ID A0A109IQ05_9ACTN Unreviewed; 1471 AA.
AC A0A109IQ05;
DT 13-APR-2016, integrated into UniProtKB/TrEMBL.
DT 13-APR-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:SCG72691.1};
GN ORFNames=GA0070623_3705 {ECO:0000313|EMBL:SCG72691.1};
OS Micromonospora rifamycinica.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Micromonospora.
OX NCBI_TaxID=291594 {ECO:0000313|EMBL:SCG72691.1, ECO:0000313|Proteomes:UP000198226};
RN [1] {ECO:0000313|EMBL:SCG72691.1, ECO:0000313|Proteomes:UP000198226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44983 {ECO:0000313|EMBL:SCG72691.1,
RC ECO:0000313|Proteomes:UP000198226};
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; LT607752; SCG72691.1; -; Genomic_DNA.
DR RefSeq; WP_067300887.1; NZ_LT607752.1.
DR OrthoDB; 9814270at2; -.
DR Proteomes; UP000198226; Chromosome i.
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; 2.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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; 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};
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 621..691
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 1471 AA; 150273 MW; B506B50E117035B4 CRC64;
MTTLGRVAGR ILPSVPVPPL VGGVSRGVGS AAGRLARVAG LTRRRVWSRD GRHHIEVHGV
CQDGGDRLAR QVEVALQRLP GVAWARVNAP SGRVVVAVVE PKPRLRDLID TVARVERVCP
HEPDPEIPPP HPPEDGPRTP RTLGALASDA LGLTISAATR ILPFTPVPGE VAGLLTAVDL
HPKLHDLAGR GLRADPRAEV LFPLAEAVVQ GLTGGWAGIV LDGAQRVVQW GEARAQLATW
TRAEPGLTGD PERAVARSPG VHRPCPRPDG PVERYVSTML ATGAAAGAAA WPVAGPKRAA
ALGLAALPKA PGSGREGYAA QLGRMLARRG VIAMDRSVLR ELDRIDTVVL DAAVLGSARG
VLADLAPLAG ADTGEVAGRA FTLFDPDHPE DVHEAEGWRL GPLADLDAAD PGDTPDSARL
RAAGGPLLGL AHGGGLVAVV RVAPEPAPGV DALPTAARHA GLRLVVAGAD PQRYGFADAV
LPGGDRLAES VRALQRDGAV VMLVSGDRMA LAGSDCGLGV AAPEELPPWG AHLLVGTDLR
IPALLIEAAG VARRMTGQNI RLAMAGTGLG ALGAFTAAAP QLPGRSLAAV NGAAALAFAN
GVWRARRLPD PTGAPPPATT AWHLMPVATV LRQLDTGPDG LTDAEAQRRH RADPDPSAGP
VGLFRAFVDE LANPLTPVLA AGAVLSAAFG SLVDAALVGG VVGGSALVGA VHQRNTDRAL
AELLSRSAVT ARVLRDGAER VVPAEDLVCG DVVLLGPGDA VPADCRVLTA DGLEADESSL
TGESLPVGKG TGPVVAAALA DRTSMLYEGT TIATGRGTAV VVATGARTES DRSLALARQA
PPESGVEARL GRLTRSAIPL AVASAVAVAG AGLLRGVPLG QTAATAANLA VASVPEGLPF
LVSAAQLAAA RRLAEHGALV RNPRTIEALG RVDVLCFDKT GTLTEGRLLL AGVGDDDRFA
PVDRLDDGLR RVLAAGLRAT PYAADPQELP QHTDRAVRYG ARQAGVTEQH GAAGWAAVGG
LPFEPSRGYH ATVGRTAEGL LLSVKGAPET VLPRCGSWRL PGGRDEPLDA VRRDRLHTAL
ADRAGAGHRI LAVAECRAGA GAVTDDEVRG LVFVGFLALA DGVRESAAPA VRRIRQAGVH
TIMITGDHPA TAAAIAATIS PQADGQRVVT ATELDELDDA ALGERLARTD VVARCTPAHK
VRIIQALQRC GRTVAMTGDG ANDAPAIRLA DVGIALGQRG TPAARAAADL VVTDDRLETI
IATLVEGRAM WSSVRHALSI LVGGNLGEIA FSVLSAAVTG RSALNGRQLL LVNLLTDLAP
ALAIAVRPPG SDHADGLLRE GPDASLGDTM TREIGLRAAA TTLGATAGWT VARWTGRERR
AGTVALVSLV GTQLGQTVLA GGTSPTVLAS TAASVGVLAA VVQTPGVSQF FGCTPLGPVG
WGIAAGSALG ATFANGALTR LVEHLPAPPT R
//
