ID A0A3A5LZL6_9MICC Unreviewed; 906 AA.
AC A0A3A5LZL6;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=Cation-translocating P-type ATPase {ECO:0000313|EMBL:RJT75961.1};
GN ORFNames=D6T63_16990 {ECO:0000313|EMBL:RJT75961.1};
OS Arthrobacter cheniae.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1258888 {ECO:0000313|EMBL:RJT75961.1, ECO:0000313|Proteomes:UP000272560};
RN [1] {ECO:0000313|EMBL:RJT75961.1, ECO:0000313|Proteomes:UP000272560}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hz2 {ECO:0000313|EMBL:RJT75961.1,
RC ECO:0000313|Proteomes:UP000272560};
RA Liu Q., Xin Y.-H.;
RT "Novel species of Arthrobacter.";
RL Submitted (SEP-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + H(+) + phosphate; Xref=Rhea:RHEA:13065,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:456216;
CC Evidence={ECO:0000256|ARBA:ARBA00001836};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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:RJT75961.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; QZVT01000013; RJT75961.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3A5LZL6; -.
DR OrthoDB; 9814270at2; -.
DR Proteomes; UP000272560; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma 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; 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; 3.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF29; SECRETORY PATHWAY CALCIUM ATPASE, ISOFORM G; 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 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 63..81
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 87..104
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 249..272
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..303
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 706..727
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 774..795
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 807..826
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 846..866
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 878..896
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 9..83
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 906 AA; 95977 MW; F406C0B2DF887A05 CRC64;
MISGVTQKAW HTRSAAESAA VLGVDPSAGL TTAEVNARRA RHGSNVLEDE AAVPVWRRIL
RLLADRMILV LVVAAVVSAI VSREWETPIV ILAVIVLNTV LNYVQESRAE NSLAALRTMS
VDTSRVRRDG RAEEVSNEEL VPGDIVLLEA GETIPADGRL LESARLQVAE AALTGESQPT
EKAAAILEDP ALPLADRTNM LFMNTDVTRG RAVMVVTGTG MDTQIGGIAT LLKGAGQGKT
PLQRRIDQLA QLLTVVALSV VTVVFVLGIL RGQSWSDLLI TAVSLAVATI PEGLTAVVAF
TLAMGASRMA SRGAIIKQLS AVETLGSTTH IATDKTGTLT LNEMTARRLH TMGRSFRVTG
EGYSSDGRIL TGDAEPLPPM SDALVAMALC NDAGIQAGKL VGDPTEGALV ALAAKGGIDV
EAVRGNHPRV AEVPFDSDYK FMATFHEQNF TEGDHTAARF RCFVKGAPGA LLERADSVLT
TEGIVPLTDM DRQKVEKDVQ AMAAEGLRTL MIAGRRLDGQ LPIDDDELRA AAKHLTVYAV
VGIVDPPRAE AAGAIATARA AGIAVHMITG DHLTTASSIA EQLGIPGEAA SGTELDGLND
DELNRRAAGF GVLARVAPEH KIRMIKALQQ DGNVVAMTGD GVNDAPALKQ ADIGIAMGIT
GTDVSKSAAK MILTDDNFAT IISAIEEGRG IYANIIKFVK FQLTTAWGFV LIFITAGVLG
LAGGAPFTAL QILWVNIIMD GPPALALGVD PAEPDIMKQK PRPADEPLLT RDRLLRILGL
GLVMAAGTIA VLALAPTLFP EASSNPLLGT TLAFTTFVFL QVFNLLNVRS ESGSVFSLQT
FTNRSIWVSL LAVVTLQVLV VNLDMLQGFF ETTALSPAQW GLTVLVGSSV LWVEEIRKAI
VRFRHH
//