ID E7GMR1_CLOSY Unreviewed; 828 AA.
AC E7GMR1;
DT 05-APR-2011, integrated into UniProtKB/TrEMBL.
DT 05-APR-2011, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE SubName: Full=ATPase {ECO:0000313|EMBL:EGA94003.1};
GN ORFNames=HMPREF9474_02206 {ECO:0000313|EMBL:EGA94003.1};
OS [Clostridium] symbiosum WAL-14163.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae.
OX NCBI_TaxID=742740 {ECO:0000313|EMBL:EGA94003.1, ECO:0000313|Proteomes:UP000002970};
RN [1] {ECO:0000313|EMBL:EGA94003.1, ECO:0000313|Proteomes:UP000002970}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WAL-14163 {ECO:0000313|EMBL:EGA94003.1,
RC ECO:0000313|Proteomes:UP000002970};
RA Earl A., Ward D., Feldgarden M., Gevers D., Finegold S.M., Summanen P.H.,
RA Molitoris D.R., Vaisanen M.L., Daigneault M., Young S.K., Zeng Q.,
RA 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 Heilman E., Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P.,
RA Mehta T., Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
RA Roberts A., Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S.,
RA White J., Yandava C., Nusbaum C., Birren B.;
RT "The Genome Sequence of Clostridium symbiosum strain WAL-14163.";
RL Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
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:EGA94003.1}.
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DR EMBL; ADLQ01000049; EGA94003.1; -; Genomic_DNA.
DR RefSeq; WP_003500360.1; NZ_GL834309.1.
DR AlphaFoldDB; E7GMR1; -.
DR STRING; 1512.GCA_900049235_02381; -.
DR eggNOG; COG0474; Bacteria.
DR HOGENOM; CLU_002360_3_3_9; -.
DR Proteomes; UP000002970; 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 Gene3D; 3.40.1110.10; Calcium-transporting ATPase, cytoplasmic domain N; 2.
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; 2.
DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 2.
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; 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 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:UP000002970};
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 40..62
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 68..84
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 228..248
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 260..284
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 629..646
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 700..726
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 738..758
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 779..796
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 802..824
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 1..64
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 828 AA; 89490 MW; A39B76151A2B0B94 CRC64;
MAGTDRAQAG LTSAQAAKLL EQYGKNELTS GKKGKFLRKA LHILGEPMFL LLFFAAVVYF
ILGEPKDGAV MFIFITGVVG IDVMQEWKTD RTLAALQKMT APRVKALRDG REQVIPGEEL
VPGDVFFLCE GDRVPADAVI LTCSDFCVDE SMLTGESAGV WKTAKKDGPE GTAGDTCYAG
TLVIQGNAAL LTERTGITTE YGKIGLNVAE APEEDTPLQR QTAGLVKVCA AIAAVLFLLA
GIFTYFSLSG LGEAERMTRS ILAGVTLAMA LIPEEFPVVL TVFLSMGAWR LAKKHSLVRR
LPSVETLGAV SVLCCDKTGT LTMNKMSVGR TWAADKDERT LLMLMGMGCE PEAYDPMEKA
MLQYCGEQGI SEEEIFGGSL VKEYAFTNGK KMMGHVWLRD GRLTAAVKGS PEKVAAICRS
GEEIDEALQI GKDMAAEGLR VIAVASAEED ADFFEIPEEP EGWKLRLCGL IGLSDPPRPG
ISEDIRVCRN AGIRVIMITG DNGVTASSVA RRIGIDGGKV VTGDEMEQMT DEELGKAAAE
TSVFSRVVPE HKMRIIKALQ KNGETVAMTG DGVNDAPALK YADIGIAMGL RGSEVSREAA
DLILLDDNFT TIVETVKDGR RIYDNIRRAV GYIFTIHLPI ILASLLPPLF GTPPSAQMLL
PVHIVLLELI IDPTCSIVLE RQPAEPDIMK RKPEESRGRL LTPQILAKSV LQGIAIAIAS
FAVYFFHLKN CPDRAVVSRS MGLMVIMISN LFLVLVNCSD SESALRSLFR LLKDRGMQAA
FAAMVLMPAV IFYSPVNTFL KLAPLSAGQL AVAVLVSAAA VFWYEVIK
//