ID A0A1C6VGR5_9ACTN Unreviewed; 1520 AA.
AC A0A1C6VGR5;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=ATPase, P-type (Transporting), HAD superfamily, subfamily IC {ECO:0000313|EMBL:SCL65387.1};
GN ORFNames=GA0070603_3964 {ECO:0000313|EMBL:SCL65387.1};
OS Micromonospora chersina.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=47854 {ECO:0000313|EMBL:SCL65387.1, ECO:0000313|Proteomes:UP000198605};
RN [1] {ECO:0000313|EMBL:SCL65387.1, ECO:0000313|Proteomes:UP000198605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44151 {ECO:0000313|EMBL:SCL65387.1,
RC ECO:0000313|Proteomes:UP000198605};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) 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; FMIB01000002; SCL65387.1; -; Genomic_DNA.
DR STRING; 47854.GA0070603_3964; -.
DR OrthoDB; 9814270at2; -.
DR Proteomes; UP000198605; 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; 2.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF31; PLASMA MEMBRANE ATPASE-RELATED; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 655..725
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 152..172
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 437..458
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1520 AA; 155370 MW; C5C41C04CE80E194 CRC64;
MTSLGRVAGL LLSPAAVPDA VARVARGVAT ALPDTARTVG SALPGTARNA VPGSVAEAAG
SVGAAATRLA RLAGLTRRRV WSRDGRHHIE VHGVCQDGGD RLARQVEAAL EALPGVAWAR
VNAPSGRVIV AVEEPKPKLR DLIATVARTE RVCPHEPDPE IPPPHPPEEG PRTPRALGAL
ASDALGLTIS AATRILPFTP VPGEVAGFLA AVDLHPKLHA LADRGLRADP RAELIFPLAE
AVVQGLTGGW AGIVLDGAQR VVRWGEAQAQ LAAWTKAEPR LTGDPDRAVA RVPDGERPCP
VPDGPAERYV SRMLAAGAAA GAAAVPVAGG KRAAALALSS LPKAPGSGRE GYAAQLGRML
GRRGVIAMDR SVLRELDRID TVLLDAAVLG SDRGVLADLA PLAGADTGQV AARSFALFDP
AAPDAVRNAD GWRLGPLDRM DVTDPGDTPD SARLRSDGGR LLGLAEGGRL AAVLRVEPEP
VPGVDALATA ARHAGLRLVV AGDDDGRYDF ADALVPGGSR LAESVRELQR EGAVVMVVSG
DRAALGAADC GLGVSGPEDL PPWGAHLLVG DDLRIPALLI DATGVARRMT RQNIRISMAG
TGLGALGAFT AERERLPGRA LGAVNGAAAL AFAHGVWRAR RLPDRTRTPA PALTAWHLMP
VDTVLDQLGT HAEGLTGEEA ARRRRAVTGD GQGPPGLLRA FVDELSNPLT PVLAAGAVLS
ATFGSLVDAA LVGGVVGGSA LIGAVHQHNT ERSLAELLSR SAVTARVLRD GAEQVVAAEE
LVAGDVVAVG PGDAIPADCR VLTSDGLETD ESSLTGESLP VGKTAEPVVA AAVAERHSML
YEGTTVAAGH GTAVVVATGQ ETEAGRSLAL AREAPPASGV ETRLGKLTSA AVPLAAGSAI
AVAGAGLLRG VPLAETAATA ANLAVASVPE GLPFLVSAAQ LAAARRLAEH GALVRNPRTI
EALGRVDVLC FDKTGTLTEG KLLLAGVGGG DDRYAPPDRL DEPLRLTLAA ALRATPAATD
PDELPQQTDR AVRRGAGTAG VLEWTGAPDW TAVGGLPFEP SRGYHATVGR TAGGLLLSVK
GAPESVLPRC AARRTAQGDM PLDRAGRDAL HAMLAERAGA GHRILAVAEC PVGAESVTDE
QVDGMVFVGF LALADGVRES AAPAVRRIRQ AGVHTIMITG DHPATAEAIA ATISPDHGEQ
RVVTATELNR LDDEALAERL MATDVVARCT PAHKVRIIQA LQRRGRTVAM TGDGANDAPA
IRLADVGIAL GQRGTPAARA AADLVVTDDR LETIIATLVE GRAMWSSVRH ALSILVGGNL
GEIAFSVLTA ASTGRSALTG RQLLLVNLLT DLVPALAIAV RPPAADGADH LLREGPDTSL
GETLTREIAL RAGATTLGAT AGWTLARWTG RERRAGTVAL ASLVGTQLGQ TVLAGGTSPT
VLASTAASIG VLVAVVQTPG VSQFFGCTPL GPVGWTIAAG SALGATFANG ALTRLVDRLP
QRGAALHGET DQGYGEEHDA
//