ID A0A2P1PP41_9GAMM Unreviewed; 787 AA.
AC A0A2P1PP41;
DT 23-MAY-2018, integrated into UniProtKB/TrEMBL.
DT 23-MAY-2018, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE SubName: Full=ATPase P {ECO:0000313|EMBL:AVP96613.1};
GN ORFNames=C7S18_05085 {ECO:0000313|EMBL:AVP96613.1};
OS Ahniella affigens.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Ahniella.
OX NCBI_TaxID=2021234 {ECO:0000313|EMBL:AVP96613.1, ECO:0000313|Proteomes:UP000241074};
RN [1] {ECO:0000313|EMBL:AVP96613.1, ECO:0000313|Proteomes:UP000241074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D13 {ECO:0000313|EMBL:AVP96613.1,
RC ECO:0000313|Proteomes:UP000241074};
RA Ko Y., Kim J.-H.;
RT "Ahniella affigens gen. nov., sp. nov., a gammaproteobacterium isolated
RT from sandy soil near a stream.";
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AVP96613.1, ECO:0000313|Proteomes:UP000241074}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=D13 {ECO:0000313|EMBL:AVP96613.1,
RC ECO:0000313|Proteomes:UP000241074};
RA Keele B.F.;
RL Submitted (MAR-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362081}.
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}.
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DR EMBL; CP027860; AVP96613.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2P1PP41; -.
DR KEGG; xba:C7S18_05085; -.
DR OrthoDB; 9814270at2; -.
DR Proteomes; UP000241074; Chromosome.
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 GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR CDD; cd00371; HMA; 1.
DR CDD; cd02079; P-type_ATPase_HM; 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; IPR021993; ATPase-cat-bd.
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 NCBIfam; TIGR01511; ATPase-IB1_Cu; 1.
DR NCBIfam; TIGR01512; ATPase-IB2_Cd; 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:SF5; CATION-TRANSPORTING P-TYPE ATPASE-RELATED; 1.
DR Pfam; PF12156; ATPase-cat_bd; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
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; PS01229; COF_2; 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:UP000241074};
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 174..191
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 211..231
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 243..262
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 268..286
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 423..445
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 451..477
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 742..761
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 90..156
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 787 AA; 83968 MW; 61EA99F67C5615D6 CRC64;
MNTLNPALAG TNAGCFHCGE PLTGPALLAK GQRYCCTGCL AAAEFIHQQG LGDYYRLRTE
RGSRPEHSDL SVFDRPEVQA RYAEKLGEQC AIELAVEGMH CAACAWLIGE TLRRLPGVTD
ASASVVSARL RLVWTPGAVQ LSDALQRVET LGYGLSLAGT NAQQEQRRKA RRTLMLRLGI
AALATMQAMM FSEALYLDKA GEMSVATRDF FRWLTFLMST PVLSYSAWPF WRGALNEWRL
RRFGMDTLAA VSIALAYGAS LVETIRGGPF VWFDAAVMFV FFLLLARSLE GMLRSRGQAQ
LDRMAAARPA LAMRRVDDRV QTVPAEEIAV GDVVLVAAGA TVPADGKLCS HAAQFDESLL
HGESRPQARL QGDRVLAGSI CLNAQIEIQV TAVGAETRLS EIERAMLRAA ETRPAMARWL
DRLVQRFVLI VFGLAIVTAI GWSVVDPSLS LPYALAVLMV SCPCALALAI PTAILAAQSK
LVRAGVLCLD TDALLKLRQL DRVVFDKTGT LTEGHPRIAA VDVFGAVDTA VCLALARALE
QHVHHPIAEA FAGASPYVAE HVVVTAGAGV SGHIDGQSYR LGSADFCDYP GSDRAGVFLR
HDAGILARFR LSDALRPEAS AVVASLQSEG LAVTLLSGDQ SAAVQTVADQ IGVADARSSL
SPEAKLATLQ QYRQAGQVVA MLGDGINDAP VLAAADVGFT LAKAAPLAQH ASALIALNGS
LEGFLVARRM SAALHDVIRQ NLGWALGYNV LMLPLAAFGV VGPGLAAIGM SVSSLFVTLN
AMRLYRQ
//
