ID A0A1I5B468_9MICO Unreviewed; 922 AA.
AC A0A1I5B468;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 28-JAN-2026, entry version 29.
DE SubName: Full=Plasma-membrane calcium-translocating P-type ATPase {ECO:0000313|EMBL:SFN69518.1};
GN ORFNames=SAMN05216219_1720 {ECO:0000313|EMBL:SFN69518.1};
OS Mycetocola miduiensis.
OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Micrococcales;
OC Microbacteriaceae; Mycetocola.
OX NCBI_TaxID=995034 {ECO:0000313|EMBL:SFN69518.1, ECO:0000313|Proteomes:UP000198867};
RN [1] {ECO:0000313|Proteomes:UP000198867}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.11101 {ECO:0000313|Proteomes:UP000198867};
RA Varghese N., Submissions S.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + H2O = ADP + phosphate + H(+); 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:ARBA00049360};
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIA subfamily. {ECO:0000256|ARBA:ARBA00005675}.
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DR EMBL; FOVM01000004; SFN69518.1; -; Genomic_DNA.
DR RefSeq; WP_090710553.1; NZ_FOVM01000004.1.
DR AlphaFoldDB; A0A1I5B468; -.
DR STRING; 995034.SAMN05216219_1720; -.
DR OrthoDB; 9814270at2; -.
DR Proteomes; UP000198867; 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 FunFam; 3.40.50.1000:FF:000028; Calcium-transporting P-type ATPase, putative; 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; IPR059000; ATPase_P-type_domA.
DR InterPro; IPR050510; Cation_transp_ATPase_P-type.
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:SF21; CATION TRANSPORTING 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 PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00120; HATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000198867};
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 83..103
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 250..272
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 278..307
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 786..805
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 858..878
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 890..907
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 2..76
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 922 AA; 96963 MW; C60D0819432F18D5 CRC64;
MNPSLESAEA VADLLGVDLE RGLSHTEAAK RLTEDGPNEL RGVKAKPLWL VFLAQFHDPL
IYLLLGAVAV SLAAWLAEGA EGWPIDAIVI SAIVVLNAVL GFVQEFRAAS AVAALATMTA
ASSTVVRDGA LETVHSSELV RGDLLALSEG DSVGADARIV GASALRIAEA SLTGESEAVE
KHPGLLSGPV PLGGRTNMAF KGTSVVQGVG RAVVTATGMD TEVGAIAHLL DATTEEPTPL
SLEVARIGRM LGIAVIAIAI VVMGTITIVN GISTPSDFVV VLLLGVSLAV AAVPEGLPAI
LSLVLAIGVQ RMARRNAVVK QLSAVESLGS ASVICTDKTG TLTRNQMTIE RLITASGRAD
VTGTGYTPLG EVLSGGSSLS ADGHTEARLL LTAGALANNA QLSERDDGWE IEGDPTEAAF
LVAARKLDGT TDRMDRFTRR AEIPFTSDRK MMSTVHSDAD GRTLLFSKGA PDVLLSNCTR
LRVGTTDVPL TDERRQQALD DIEALSSDAF RTLGAAYRPI SDDEDNVSEA LEHDLVYAGT
AGIIDPPRSE VAAAIAEAQR AGIRIVMITG DHPATATRIA VDLGIVKRGA RALTGTEIDD
LDADALREAT RTVSVFARVA PLHKLRLVDA LQADGRIVAM TGDGVNDAPA LKSADIGIAM
GITGTEVTKE AARMILADDN FATIVAAVRQ GRAIFDNIKK FLRYLLSSNM GEVLTVFLGV
VFAAALGLAG AGTETVVIPL LATQILWINL VTDSGPALAM GVDPEVDDVM ARAPRKLTDR
AIDGRMWAGI LSIGLVMALV TLATIDRFLP GGFLEGSDSL DVARTAGFTT LVFTQLFNAF
NARSETTTAF HGLFSNPWLW GSVALAALLQ VAVVQVPFLQ VAFGTTPLDL AHWLWCVVAA
SAVLWFSEIR KAGYRLLERR RR
//
