ID A0A0S2W6W9_9FIRM Unreviewed; 877 AA.
AC A0A0S2W6W9;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Putative cation-transporting ATPase {ECO:0000313|EMBL:ALP95078.1};
GN ORFNames=IB211_02687c {ECO:0000313|EMBL:ALP95078.1};
OS Intestinimonas butyriciproducens.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Intestinimonas.
OX NCBI_TaxID=1297617 {ECO:0000313|EMBL:ALP95078.1, ECO:0000313|Proteomes:UP000064844};
RN [1] {ECO:0000313|EMBL:ALP95078.1, ECO:0000313|Proteomes:UP000064844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF211 {ECO:0000313|EMBL:ALP95078.1,
RC ECO:0000313|Proteomes:UP000064844};
RX PubMed=26620920; DOI=10.1038/ncomms10062;
RA Bui T.P., Ritari J., Boeren S., de Waard P., Plugge C.M., de Vos W.M.;
RT "Production of butyrate from lysine and the Amadori product fructoselysine
RT by a human gut commensal.";
RL Nat. Commun. 6:10062-10062(2015).
RN [2] {ECO:0000313|Proteomes:UP000064844}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AF211 {ECO:0000313|Proteomes:UP000064844};
RA de Vos W.M., Bui N.T.P., Plugge C.M., Ritari J.;
RT "A butyrogenic pathway from the amino acid lysine in a human gut
RT commensal.";
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; CP011307; ALP95078.1; -; Genomic_DNA.
DR RefSeq; WP_058118319.1; NZ_CP011307.1.
DR AlphaFoldDB; A0A0S2W6W9; -.
DR STRING; 1297617.IB211_02687c; -.
DR KEGG; ibu:IB211_02687c; -.
DR PATRIC; fig|1297617.4.peg.2764; -.
DR eggNOG; COG0474; Bacteria.
DR Proteomes; UP000064844; Chromosome.
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: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 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Reference proteome {ECO:0000313|Proteomes:UP000064844};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 4..77
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
SQ SEQUENCE 877 AA; 94440 MW; 5416C34D12C2778D CRC64;
MESSFFNRTV DETLSALGGT KAGLTSKEAA ERLQKHGKNA LAEGKKKSGL QVFLDQFKDL
LVVILIIAAL ISMVSDNVES TVVIFAVLIL NAVLGTVQHF KAEKSLESLK AMSSPSAKVL
RDGVRSVVPS AQVVPGDIVE LEAGDMVVAD GRILENFSLK VNESSLTGES EGVEKTSDVI
AAEKVALGDQ KNMVFSGSLV TYGRATVVVT GTGMDTELGK VAALMNRTQQ RKTPLQESLD
DFSKKLATAI LGICVVVFAL SLFHHMALLD SLMFAVALAV AAIPEALSSI ITIVQAMGTQ
KMARQNAIIK DLKAVETLGS VSVICSDKTG TLTQNRMTPQ KIYADGSLLE GDDLDLVNDV
QRLLLKAALL ASDATTNVED GTSIGDPTEV ALVMLGDRIG VDEELYRRHH PRLGELAFDS
DRKLMSTLHE IEGVPTLYTK GAIDVLLDRS RYVLTREGQV PMTPEWRERI SRINMELSME
GLRVLAFSYR ELPEVRALTL EDERDFTFIG LISMIDPPRP EAVQAVADAK RGGIRTIMIT
GDHKVTATAI ARQIGIFREG DEAVSGVELS DMSDHDLDER LERISVYARV SPEHKIRIVE
AWQRKGKIVS MTGDGVNDAP ALKAANIGVA MGITGTEVSK DAASMILADD NFATIVKAVV
NGRGVYTNIK NAINFLLSGN MAGILSVLFT SILGLSMPFA PVHLLFINLL TDSLPAIAIG
VEPARKGLLD QPPRDPNEPI LTRGLMLKIL AYGALIACAT MGAYFIGLNA DNGGAGLAMT
LAFSTLTLAR LFHGFNCRGI ESIFRLGLTT NRASLGAFAA GVVLLLAVLF LPGLNALFQV
SPFTMAQFGW VILLAFLPTV AIQIYKVIHD AVRRKNR
//
