ID A0A0R1GYK0_9LACO Unreviewed; 916 AA.
AC A0A0R1GYK0;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE SubName: Full=Cation transport ATPase {ECO:0000313|EMBL:KRK39366.1};
GN ORFNames=FD07_GL001161 {ECO:0000313|EMBL:KRK39366.1};
OS Levilactobacillus parabrevis ATCC 53295.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC Levilactobacillus.
OX NCBI_TaxID=1267003 {ECO:0000313|EMBL:KRK39366.1, ECO:0000313|Proteomes:UP000051176};
RN [1] {ECO:0000313|EMBL:KRK39366.1, ECO:0000313|Proteomes:UP000051176}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 53295 {ECO:0000313|EMBL:KRK39366.1,
RC ECO:0000313|Proteomes:UP000051176};
RX PubMed=26415554; DOI=10.1038/ncomms9322;
RA Sun Z., Harris H.M., McCann A., Guo C., Argimon S., Zhang W., Yang X.,
RA Jeffery I.B., Cooney J.C., Kagawa T.F., Liu W., Song Y., Salvetti E.,
RA Wrobel A., Rasinkangas P., Parkhill J., Rea M.C., O'Sullivan O., Ritari J.,
RA Douillard F.P., Paul Ross R., Yang R., Briner A.E., Felis G.E.,
RA de Vos W.M., Barrangou R., Klaenhammer T.R., Caufield P.W., Cui Y.,
RA Zhang H., O'Toole P.W.;
RT "Expanding the biotechnology potential of lactobacilli through comparative
RT genomics of 213 strains and associated genera.";
RL Nat. Commun. 6:8322-8322(2015).
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:KRK39366.1}.
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DR EMBL; AZCZ01000003; KRK39366.1; -; Genomic_DNA.
DR RefSeq; WP_020088451.1; NZ_KB911367.1.
DR AlphaFoldDB; A0A0R1GYK0; -.
DR STRING; 357278.IV61_GL000075; -.
DR PATRIC; fig|1267003.4.peg.1230; -.
DR eggNOG; COG0474; Bacteria.
DR OrthoDB; 9760364at2; -.
DR Proteomes; UP000051176; 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; 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; 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; SFLDG00002; C1.7:_P-type_atpase_like; 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 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 80..98
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 104..121
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 262..283
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 705..725
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 737..756
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 776..796
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 802..826
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 846..864
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 876..897
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 27..100
FT /note="Cation-transporting P-type ATPase N-terminal"
FT /evidence="ECO:0000259|SMART:SM00831"
FT REGION 1..28
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..28
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 916 AA; 99651 MW; 6BC638F1176F9981 CRC64;
MAQDPEATVT PTEVAESTDP GPSQELPLWQ RTTESLLADY ATDRDDGLST GEAQQRLRTN
GPNELTVKKQ SNLLRFLKQF NNSIIYILAG AALLTFFMHH YSDSIVIGLV IIANAFIGYF
QEKSADNALD RIKALLVNEA VVIRDGQKIN LPARELVTGD IVQLEAGDTV PADLRLIDAD
NLKIQESALT GETDSVLKGE DPLTAPDLPL AERSNQAFAS TAVTNGSGRG IVTVTGVDTE
IGHIQQNVAE VKQQRTPLMK NLNSLGLGLS IAILVVAALL FILGMITHVY SLPTLLIAVI
TMVVGSMPEG LPASTSVVLA MGTQAMTKQN VIVKTLPAVE TLGAVDIVNT DKTGTLTKNE
MTVTDVLTAA DTYTVSGIGY DATGQIENDE GQTVPWQHDA DLEWLVQIAG QTSDAEFHEE
DGQWVLTGEP TDGALTALYH KLVGTEPDPQ EIDSLPFDSA IRYSARLVDH DGQRVLLVKG
APQTLMRMMS EQGQPVDQAA WQTRLSQLTQ QGKRVVALGY QPVAADVTDV ANVTVGQNFH
LAGMAGIIDP PRPGVADAVK QLRYAGIKVK MITGDDPETA AAIAQQLNLS EKARAITGPE
LAQLSDEELA AKIDQYTVFA RTTPADKLRI VKAQQQRGHV VSMTGDGVND APALKQADIG
VAMGIRGTDV AKDSADMVLA DDDFTSILRA VREGRHVFDN IRKTIRFLLP TSFAEGLIVV
LSILMDQELP LFPTQLLWIN MVSALTIQFA FIFEPAESGI MKRGPRDVTR GILSKLDVFE
VTYVSLLISG LGMFAYDFLT NQGLSAVIGS TMTLNVIIFG KVFYLFNLQN DHPVLSKYFF
RNKMSFVIVA ILLVLQAGII YWPAMQSVFH TTSVNFFYGW WIPIIAGFVV LVVTEIAKAI
RHRIDNQTVA REQRNF
//
