ID C1D7C9_LARHH Unreviewed; 817 AA.
AC C1D7C9;
DT 26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 26-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Probable cation transport P-type ATPase {ECO:0000313|EMBL:ACO74369.1};
GN OrderedLocusNames=LHK_01379 {ECO:0000313|EMBL:ACO74369.1};
OS Laribacter hongkongensis (strain HLHK9).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC Aquaspirillaceae; Laribacter.
OX NCBI_TaxID=557598 {ECO:0000313|EMBL:ACO74369.1, ECO:0000313|Proteomes:UP000002010};
RN [1] {ECO:0000313|EMBL:ACO74369.1, ECO:0000313|Proteomes:UP000002010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLHK9 {ECO:0000313|EMBL:ACO74369.1,
RC ECO:0000313|Proteomes:UP000002010};
RX PubMed=19283063; DOI=10.1371/journal.pgen.1000416;
RA Woo P.C., Lau S.K., Tse H., Teng J.L., Curreem S.O., Tsang A.K., Fan R.Y.,
RA Wong G.K., Huang Y., Loman N.J., Snyder L.A., Cai J.J., Huang J.D., Mak W.,
RA Pallen M.J., Lok S., Yuen K.Y.;
RT "The complete genome and proteome of Laribacter hongkongensis reveal
RT potential mechanisms for adaptations to different temperatures and
RT habitats.";
RL PLoS Genet. 5:E1000416-E1000416(2009).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362081}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000256|ARBA:ARBA00006024,
CC ECO:0000256|RuleBase:RU362081}.
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DR EMBL; CP001154; ACO74369.1; -; Genomic_DNA.
DR RefSeq; WP_012696855.1; NC_012559.1.
DR AlphaFoldDB; C1D7C9; -.
DR STRING; 557598.LHK_01379; -.
DR KEGG; lhk:LHK_01379; -.
DR eggNOG; COG2217; Bacteria.
DR eggNOG; COG2608; Bacteria.
DR HOGENOM; CLU_001771_0_3_4; -.
DR Proteomes; UP000002010; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR CDD; cd00371; HMA; 1.
DR CDD; cd02079; P-type_ATPase_HM; 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; 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; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR NCBIfam; TIGR01511; ATPase-IB1_Cu; 1.
DR NCBIfam; TIGR01512; ATPase-IB2_Cd; 1.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
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; PF00403; HMA; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
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; SSF55008; HMA, heavy metal-associated domain; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS50846; HMA_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Cell membrane {ECO:0000256|RuleBase:RU362081};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Reference proteome {ECO:0000313|Proteomes:UP000002010};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362081}.
FT TRANSMEM 179..199
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 211..232
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 244..266
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 272..291
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 429..449
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 455..475
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 762..780
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 91..157
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
SQ SEQUENCE 817 AA; 87775 MW; 7216A150E27C47E2 CRC64;
MTESCFHCGL PVPAGADFPV RYRQSPHATC CAGCQAVAQT IIDAGLDDYY QHRTEDARRA
EPLPADLLEQ IRLYDAPELQ QSFVHCEGDE REAALMLEGI TCAACVWLNE QHLKKLPGVL
SVDVNYSSLR ARVKWDDSRI HLSQILEAIA SIGYRAHPYD ADRQEKLAQQ ERKSQINRLW
VAGLSMMQVM MYVVPTYLAP DGDIDPQWLW MLHWASLVLT LPVVLYSAWP FYKGTWRDLR
SRRVGMDVPV TIGILTAFFA SCWALFRHID HGIYFDSVSM FVFLLLGGRY LEGIARRRAG
DAAERLVKLI PAFTHRLAGW PASREAHVAT VASVRSGDVL LIKPGDTLPV DGVVLEGESS
LNESLLTGES LPVRKQAGDA VIAGSVNTAS PLVIETSHVG ETTRLAGIVR LLDHAMAQKP
RLAVLADRVA GWFVAGLLLA AAAAFWLWYG IDPDRALWIM VAVLVISCPC ALSLATPAAL
TAAGGALADH GVLLARGTAL ESLARVTDAV FDKTGTLTTG VMQHNATSLL DPQLTEAEAL
TLARGLESGS EHPIARALLA TGESVPLATG ISNHVGAGVE GRIDGRRYRL GKPEFVAELT
GTPLAASEAF GGTDSIVALG SDTGWLALFA IGDRLRDEAR AMVDSLHARG IRVHLASGDS
QRVVDGVAGR LGIEDARANL TPEAKLALVT RLQAEGRTVL MVGDGVNDAP VLAQANVSAA
MGQGADVARL SGDIVLIGEG LTPLLPALTI ARRTRTIIRE NLAWAVGYNV VALPLAFMGW
VTPWLASLGM AASSLLVVGN ALRLSRQPAS RTVRPKD
//
