ID H0R0C9_9ACTN Unreviewed; 731 AA.
AC H0R0C9;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 24-JAN-2024, entry version 55.
DE SubName: Full=Putative cation-transporting ATPase {ECO:0000313|EMBL:GAB18530.1};
GN ORFNames=GOEFS_057_00060 {ECO:0000313|EMBL:GAB18530.1};
OS Gordonia effusa NBRC 100432.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1077974 {ECO:0000313|EMBL:GAB18530.1, ECO:0000313|Proteomes:UP000035034};
RN [1] {ECO:0000313|EMBL:GAB18530.1, ECO:0000313|Proteomes:UP000035034}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 100432 {ECO:0000313|EMBL:GAB18530.1,
RC ECO:0000313|Proteomes:UP000035034};
RA Yoshida I., Takarada H., Hosoyama A., Tsuchikane K., Katsumata H.,
RA Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia effusa NBRC 100432.";
RL Submitted (DEC-2011) to the EMBL/GenBank/DDBJ databases.
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 IB subfamily. {ECO:0000256|ARBA:ARBA00006024,
CC ECO:0000256|RuleBase:RU362081}.
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:GAB18530.1}.
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DR EMBL; BAEH01000057; GAB18530.1; -; Genomic_DNA.
DR RefSeq; WP_007317867.1; NZ_BAEH01000057.1.
DR AlphaFoldDB; H0R0C9; -.
DR STRING; 1077974.GOEFS_057_00060; -.
DR eggNOG; COG2217; Bacteria.
DR OrthoDB; 7059309at2; -.
DR Proteomes; UP000035034; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
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; 3.40.50.1000; HAD superfamily/HAD-like; 1.
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; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01511; ATPase-IB1_Cu; 1.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF8; COPPER-TRANSPORTING ATPASE 2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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 PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Cell membrane {ECO:0000256|RuleBase:RU362081};
KW Membrane {ECO:0000256|ARBA:ARBA00023136};
KW Metal-binding {ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000035034};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
SQ SEQUENCE 731 AA; 76442 MW; 0AE19F08212A65BA CRC64;
MTAVKVELAH QVCSAAAGRL RIVVPSFARA SDHRAVAVEE AVAAVAGVRA VHAFGRTGSV
VIWHRNTLTR DELLEAISAG LCADLDSLAR HTPHSADVSN GDLVRMGSGA VALVLLGLRR
YGLRRPPLLG PLSRTAATGV TIFSGYPFLR GAARSLRGGR AGTDALVSAA TVASLLLREN
VVALTVLWLL NIGEFLQELT LRRTRRAITD LLRGNTDTVW LRTDDGTEIQ VPLDTVGVGD
TVVVHEHVAI PVDGMIIDGD AAVDQSALTG ENLPVSKSVG DDVHAGSVVM SGRLVVTATA
VGADTAIGRV IARVEEAQHD RAPIQTVGDS FSRRFVPTSF ALSAVTFLAT RDLRRAMTML
LIACPCAVGL ATPTAISGAI GNGARRGILI KGGSHLEAAG RVTAIVFDKT GTLTAGRPVV
TNVIAFDDAW TPEGILAYAA SSEIHSRHPL AEAVIRSTEE RRIEIPPHAE CEVIVGLGMR
TRADDGRVFL LGSPALLARH DVTVSDAAST WVENLRAQCE TPLLLAVDGV LVGLLSLRDE
VRPEAAETLA RLRDSGITAI SMVTGDHPQT AAAIAAELGI TSWQAEVLPD DKLAEVRRLQ
DQGHVVAMVG DGINDAPALA AADLGIAMGL AGTDVAVETA DIALAADDLT KLLDVGDLGR
HTVAVVRQNY GMSIAVNALG LLVSAGGALS PVLAAILHNA SSVAVVLNSS RLIRYRVEEP
GTPRALSEPR P
//
