ID A0A0R1MAK8_9LACO Unreviewed; 879 AA.
AC A0A0R1MAK8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE SubName: Full=Cation transport ATPase {ECO:0000313|EMBL:KRL05184.1};
GN ORFNames=FD46_GL001135 {ECO:0000313|EMBL:KRL05184.1};
OS Liquorilactobacillus oeni DSM 19972.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Liquorilactobacillus.
OX NCBI_TaxID=1423777 {ECO:0000313|EMBL:KRL05184.1, ECO:0000313|Proteomes:UP000051686};
RN [1] {ECO:0000313|EMBL:KRL05184.1, ECO:0000313|Proteomes:UP000051686}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19972 {ECO:0000313|EMBL:KRL05184.1,
RC ECO:0000313|Proteomes:UP000051686};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRL05184.1}.
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DR EMBL; AZEH01000034; KRL05184.1; -; Genomic_DNA.
DR RefSeq; WP_057896010.1; NZ_AZEH01000034.1.
DR AlphaFoldDB; A0A0R1MAK8; -.
DR STRING; 1423777.FD46_GL001135; -.
DR PATRIC; fig|1423777.3.peg.1169; -.
DR OrthoDB; 9760364at2; -.
DR Proteomes; UP000051686; 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:SF156; CALCIUM-TRANSPORTING 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; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000051686};
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 64..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..106
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 255..275
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 281..306
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 752..769
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 781..801
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 822..846
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 852..869
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 7..81
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 879 AA; 95204 MW; CD248E9C52970053 CRC64;
MKNDVHKFTK LKPTEVEKYF ETSCIKGLTA DSVTKRREKY GDNELVEAKK PNLLMQIIHH
LDDITSLILL FAVALSAYLA LTTDSDWTKA IVIGAIVILN VGIALFQEHS AEKALSALKS
MTQQTVTVIR AGEKQVIPTN ELVPGDLISL ESGDIVPADS RIIKSTSLSA DEAILTGESL
PIEKTANAMD VAPESLGDSK NMLFSGTAIT QGTATAIVTA TGMQTELGKI ATLLNTTQKQ
QTPLSKRLDS LTKRLSFVAV LGGTATILIA TLFHQETFTE SLMFGVSLAI AAVPETLPVI
VTLSMAHGVQ KMAKKKAIIR QVSAVETIGN VNVIASDKTG TLTQNKMTIT KYWPENKNVR
TVEKIKGSEK LAKEDKQFLT YLGLSTNAEL TTNGKADIGD PTELAIVHLL ARFKMTRAEC
EKSYPRIAED PFDSDKKTMT TWHKRPDGKY VAIIKGAIDR IPFGKSVEKN KLYDIHDQFA
AEALRVLAAG FQVFDSLPAE RNDDALTDIQ LLGLIGIIDP PRPEVIPAIK AAQKGGIATV
MITGDHLETA KAIAQEIGIL KAGKIAITGQ QLNELDDEEF AAKIDSIRVY ARTSPADKIR
IVKAWQSHGA IVAMTGDGVN DAPALKAANV GIAMGITGTE VSKNAADMVL ADDNFATIIE
AVKQGRTVYE NILKAVEFLV SVNFAQIFTM VGAIAMGWGA PMTPEQLLIV NVLADGIPGF
FLSREIAEPG IMNFSPIKKD TSIWSRGLGK RVAVRSATYI ILILAIYVLG RFGLNNNLPE
IGTTMLFLVL AIGSMLDIYP IKTRQSITKH AYTNNPALNK SLIFTLLGIV IIALFQPLAT
LFSIAALNLT EWVIVIVAIF IPTIVIELYK RSQGKIAKS
//
