ID A0A0M2PUV5_PROHO Unreviewed; 839 AA.
AC A0A0M2PUV5;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 39.
DE SubName: Full=ATPase {ECO:0000313|EMBL:KKI98423.1};
GN ORFNames=PROH_18365 {ECO:0000313|EMBL:KKI98423.1};
OS Prochlorothrix hollandica PCC 9006 = CALU 1027.
OC Bacteria; Cyanobacteriota; Cyanophyceae; Prochlorotrichales;
OC Prochlorotrichaceae; Prochlorothrix.
OX NCBI_TaxID=317619 {ECO:0000313|EMBL:KKI98423.1, ECO:0000313|Proteomes:UP000034681};
RN [1] {ECO:0000313|EMBL:KKI98423.1, ECO:0000313|Proteomes:UP000034681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CALU 1027 {ECO:0000313|EMBL:KKI98423.1};
RA Shanker A., Yadav P., Khan S., Sharma V.;
RL Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KKI98423.1, ECO:0000313|Proteomes:UP000034681}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CALU 1027 {ECO:0000313|EMBL:KKI98423.1};
RA Syromyatnikov M.Y., Popov V.N.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KKI98423.1}.
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DR EMBL; AJTX02000008; KKI98423.1; -; Genomic_DNA.
DR RefSeq; WP_017712914.1; NZ_KB235938.1.
DR AlphaFoldDB; A0A0M2PUV5; -.
DR STRING; 317619.GCA_000332315_02563; -.
DR eggNOG; COG2217; Bacteria.
DR OrthoDB; 525483at2; -.
DR Proteomes; UP000034681; 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 CDD; cd00371; HMA; 1.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 3.30.70.100; -; 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; 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; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
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; PF00403; HMA; 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 SUPFAM; SSF55008; HMA, heavy metal-associated domain; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01047; HMA_1; 1.
DR PROSITE; PS50846; HMA_2; 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, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000034681};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362081}.
FT TRANSMEM 108..126
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 132..155
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 176..196
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 369..391
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 457..480
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 783..802
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 808..832
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 19..85
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 839 AA; 88230 MW; 7C6431023C0E7146 CRC64;
MAPLAPQPLR PIVPVSAPQT LALEVDGMKC AGCVRAVETR LTQQPGVLSA SVNLVTRVAT
VDYAPQDTDG DTLAQVLTAV GFPSQRRDRP RTADESLREA DQALQHQTRN LAIAALLLIL
SSIGHLEHLF GWVLPGFDAM VVHWGLATLT LAFPGRPLWV NGFQGLRHGI PTMNTLVGLG
AWSAYLASCV ALVLPSLGWE CFFDEPVMLL GFILLGRTLE QRARHRAGAS LRTLLALQPT
LARLIAEGGL GDREAWDPRQ LLNAKVVEVA TDRLRVGELL RVLPGEKFPV DGAVVAGQGT
VDESMLTGES LPVLKQAGSG VSAGSLNLSG VLVVEATQVG QDTTLAQIIQ LVETAQGRKA
PIQRLADTVA GYFTYGVMAI AALTFGFWAL VGTRIWPSVL TDHGVWLMGM DHALDHALNH
ALDHALDPAL GQAMDSAMAM ATPAEALTSP LLLSLKLAIA VLVIACPCAL GLATPTALLV
GSGLGAEKGL LIRGGDALEH LDRLTTLVFD KTGTLTTGKP QVTDCRVNGD VTQPSGAEGD
GSVVGGDRLL QLAASLEVGT RHPLARAIQQ AAQDQGLPLL RADQFHTEPG FGVSAQVEGV
PTVLGNRSWL LDHGMAVPPP LEAQAETLAA TGKTVIYLGQ GSQTLGLIAV QDPLRPDALE
TLNQIKAWGL EVLMVTGDRP ATALAIAQAL HLDPSQVRAE VRPDQKAVVI RQLQSQGQQV
AMVGDGINDA PALAQAEVGI ALHGGTEVAA ETAHIVLMGD RLGQVPEALA LGKATLSKIR
QNLFWALAYN SLGIPVAAGL LLPHWGFALS PAVAGAFMAF SSISVVSNSL LLRWGRSPE
//
