ID A0A1Z2KXC3_9ACTN Unreviewed; 868 AA.
AC A0A1Z2KXC3;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=Putative calcium-transporting ATPase {ECO:0000313|EMBL:ARZ66694.1};
GN ORFNames=SMD11_1030 {ECO:0000313|EMBL:ARZ66694.1};
OS Streptomyces albireticuli.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1940 {ECO:0000313|EMBL:ARZ66694.1, ECO:0000313|Proteomes:UP000195755};
RN [1] {ECO:0000313|EMBL:ARZ66694.1, ECO:0000313|Proteomes:UP000195755}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MDJK11 {ECO:0000313|EMBL:ARZ66694.1,
RC ECO:0000313|Proteomes:UP000195755};
RA Wang Y., Du B., Ding Y., Liu H., Hou Q., Liu K., Yao L., Wang C.;
RT "Streptomyces albireticuli Genome sequencing and assembly.";
RL Submitted (JUN-2017) 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}.
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DR EMBL; CP021744; ARZ66694.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1Z2KXC3; -.
DR KEGG; salj:SMD11_1030; -.
DR Proteomes; UP000195755; Chromosome.
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; 2.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF156; CALCIUM-TRANSPORTING ATPASE; 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; 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 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 224..243
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 249..276
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 661..682
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 694..714
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 734..756
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 762..781
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 793..813
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 825..849
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 3..64
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 868 AA; 89758 MW; 68F3889B9ED4E8D4 CRC64;
MTTRPQDLQG LPQAEAERRL ARHGPNIVSS GRPTPVWRRV LAQLRDPLIL VLLGAMALTV
ATGDLVDTSI IAIVIVANST VGVAQEVRAE RAVAALRALS APVVRVVRDG AEREVNAADV
VPGDVVLLGE GDIVPADGRV IEAATLLVDE SSLTGESVPV AKETSPDDPV LGAVSAGTTV
LRGRGRVEVT ATGAASATGR IAALMAAPPG LTPLQHRLAR FGRALALAAV ALSAVVLAVG
ITRGQPVELM VVTAISLVVA AVPESLPAVV TLALALGARR MAQRHAIVRR LPAVETLGSI
TVLATDKTGT LTEGRMAAQR LWTPAGGEAT VSGIGYVPQG HVERDGHVLT AGQAADLSEL
LTAAVLCNDA ALQPPGAGNG TWTALGDPTE AALLAAAARL GLDMAELRER MPRVDEIPFS
SERKRMTTVH RRPGGDLRVV CKGAPETVLR AGLLAEGGPE PRDRALERAR QWAQQGYRVL
AVAAADRTAP APDDWEGGLT LLGMVAILDP PREAAAGTVT ACRAAGITPV LVTGDHPLTA
EAVARRLGIA FAQDTAVTGE GIQGGTVGDP TAVRVFARTT PEQKVGIVES WRQAGHVVAM
TGDGVNDGPA LRRADIGVAM GRRGTEVARQ AADLVLADDD IGTVVAAIEE GRRVYANVRR
FLLYALAGGS AEILVMLTGP ALGMALPLLP AQILWINLLT HGLPGVALGA EPTAGDSMHR
PPRPPEESVL GQGLWARILT LGVLITAVTL AVGYWAHGTG RPWQTLVFLT LGATQLGVGL
GSRARPGTLT NPFLLLALTA ALALQIAGAY VPVLRDLLGT RPPEWADLGA VGAAFVLGYG
AMRLQAWLVP EGGRARRLSR SGDASAAA
//
