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Database: UniProt
Entry: G5ICX0_9CLOT
LinkDB: G5ICX0_9CLOT
Original site: G5ICX0_9CLOT 
ID   G5ICX0_9CLOT            Unreviewed;       883 AA.
AC   G5ICX0;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   27-MAR-2024, entry version 51.
DE   RecName: Full=Cation-transporting P-type ATPase N-terminal domain-containing protein {ECO:0000259|SMART:SM00831};
GN   ORFNames=HMPREF9473_01305 {ECO:0000313|EMBL:EHI60741.1};
OS   Hungatella hathewayi WAL-18680.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae; Hungatella.
OX   NCBI_TaxID=742737 {ECO:0000313|EMBL:EHI60741.1, ECO:0000313|Proteomes:UP000005384};
RN   [1] {ECO:0000313|EMBL:EHI60741.1, ECO:0000313|Proteomes:UP000005384}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WAL-18680 {ECO:0000313|EMBL:EHI60741.1,
RC   ECO:0000313|Proteomes:UP000005384};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Finegold S.M., Summanen P.H.,
RA   Molitoris D.R., Song M., Daigneault M., Allen-Vercoe E., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Clostridium hathewayi WAL-18680.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
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:EHI60741.1}.
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DR   EMBL; ADLN01000012; EHI60741.1; -; Genomic_DNA.
DR   RefSeq; WP_006779289.1; NZ_JH379027.1.
DR   AlphaFoldDB; G5ICX0; -.
DR   PATRIC; fig|742737.3.peg.1314; -.
DR   HOGENOM; CLU_002360_3_3_9; -.
DR   OrthoDB; 9760364at2; -.
DR   Proteomes; UP000005384; Unassembled WGS sequence.
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   CDD; cd02089; P-type_ATPase_Ca_prok; 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; 3.
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   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:UP000005384};
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        60..79
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        85..101
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        253..274
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        286..309
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        675..697
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        703..720
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        741..767
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        787..806
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        818..839
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        851..870
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          2..76
FT                   /note="Cation-transporting P-type ATPase N-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00831"
SQ   SEQUENCE   883 AA;  95041 MW;  6B5FE864112FB230 CRC64;
     MKEYLKTGEE VLREQSVDAG QGLSEAEVAG RLSKHGKNKL VEAKKTPIWK RFLEQLADPM
     IIILIAAAAV SGVTAVYAGE SFADVIIILA VVIINAVLGV VQESKAEAAI AALQEIAAAT
     SKVIRGGHQL TVRSEELVPG DIIVLEAGDS VPADARIVEC ASMKIEEAAL TGESVPVLKT
     TDQLAAEENG KDVSLGDRKN MVYMGSSVAY GRGRAVVTAT GMDTEMGKIA DALTLAKDNA
     TPLQMKLAQL SKVLSFLVIG ICVIIFGVSL VRAYPDVSGE VMLDTFMVAV SLAVAAIPEG
     LAAVVTIVLS IGVTNMSKKA AIVRKLTAVE TLGCTQIICS DKTGTLTQNK MTVVEHTGQE
     EKLLAIAMSL CNDAGLDENH EAVGEPTEAA LVNYAWKAGL NKNRLVATYP RIGEAPFDSM
     RKMMSTVHRM EDGTVVQFTK GAPDEILKRC TQICLDGQAE ELTEDIRASI LKENKAMADK
     ALRVLGAAMR TWEEEPSDYG AEVLEQDLCF LGLTGMIDPV RPEVKPAIDE CRAAGIRPIM
     ITGDHKDTAV AIAMQLGIID DASQAITGSQ LDDISDEELE NEIERYSVYA RVQPEHKVRI
     VNAWQKRGKI TAMTGDGVND APSIKNADIG VGMGITGTDV TKNVADMVLA DDNFATIVSA
     VSEGRRIYDN IRKAIQFLLA SNLSEVLAIF FATLMGFTIL KPVHLLWINL ITDCFPALAL
     GMEKPEKDIM KRAPRDPKDG IFAGGVGINV ALQGIAVAVI TLAAYFIGHY IEAGVWEITN
     SADGMTMAFL TLSMTEIFHS FNMRSLHKSI LHTREQNGWL WLSMAASLIC TTAVIYVPVL
     ADAFGFEHIS LMEYGVSIGL AVCIIPVVEI SKVIQRNQKT FQE
//
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