ID A0A0U1QNR5_9BACL Unreviewed; 885 AA.
AC A0A0U1QNR5;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 29.
DE SubName: Full=ATPase {ECO:0000313|EMBL:KLI02266.1};
GN ORFNames=SINU_08995 {ECO:0000313|EMBL:KLI02266.1};
OS Sporolactobacillus inulinus CASD.
OC Bacteria; Bacillota; Bacilli; Bacillales; Sporolactobacillaceae;
OC Sporolactobacillus.
OX NCBI_TaxID=1069536 {ECO:0000313|EMBL:KLI02266.1, ECO:0000313|Proteomes:UP000035553};
RN [1] {ECO:0000313|EMBL:KLI02266.1, ECO:0000313|Proteomes:UP000035553}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CASD {ECO:0000313|EMBL:KLI02266.1,
RC ECO:0000313|Proteomes:UP000035553};
RX PubMed=21952540; DOI=10.1128/JB.05934-11;
RA Yu B., Su F., Wang L., Xu K., Zhao B., Xu P.;
RT "Draft genome sequence of Sporolactobacillus inulinus strain CASD, an
RT efficient D-lactic acid-producing bacterium with high-concentration lactate
RT tolerance capability.";
RL J. Bacteriol. 193:5864-5865(2011).
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:KLI02266.1}.
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DR EMBL; AFVQ02000112; KLI02266.1; -; Genomic_DNA.
DR RefSeq; WP_010023986.1; NZ_AFVQ02000112.1.
DR AlphaFoldDB; A0A0U1QNR5; -.
DR STRING; 1069536.SINU_08995; -.
DR OrthoDB; 9813266at2; -.
DR Proteomes; UP000035553; 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 GO; GO:0006811; P:monoatomic ion transport; IEA:UniProtKB-KW.
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 Ion transport {ECO:0000256|ARBA:ARBA00023065};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000035553};
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}; Transport {ECO:0000256|ARBA:ARBA00022448}.
FT TRANSMEM 48..74
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 80..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 245..263
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 275..300
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 673..697
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 703..721
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 741..764
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 784..803
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 824..847
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 859..876
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 885 AA; 96191 MW; D7524BE52279622A CRC64;
MNWFSQNAEQ VLQELNVDPK QGLSDAEIQS RLEKYGENKL KGKKKKSLAA LFFAQLKDML
IYVLLGAAVI TLLIGEYADA IIILLVVLLN AVIGVFQEFK AEKAIEALQK MTTPRALVRR
GGDVVEIDSK NIVPGDIVVL DAGRYIPADL RLTESANLQI EESALTGESV PSEKNAARLF
EDPKTPLGDL ANMAFMSTLV TYGRAEGVVV GTGMNTEIGK IAKGLDETQT DLTPLQKRLA
GLGKTLGYLA IGICVLIFII ALIQRRDLFE MFLTAISLAV AAIPEGLPAI VAIVLALGVT
RMSKINAIVK RLPAVETLGS VNIICSDKTG TLTQNKMTVL HLYTHRKFLD VPSEGTATAA
ESTQKKLIQT MVLCNDATLD DGEGTGDPTE IALVVLGNKY HFPKRELEAA HERVAERPFD
SDRKLMSTVN KEGDHYRVHT KGAFDSILKI ATHALVNGEK VPLTDDLKAD FLRAAEEMSD
QALRVLGAAY KDSDEVVEPD QMENDLTILG LVGMIDPPRL EVKDAIRQAK EAGITPVMIT
GDHQHTAAAI AMQLGMAESL DQSISGSQLD AMSDDELKQK INHYRVFSRV SPEHKVKIVN
AFRSHGNIVS MTGDGVNDAP SLKNADIGVA MGITGTDVSK GASDMILTDD NFTTIVAAIR
EGRNIYNNIK KSVVFLLSCN LGEIVAILAS VLFFWPMPLL PTQILWINLI TDTFPAIALG
VDPGDKDVMK KKPRDAKESF FAGGAAFRAI IGGLLIGILT LVAFYFGLSE HGYQLWSGSI
PEDVLTYAET MAFVVLAVSQ LFYSLSMRSA THSILHVGLF SNKYLIGAII LGIVLQFAVI
SIPILAGAFH VQMLTLRDWI IVIAFALVPL VINELIKRFT RSANN
//
