ID A9DQ30_9FLAO Unreviewed; 790 AA.
AC A9DQ30;
DT 05-FEB-2008, integrated into UniProtKB/TrEMBL.
DT 05-FEB-2008, sequence version 1.
DT 27-MAR-2024, entry version 92.
DE SubName: Full=Cu(I)-translocating P-type ATPase {ECO:0000313|EMBL:EDP96559.1};
GN ORFNames=KAOT1_15388 {ECO:0000313|EMBL:EDP96559.1};
OS Kordia algicida OT-1.
OC Bacteria; Bacteroidota; Flavobacteriia; Flavobacteriales;
OC Flavobacteriaceae; Kordia.
OX NCBI_TaxID=391587 {ECO:0000313|EMBL:EDP96559.1, ECO:0000313|Proteomes:UP000002945};
RN [1] {ECO:0000313|EMBL:EDP96559.1, ECO:0000313|Proteomes:UP000002945}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OT-1 {ECO:0000313|EMBL:EDP96559.1,
RC ECO:0000313|Proteomes:UP000002945};
RX PubMed=21622754; DOI=10.1128/JB.05241-11;
RA Lee H.S., Kang S.G., Kwon K.K., Lee J.H., Kim S.J.;
RT "Genome sequence of the algicidal bacterium Kordia algicida OT-1.";
RL J. Bacteriol. 193:4031-4032(2011).
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:EDP96559.1}.
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DR EMBL; ABIB01000003; EDP96559.1; -; Genomic_DNA.
DR RefSeq; WP_007095615.1; NZ_DS544873.1.
DR AlphaFoldDB; A9DQ30; -.
DR STRING; 391587.KAOT1_15388; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_0_3_10; -.
DR OrthoDB; 1521937at2; -.
DR Proteomes; UP000002945; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd00371; HMA; 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; IPR008250; ATPase_P-typ_transduc_dom_A_sf.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR001757; P_typ_ATPase.
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; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00943; CUATPASE.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF56784; HAD-like; 1.
DR SUPFAM; SSF55008; HMA, heavy metal-associated domain; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 4: Predicted;
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000002945};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 167..190
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 202..221
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 233..251
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 257..278
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 419..437
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 443..466
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 734..754
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 760..785
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 5..57
FT /note="Putative metal-binding"
FT /evidence="ECO:0000259|Pfam:PF12156"
SQ SEQUENCE 790 AA; 88332 MW; 40B79B2033575AB6 CRC64;
MSETTCFHCG DTCKEEIIQL EEKSFCCFGC KTVYELFSEN DLACYYDLQA APGAIPKEIA
GKYDFLSQQN IIDKLLEFND DTIQIVTLYI PHIHCSSCIW ILENLHKLNP EITASQVNFG
KKTVRITYNA TTFSLKEVVL LLSKIGYEPY ISLEDYSAGK NKINRTLIYK LGIAGFAFGN
VMFLSFPEYF QVSGFWIEQY KILFRWLMFA FSLPVVFYAA QDYFISAYKG LRAKLLNIDV
PIALGILVLF IRSTVEIIFD FGSGFFDSLT GLVFFLLLGK FFQQKTYSFL SFERDYKSYF
PIAITKISNG KETPIQVYDI EKGDRLLIRN EELIPVDGIL INGIAAIDYS FVTGESETVQ
KQSGDKVFAG GKQTSGIIEI EAIKSVEQSY LTQLWSNDVF EKNKEEGFTT VTNAISKHFT
VTVLSIAVVA TIFWLMVDAS KAMNVFTAVL IIACPCAIAL AAPFTFGNLL RIFGKLKFYV
KNASVLEQLS SINTIIFDKT GTITSNQKST ASYDGTQLTT AETTLLKSTL RGSNHPLSRT
LYNILEEQNI VTLDHFEEHI GKGMTASYHN DHIKVGAAKF VGYTDDATVL NTTVHISTNN
TYKGKYTFYN KYRKGLSKLF NNLKKQYDLA ILSGDNEGEL ENLKKLLPSK TKLIFNQTPN
DKLEYIQYHQ AEGAKVLMVG DGLNDAGALA QSNIGIALSE NVNVFSPACD AILDASKFNQ
LDQYIKASKT AIKIIKWSFV LSFIYNSIGL YFAITGQLAP VIAAILMPLS SISIVVFTTI
CTSILGRKLK
//
