HOGENOM; CLU_002360_3_3_9; -.
DR Proteomes; UP000000362; Chromosome.
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; PTHR43294:SF22; P-TYPE ATPASE; 1.
DR PANTHER; PTHR43294; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 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 72..90
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 96..113
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 260..281
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 287..311
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 697..717
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 729..748
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 768..788
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 794..815
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 836..855
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 867..886
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 19..92
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 896 AA; 98169 MW; 6442BBEE91108AFE CRC64;
MSTKSKEVDD DVPLSSSAKF HHQEWSKIVN DLHADYPSGL SDEQVNNRLQ KNGYNEVNPK
VIPKWLIFLR QFNNVIVYIL VVAALLTLFM QHYADSVVIA LVVLINALIG YLQEVNASNA
LDKIKNMLSV EATVIRDGER FDVPARELVP GDLVYLEAGD NVPADLRIID ADNLRIQESS
LTGEADSVLK NEAILSERVP LAERSNMAYA STAVTNGSAT GIVVNTGVHS QIGQISQSVA
DVSDKKSPLT RELDSLGHGI SWLIIVVAIV MFALGWFFKI YDISTLIMAI IAMIVGAMPE
GLPAATSIIL ATGVQKLTKK NAIVKTLPAA ETLGAIDIIA SDKTGTLTKN EMTIQDIIVG
ENHYTVTGTG YAPDGGIFIG NKLVDATQDK NLEMFLTMGH QANDTFLTEE AGIWTINGEP
TDAAFLSAYY KAFGQKVPKL KELDRIPFDS DYRYMARLVE NKHQQRFVAI KGAPDRLFTL
ARKDSNFDYE YWKKVSAKFA KSGKRVIAVG YVDVDSDTSE VLHETLAAEG VTFLGLAAII
DPPRPEVVDA ISDMREAGIR VKMITGDSPD TAKAIAQQLG LADQIEAVTG SEVEAMTDNQ
LAKVVTNYDV FARTTPQDKL RIISAYQANG LVTAMTGDGV NDAPALKKAD IGVAMGIKGT
DVAKDSADMV LANDDFSTIK VAIEQGRRLY DNIRKTILYL LPTSFAEGLI VVFSILLRQP
MPLTATQLLW INLVSALTLQ LAFIFEPAEP GLMKRPPRKT TAKLMSRYDV FQMVYVSVII
AAVALVVFEH LDDITGFAVA STMAVNILIF GKIFYMFNIR TAAPALSKTF WTNPMAFVAI
GAMIILQLLF TYVPFMQGVF STAALSLSDW SFIILTGLIV LIVTELDKYR RMIVKR
//
