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Database: UniProt
Entry: Q2S799_HAHCH
LinkDB: Q2S799_HAHCH
Original site: Q2S799_HAHCH 
ID   Q2S799_HAHCH            Unreviewed;       905 AA.
AC   Q2S799;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 119.
DE   SubName: Full=Cation transport ATPase {ECO:0000313|EMBL:ABC33475.1};
GN   OrderedLocusNames=HCH_06855 {ECO:0000313|EMBL:ABC33475.1};
OS   Hahella chejuensis (strain KCTC 2396).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC   Hahellaceae; Hahella.
OX   NCBI_TaxID=349521 {ECO:0000313|EMBL:ABC33475.1, ECO:0000313|Proteomes:UP000000238};
RN   [1] {ECO:0000313|EMBL:ABC33475.1, ECO:0000313|Proteomes:UP000000238}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KCTC 2396 {ECO:0000313|EMBL:ABC33475.1,
RC   ECO:0000313|Proteomes:UP000000238};
RX   PubMed=16352867; DOI=10.1093/nar/gki1016;
RA   Jeong H., Yim J.H., Lee C., Choi S.-H., Park Y.K., Yoon S.H., Hur C.-G.,
RA   Kang H.-Y., Kim D., Lee H.H., Park K.H., Park S.-H., Park H.-S., Lee H.K.,
RA   Oh T.K., Kim J.F.;
RT   "Genomic blueprint of Hahella chejuensis, a marine microbe producing an
RT   algicidal agent.";
RL   Nucleic Acids Res. 33:7066-7073(2005).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR   EMBL; CP000155; ABC33475.1; -; Genomic_DNA.
DR   RefSeq; WP_011400525.1; NC_007645.1.
DR   AlphaFoldDB; Q2S799; -.
DR   STRING; 349521.HCH_06855; -.
DR   KEGG; hch:HCH_06855; -.
DR   eggNOG; COG0474; Bacteria.
DR   HOGENOM; CLU_002360_3_0_6; -.
DR   OrthoDB; 9814270at2; -.
DR   Proteomes; UP000000238; Chromosome.
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   GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
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; 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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000238};
KW   Translocase {ECO:0000256|ARBA:ARBA00022967};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT   DOMAIN          12..85
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   905 AA;  97994 MW;  EF4775D2B865B95E CRC64;
     MQNTERRFSE VKWHSVSIDS TLEQLQTSTT GLTQADASLR LAAYGPNRLP QIARRNSLIR
     FLQHFHNILI YVLIGSAVVT AVLSHWVDSG VILAVVIANA IIGYIQEGKA EQAMDAIRHM
     LAPRANVIRD GERITIDGEQ LAPGDIVLLE AGDKVPADLK LLTAHSLLVQ EAILTGESVP
     VEKFTQAVDE GAPLGDRSCM AYSGTLVACG QGKGVVVATG AGTEIGQISG LLSEVETLTT
     PLVEQMGVFA KWLTMMILFI AAVLLVFGYF VSHYDFTEMF MAVVGLSVAA IPEGLPAVLT
     ITLAIGVQAM ARRNAIVRRL PAIETLGSVS VICTDKTGTL TRNEMMVASV ITNQHFFTLE
     GSGYAPSGAL KLDEAYVSPS EHTILEELAR AAALCNDAAL REHSGVWVVE GDPMEGALLA
     FSEKVDVDSR REQINWTRTD SIPFDARHRF MATLNHDHDG HACIFVKGAP EQVLAMCTDQ
     MGANGAVEEL DIAYWTKHAE RIAALGQRVL AFADKTVALQ HTVLEHSDVK GSLTMLGMVG
     MIDPPRAEAI TAITECRGAG IRVKMITGDH SQTAAAIGEQ IGLENTATVL TGTEIDALDD
     LALRQAVLGC DIFARTSPEH KLRLVMALQS HGMTVAMTGD GVNDAPALKR ADAGIAMGRK
     GSEAAKEAAE LVLADDNFAS IVAAVREGRT VYDNFKKVIS WTLPTNAGEA MTIVVALLLG
     MTLPVTPIQI LWINLITAIT LGVALAFEPT EKNTMRRPPR ARHEPLLTGE LVWHVVLVSI
     LFLCGVFGIY HYAIDRGYSV ELARTIALNT LVVMEIFHLF FIRNIYSTSL TWQAVRGTKV
     MWVVIVVITV AQFAITYLPP LQAVFATEAV PLLDGLLIVG VGTALFAIIE LEKQMRLTYR
     RMREV
//
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