ID I4W0R3_9GAMM Unreviewed; 841 AA.
AC I4W0R3;
DT 05-SEP-2012, integrated into UniProtKB/TrEMBL.
DT 05-SEP-2012, sequence version 1.
DT 27-MAR-2024, entry version 64.
DE SubName: Full=Cation transporting P-type ATPase {ECO:0000313|EMBL:EIL93054.1};
GN ORFNames=UU7_09800 {ECO:0000313|EMBL:EIL93054.1};
OS Rhodanobacter spathiphylli B39.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC Rhodanobacteraceae; Rhodanobacter.
OX NCBI_TaxID=1163407 {ECO:0000313|EMBL:EIL93054.1, ECO:0000313|Proteomes:UP000003226};
RN [1] {ECO:0000313|EMBL:EIL93054.1, ECO:0000313|Proteomes:UP000003226}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B39 {ECO:0000313|EMBL:EIL93054.1,
RC ECO:0000313|Proteomes:UP000003226};
RX PubMed=22843592; DOI=10.1128/JB.00871-12;
RA Kostka J.E., Green S.J., Rishishwar L., Prakash O., Katz L.S.,
RA Marino-Ramirez L., Jordan I.K., Munk C., Ivanova N., Mikhailova N.,
RA Watson D.B., Brown S.D., Palumbo A.V., Brooks S.C.;
RT "Genome sequences for six rhodanobacter strains, isolated from soils and
RT the terrestrial subsurface, with variable denitrification capabilities.";
RL J. Bacteriol. 194:4461-4462(2012).
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:EIL93054.1}.
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DR EMBL; AJXT01000024; EIL93054.1; -; Genomic_DNA.
DR RefSeq; WP_007807825.1; NZ_AJXT01000024.1.
DR AlphaFoldDB; I4W0R3; -.
DR STRING; 1163407.UU7_09800; -.
DR PATRIC; fig|1163407.3.peg.1972; -.
DR eggNOG; COG0474; Bacteria.
DR OrthoDB; 9814270at2; -.
DR Proteomes; UP000003226; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
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, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000003226};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 39..64
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 70..86
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 224..242
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 254..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 634..655
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 704..729
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 741..758
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 779..797
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 809..827
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 3..66
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 841 AA; 90111 MW; 4AE6379E1123D2C3 CRC64;
MNDKAAAPAR HGLGPAEAAR RLAADGPNLL PGNTPRSMLA IVGGVLTEPM FLMLLVAGGL
YLALGDRAEA AFLLSFVFVV IGITLAQERK TQRALESLRE LSAPRALVIR GGEEVRIPGR
EVVVGDLLVL HEGDRVAADA VLLDGHLDVN ESLLTGEAVP VTKLPGEDTG QLFASTVATK
GVGVAEVRAI AGATAVGRIG QALVDTAEPV SGLQRASRRL IRNLTIGGLL LATTYTLLGW
LWDSHGLLES VLAGIALTMA ILPEEIPVIL TVFLALGAWR ISKHKVLTRR VPAVEALGAI
SVLAVDKTGT LTQNRMQVAE LDLIGDTFRD AGADALPEPF HALVEFAMLA TPADPFDPME
KAIQQFGLRW LTNTEHVHAE WAPEFEYALS PEILAMTHVF RGDARDAHLL ATKGAPEAVI
DLCHLDADAA AAILRQVESM AERGLRVLGV ARGEWQGEAW PRSQHDFDFR FLGLLGFVDP
PRPEVPAAIA ECRSAGIRII MMTGDHPATA RAIAREVGLS ERAEVITGAE MAALDDVALR
ERLRRVDLCA RLKPEQKLRL VQLLREGGEV VAMTGDGVND APALKAADVG IAMGERGTDV
AREAAALVLL DDSFASIVSA IRQGRRIYDN ITKATRFVFA VHMPIIALAL VPALLHWPVL
LMPVHIVLLE LLIDPACSIV FEAEPADDDI MRRPPRAASD SPFAAANLRF AVIQGLGFAG
ILLLGYGLLP GQGMDAVQSR SAVFIALIMG LFLLTLANRD LSHPMLARHP AKNPWLRRMF
GAVTAMLVIV IGVPFFRGVM GLALPNAPLL LASAGMLLAA IAWLEFLRRA THVRPRAFVA
P
//
