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Database: UniProt
Entry: K2B4L4_9BACT
LinkDB: K2B4L4_9BACT
Original site: K2B4L4_9BACT 
ID   K2B4L4_9BACT            Unreviewed;       930 AA.
AC   K2B4L4;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 43.
DE   RecName: Full=Cation-transporting P-type ATPase N-terminal domain-containing protein {ECO:0000259|SMART:SM00831};
GN   ORFNames=ACD_47C00310G0001 {ECO:0000313|EMBL:EKD69017.1};
OS   uncultured bacterium.
OC   Bacteria; environmental samples.
OX   NCBI_TaxID=77133 {ECO:0000313|EMBL:EKD69017.1};
RN   [1] {ECO:0000313|EMBL:EKD69017.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=23019650; DOI=10.1126/science.1224041;
RA   Wrighton K.C., Thomas B.C., Sharon I., Miller C.S., Castelle C.J.,
RA   VerBerkmoes N.C., Wilkins M.J., Hettich R.L., Lipton M.S., Williams K.H.,
RA   Long P.E., Banfield J.F.;
RT   "Fermentation, hydrogen, and sulfur metabolism in multiple uncultivated
RT   bacterial phyla.";
RL   Science 337:1661-1665(2012).
CC   -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC       pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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:EKD69017.1}.
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DR   EMBL; AMFJ01020462; EKD69017.1; -; Genomic_DNA.
DR   AlphaFoldDB; K2B4L4; -.
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   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:SF156; CALCIUM-TRANSPORTING ATPASE; 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; PF00702; Hydrolase; 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        51..76
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        88..110
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        259..277
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        283..312
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        718..740
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        746..767
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        788..808
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        828..849
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        861..881
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        901..918
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          5..79
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   930 AA;  102874 MW;  048B9F372908804D CRC64;
     MQKHFWHSMS YQQVREYWLT DTENGLDKKA AEERLLKLGH NKLKEKPKKS LLIVFIEQLN
     NFIIWTLIVA AVVSAVTGHM ENPDGGFFVK YGDFVAIMLI VLLNGFLGLF QELKADAAME
     ALKKMSARHA KVVRNKELMT IDAEELVCGD IIVLEEGDII PADIKVFETH RFSTSEAALT
     GESVAVMKQN VEMIEKEAPL SERVNMVYMG TTVATGRARG IVVNTGMYTE LGKIAKSIDD
     ISDEDTPLQK KLNEFGHQIV YLCILVSVVI FVIGILRDKE GSLMLYFMTA VSLAVAAIPE
     GLPAITTIVM ALGTQRMANK NAVVRKLASV ETLGCTTVIC TDKTGTLTQN KMVLKKIYCD
     GDYIDVTGEG YEVKGQLIKG KNVVSTDETM KAGGALGSII DSGILCNNAR IKPNEKDPNI
     VDFVGDPTEV AFLVAAKKAA VDIDAKLLEY SFFDEVPFSS ERKMMSKVYK KADEYMIYTK
     GATEMVMARA KHILENGKVI PLDDKKRRQL LEINDKMASM AFRVLGLAGK SIAANSVDTE
     NENDANLFEK ELIFYGLAGI MDPPKIEVKD SIELCRRAGI STVMITGDHK GTASAIARDL
     GILTEGKLSL SGPELDKIDD EKLAEICSNT AVFARVTAEH KLRIVRAFKN RGEIVAMTGD
     GINDAPAIKE ASIGIAMGIA GTDVTKSAAD MVLADDNFST IVAAVEEGRV IYNNIKKFIY
     FLFSSNMGLV FAIFFTVIFG WKQPVFPLQI LWINLITNGL PALALGVDPA ERDLMSKMPR
     STKDKIIGPW EFWMIIINGF IMGIAALYAF YYEYYVIKEV GLSAQQQYYE ACTMAFAILA
     LSPIIHAFSC RSKSISAFRG IFENIWIWLS ALVAVVLQLI AVHYKPLQSA FKTIDISLEK
     WFVIIGLSIL PLLFMEFYKI GLKIKGKKVE
//
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