ID B6BMJ2_SULGG Unreviewed; 902 AA.
AC B6BMJ2; H1FYS8;
DT 25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT 25-NOV-2008, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Cation-transporting P-type ATPase {ECO:0000313|EMBL:EHP30893.1};
GN ORFNames=SMGD1_2370 {ECO:0000313|EMBL:EHP30893.1};
OS Sulfurimonas gotlandica (strain DSM 19862 / JCM 16533 / GD1).
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Sulfurimonadaceae; Sulfurimonas.
OX NCBI_TaxID=929558 {ECO:0000313|EMBL:EHP30893.1, ECO:0000313|Proteomes:UP000006431};
RN [1] {ECO:0000313|EMBL:EHP30893.1, ECO:0000313|Proteomes:UP000006431}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GD1 {ECO:0000313|EMBL:EHP30893.1,
RC ECO:0000313|Proteomes:UP000006431};
RX PubMed=22203982; DOI=10.1073/pnas.1111262109;
RA Grote J., Schott T., Bruckner C.G., Glockner F.O., Jost G., Teeling H.,
RA Labrenz M., Jurgens K.;
RT "Genome and physiology of a model Epsilonproteobacterium responsible for
RT sulfide detoxification in marine oxygen depletion zones.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:506-510(2012).
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:EHP30893.1}.
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DR EMBL; AFRZ01000001; EHP30893.1; -; Genomic_DNA.
DR RefSeq; WP_008339262.1; NZ_DS995291.1.
DR AlphaFoldDB; B6BMJ2; -.
DR STRING; 929558.SMGD1_2370; -.
DR PATRIC; fig|929558.5.peg.2360; -.
DR eggNOG; COG0474; Bacteria.
DR HOGENOM; CLU_002360_3_3_7; -.
DR OrthoDB; 2490525at2; -.
DR Proteomes; UP000006431; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR CDD; cd02080; P-type_ATPase_cation; 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; 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; 2.
DR PANTHER; PTHR43294:SF22; P-TYPE ATPASE; 1.
DR PANTHER; PTHR43294; SODIUM/POTASSIUM-TRANSPORTING ATPASE SUBUNIT ALPHA; 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 Pfam; PF08282; Hydrolase_3; 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:UP000006431};
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 58..80
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 86..105
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 249..268
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 280..304
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 705..724
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 730..748
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 769..788
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 800..820
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 832..852
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 872..892
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 8..82
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 902 AA; 100023 MW; 3D3F3CF4CA323CE5 CRC64;
MQHLIGENWH SLESQKIVEL FESDVTDGLG SLSIKHREEF FGKNALKEKK QDSYLKKFFI
QFHNALIYIL LGASAVTAFL HEWVDSGVIF GVVIINVIIG FMQEVKAQEA IESLKQMMHT
EAVVIRDSKK ITIDSVDLVP GDIVMLESGS KVPADMRLIE IRDLKVDESM LTGESLAVFK
NISTHSENSI LGDRKNMTYS GTFVTYGRAK GIVVATSNHT ELGKIAHLIE NTTAMQTPLT
KKIAEFSKIL LYVILALAAF TFIVGVLRDK SAVETFMASV ALAVGAIPEG LPAAVTITLA
IGVSRMASKN AIIRKLAAVE TLGSVTTICS DKTGTLTQNK MTVTNIFCGN ESYEVTGNGY
EPKGHILKNG EQLASCNNNL NEVLKAGYLC NESYLVRKDG HYDISGDPTE GALIVSSIKC
GWDEHRLNKS YPRVDILPFE SDRQFMATIN KYVKNNQNII YIKGSIEVIL EICDFEFLNG
ESKVIDKKSI MKKVEEYASD GLRVLAIAEK LTDKEKIEES ELENEFIFLG LQAMMDPPRP
EAIKAVQESK GAGINIIMIT GDHALTAFSI AKMMYIVDND AKFEESVLVG NDLMKISDDE
LIKKVATVKV FARVEPEQKL RIVDALQARG EIVAMTGDGV NDAPALKQAD IGIAMGYGGT
EVAKEASDMI LSDDNFRSIA HAVKEGRIVF DNLIKFITWT LPTNLGEGLV IMVAIVLGLT
LPILPLQILW INMSTAIFLG LMLVFESGEG YIMKRAPRNP NTPILTKEII HQMLVVGVYM
LVASYGMFNY ALSNGHSIEY ARTIAVNIFV FIELFYLFNC KELQRSVFRT NVFSNKFLLL
GVVLMTLSQI AFTHTDFMND IFKSESLDLS TWIEIIVISF SVMFVVEIKR YIDSVIDKRS
SS
//
