ID A0A0E3ZBE6_9FUSO Unreviewed; 871 AA.
AC A0A0E3ZBE6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 28-JAN-2026, entry version 45.
DE SubName: Full=ATPase {ECO:0000313|EMBL:AKC95440.1};
GN ORFNames=VC03_02650 {ECO:0000313|EMBL:AKC95440.1};
OS Sneathia vaginalis.
OC Bacteria; Fusobacteriati; Fusobacteriota; Fusobacteriia; Fusobacteriales;
OC Leptotrichiaceae; Sneathia.
OX NCBI_TaxID=187101 {ECO:0000313|EMBL:AKC95440.1, ECO:0000313|Proteomes:UP000033103};
RN [1] {ECO:0000313|EMBL:AKC95440.1, ECO:0000313|Proteomes:UP000033103}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SN35 {ECO:0000313|EMBL:AKC95440.1,
RC ECO:0000313|Proteomes:UP000033103};
RX PubMed=23281612;
RG Vaginal Microbiome Consortium (additional members);
RA Harwich M.D.Jr., Serrano M.G., Fettweis J.M., Alves J.M., Reimers M.A.,
RA Buck G.A., Jefferson K.K.;
RT "Genomic sequence analysis and characterization of Sneathia amnii sp.
RT nov.";
RL BMC Genomics 13:S4-S4(2012).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IIA subfamily. {ECO:0000256|ARBA:ARBA00005675}.
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DR EMBL; CP011280; AKC95440.1; -; Genomic_DNA.
DR RefSeq; WP_046328546.1; NZ_CP011280.1.
DR AlphaFoldDB; A0A0E3ZBE6; -.
DR STRING; 187101.VC03_02650; -.
DR KEGG; sns:VC03_02650; -.
DR PATRIC; fig|1069640.6.peg.510; -.
DR HOGENOM; CLU_002360_3_0_0; -.
DR OrthoDB; 9760364at2; -.
DR Proteomes; UP000033103; Chromosome.
DR GO; GO:0005886; C:plasma 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:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:UniProtKB-ARBA.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0046873; F:metal ion transmembrane transporter activity; IEA:UniProtKB-ARBA.
DR GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProtKB-ARBA.
DR GO; GO:0140352; P:export from cell; IEA:UniProtKB-ARBA.
DR GO; GO:0098662; P:inorganic cation transmembrane transport; IEA:UniProtKB-ARBA.
DR FunFam; 2.70.150.10:FF:000016; Calcium-transporting P-type ATPase putative; 1.
DR FunFam; 3.40.50.1000:FF:000028; Calcium-transporting P-type ATPase, putative; 1.
DR FunFam; 3.40.50.1000:FF:000001; Phospholipid-transporting ATPase IC; 1.
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; IPR059000; ATPase_P-type_domA.
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 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; SFLDG00002; C1.7:_P-type_atpase_like; 1.
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 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000033103};
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 59..75
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 81..100
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 244..263
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 275..299
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 656..677
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 689..708
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 729..752
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 772..791
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 812..832
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 844..864
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"
FT COILED 377..404
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 871 AA; 95970 MW; 02EA0EBBBD2022D5 CRC64;
MKYFNLDKNK CLEELVTNEN TGLTSDEAKL RLEKYGYNKL EEEKKKSILK LLFEQINDVM
IYVLLVSAVI TVVVNKEITD AVIILIVVLI NAVVGVVQEL KAEKSLNALK EMTSPKAVVL
RDSKLVEIES KYLVKGDIVL LEAGRVIPAD LRLIETMSLK IDESSFTGES VPAEKNADDI
LSENTQLADI TNMAFMSTLV SYGRAKGVVV KTGTDTQIGH IAKLLQVKEE QTPLQKKMNK
LGAYLGYIAI IICILIFVIG TIQGRNIVDM LITSISLAVA AIPEGLVAII SIVLALGVTR
MSKKNAIIKK MPAVETLGSV NYICSDKTGT LTQNKMTVVD TFTFDNSEDM LIKSMVLSSD
ATIIDGKELG DPTEVALIAY GIKNEKIKEE LEKEEKRIDE FSFDSDRKMA STLNTVDKGY
VVYVKGALDS LLKVSTKVLI NGREEELTED IKERIVNKSN EMSDKALRVL ASGYKKTDKK
IPASDFEKDI VLVGIVGMID PPRLEVKDSI NKAKKAGINI VMITGDHKNT AFAIAKELGI
ASNIDECIMG EKLDEYTDEQ MKEIVSKYKV YSRVSPLHKV RIVKALKSLG NIVSMTGDGV
NDAPSLKIAD IGVSMGITGT DVAKGASDMI LTDDNFTTIV TAISEGRNIY NNIKKAIIFL
LSCNLGEVTS IFVATILRWP LPLIATQLLW INLITDTLPA LALGVDPAST DVMCEKPRPQ
NEHFFSHGAL LRTIVGGMSI GILTLLAFYI GLKEKGIDLN TLSDINSIPY SHLAYARTMS
FIVLTISQLC YAFTMRSDRE SIIKVGIFKN KYLNISLIVG IVLQIALTEI PFLAEAFCVT
NLNFFDFDIV VLFVIIPLIL NEIIKKVQKE R
//
