ID E4PRN3_MARAH Unreviewed; 908 AA.
AC E4PRN3;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 27-MAR-2024, entry version 68.
DE SubName: Full=Cation-transporting ATPase, E1-E2 family protein {ECO:0000313|EMBL:ADP99130.1};
GN OrderedLocusNames=HP15_3366 {ECO:0000313|EMBL:ADP99130.1};
OS Marinobacter adhaerens (strain DSM 23420 / HP15).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Marinobacteraceae; Marinobacter.
OX NCBI_TaxID=225937 {ECO:0000313|EMBL:ADP99130.1, ECO:0000313|Proteomes:UP000007077};
RN [1] {ECO:0000313|EMBL:ADP99130.1, ECO:0000313|Proteomes:UP000007077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23420 / HP15 {ECO:0000313|Proteomes:UP000007077};
RX PubMed=21304739;
RA Gardes A., Kaeppel E., Shehzad A., Seebah S., Teeling H., Yarza P.,
RA Glockner F.O., Grossart H.P., Ullrich M.S.;
RT "Complete genome sequence of Marinobacter adhaerens type strain (HP15), a
RT diatom-interacting marine microorganism.";
RL Stand. Genomic Sci. 3:97-107(2010).
RN [2] {ECO:0000313|Proteomes:UP000007077}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 23420 / HP15 {ECO:0000313|Proteomes:UP000007077};
RA Gaerdes A.A.M., Kaeppel E., Shezad A., Seebah S., Teeling H., Yarza P.,
RA Gloeckner F.O., Ullrich M.S.;
RT "Complete genome sequence of Marinobacter adhaerens type strain (HP15).";
RL Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP001978; ADP99130.1; -; Genomic_DNA.
DR AlphaFoldDB; E4PRN3; -.
DR STRING; 225937.HP15_3366; -.
DR KEGG; mad:HP15_3366; -.
DR PATRIC; fig|225937.3.peg.3392; -.
DR eggNOG; COG0474; Bacteria.
DR HOGENOM; CLU_002360_4_1_6; -.
DR Proteomes; UP000007077; Chromosome.
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; 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; 1.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1.
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; 3.
DR PANTHER; PTHR42861; CALCIUM-TRANSPORTING ATPASE; 1.
DR PANTHER; PTHR42861:SF29; SECRETORY PATHWAY CALCIUM ATPASE, ISOFORM G; 1.
DR Pfam; PF13246; Cation_ATPase; 1.
DR Pfam; PF00689; Cation_ATPase_C; 1.
DR Pfam; PF00690; Cation_ATPase_N; 1.
DR Pfam; PF00122; E1-E2_ATPase; 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 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 70..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 94..110
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 257..279
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 285..310
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 702..726
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 732..753
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 774..796
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 808..825
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 837..858
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 878..898
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 18..90
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 908 AA; 97561 MW; 49332614B8C5DFD4 CRC64;
MSESVVLKNG ECEQREPEWH VLQPAEARQE LKAKEPLSED EIRQRLARHG PNALPEARAK
GPWARLGRQL KNFLIYVLAG AAVITASLGH WVDAGVILAV VVIQTLVGFV QEGKAEQALS
AIRHMLAPKA RVVRSDGQHQ IDAANLVPGD TVLLEPGDRV PADLRLEKSH NLKIDEAILT
GESEAVDKST GSVAPDAPLG DQSGMAFSGT MVATGTGRGV VVRTGARTEI GRISGLLAQT
TTLKTPLLEQ MDRFARILSI IVIAAGIAIF VGGAAFSGLP FRELFMAVVG LTVAAIPEGL
PAILTITLAI GVRQMARRQA VVRRMPVIET LGAVSVICSD KTGTLTRNEM MVTRAVLSGV
QLEVTGEGYD LDGAVNAENG HPSDSTLLDE LARAAALCND AHVHHDSGRI RIAGDPMEAA
LSVFARKAGF DVDGSAADWP RKDEIPFDTE NRFMATLNHD HHGHSVIYLK GAPERILDMC
NSEVAESGET SELRRDFWER VITEMASDGL RVLALARTPA ERGIGELAIE DLEQGAELLG
LVGLLDPPRQ EAIRAIAECH DAGIRVKMIT GDHGITAGAI ARKLGLKNTW RVLTGKELDQ
LDDDQLRDLV GEVDVFARTS PEHKLRLVTA LQALHGVVAM TGDGVNDAPA LKRADVGIAM
GVKGSEAARE ASSVVLLDDN FASIAAAVRE GRTVYTNLKK GIAFMLPING GESISLVTAL
LLGLTLPISA LQILWVNMVS SVVLAMTLAF EPTEPDVMKH PPRGRNESLL RGFVVWRVVF
VSLLFLGGIF AAWYWAMHHH GDESTARTLA VNTLVAMEMF YLFAVRYLDS ASITLRGVLG
TPIVLLAVAA VIALQLLFTY TPWFNETFGT QALSVEMLAF AAASGVVVLV ILEIETVVRR
RLLRAGPG
//
