ID Q98C24_RHILO Unreviewed; 839 AA.
AC Q98C24;
DT 01-OCT-2001, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2001, sequence version 1.
DT 27-MAR-2024, entry version 163.
DE SubName: Full=Cation transporting P-type ATPase {ECO:0000313|EMBL:BAB51797.1};
GN OrderedLocusNames=mlr5325 {ECO:0000313|EMBL:BAB51797.1};
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835 {ECO:0000313|EMBL:BAB51797.1, ECO:0000313|Proteomes:UP000000552};
RN [1] {ECO:0000313|EMBL:BAB51797.1, ECO:0000313|Proteomes:UP000000552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099
RC {ECO:0000313|Proteomes:UP000000552};
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|RuleBase:RU362081}.
CC -!- SIMILARITY: Belongs to the cation transport ATPase (P-type) (TC 3.A.3)
CC family. Type IB subfamily. {ECO:0000256|ARBA:ARBA00006024,
CC ECO:0000256|RuleBase:RU362081}.
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DR EMBL; BA000012; BAB51797.1; -; Genomic_DNA.
DR RefSeq; WP_010913136.1; NC_002678.2.
DR AlphaFoldDB; Q98C24; -.
DR KEGG; mlo:mlr5325; -.
DR PATRIC; fig|266835.9.peg.4223; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_11_3_5; -.
DR Proteomes; UP000000552; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0019829; F:ATPase-coupled monoatomic cation transmembrane transporter activity; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR CDD; cd02094; P-type_ATPase_Cu-like; 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; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR Gene3D; 1.10.620.20; Ribonucleotide Reductase, subunit A; 2.
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; IPR009078; Ferritin-like_SF.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR045800; HMBD.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR InterPro; IPR012348; RNR-like.
DR InterPro; IPR011017; TRASH_dom.
DR InterPro; IPR007029; YHS_dom.
DR NCBIfam; TIGR01511; ATPase-IB1_Cu; 1.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 1.
DR PANTHER; PTHR43520; ATP7, ISOFORM B; 1.
DR PANTHER; PTHR43520:SF8; COPPER-TRANSPORTING ATPASE 2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF19335; HMBD; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR Pfam; PF04945; YHS; 2.
DR PRINTS; PR00119; CATATPASE.
DR PRINTS; PR00943; CUATPASE.
DR SFLD; SFLDG00002; C1.7:_P-type_atpase_like; 1.
DR SFLD; SFLDF00027; p-type_atpase; 1.
DR SMART; SM00746; TRASH; 2.
DR SUPFAM; SSF81653; Calcium ATPase, transduction domain A; 1.
DR SUPFAM; SSF81665; Calcium ATPase, transmembrane domain M; 1.
DR SUPFAM; SSF47240; Ferritin-like; 2.
DR SUPFAM; SSF56784; HAD-like; 1.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU362081};
KW Cell membrane {ECO:0000256|RuleBase:RU362081};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|RuleBase:RU362081};
KW Metal-binding {ECO:0000256|RuleBase:RU362081};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW Translocase {ECO:0000256|ARBA:ARBA00022967};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692,
KW ECO:0000256|RuleBase:RU362081};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|RuleBase:RU362081}.
FT TRANSMEM 184..205
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 217..236
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 248..268
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 288..306
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 441..463
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 469..492
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 785..804
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 810..832
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 35..73
FT /note="TRASH"
FT /evidence="ECO:0000259|SMART:SM00746"
FT DOMAIN 81..119
FT /note="TRASH"
FT /evidence="ECO:0000259|SMART:SM00746"
SQ SEQUENCE 839 AA; 87386 MW; B960F5094B64312F CRC64;
MTHPDHDHRG EHHAHGAHGS CCAPKGADAA AVLRDPVCGM TVDPAAGKPT SEHGGRLYHF
CSERCRSKFQ AEPEQYLTAT DPVCGMSVDR ATARHLVRHE GQGFYFCSAG CKAKFEAAPQ
TYLGDRPAPP PAPKGTQYTC PMHPEIIRDK PGSCPICGMA LEPMGVPSGD EGPNPELVDF
TRRFWVSAVL SIPLLIVAMA PMIGVSFESW VDDRTKVWIE LVLASPVVLW AAFPFFRRGW
ESVLNRSPNM WTLISLGVGA AYLYSVVATL FPDIFPHQFR GHGGAVPVYF EAAAVIVALV
FLGQVLELRA REKTGSAIRA LLDLAPKTAR RMAEDGSETD VPLDSVKAGD RLRIRPGDAV
PVDGTVLEGR SSIDESMITG EPLPVEKAEG DALTGGTLNR QGSLIMRAER IGAETTLARI
VELVAKAQRS RAPIQGLADR VSFYFVPAVV LVAIAAFIAW AIFGPEPSLI FAIVSAVSVL
IIACPCALGL ATPMSIMTAT GRGAHAGVLI KEAAALERFA SVDTLIVDKT GTLTEGRPKL
TDVVAANGFS EDELLGLAAS LEKGSEHPLA EAIVEGAAAR GATVTDAGDF EAVTGKGVSG
TVSGKAVALG NAAMMGDLGV DVSAVSASAE ALQGDGKTAM FVAVGGTLAG IVAVADPIKA
TTAEAIRALH DSGLRIIMAT GDNERTANAI AKSLGIDEVR AGLLPEQKAA LVEELRGRGA
GVAMAGDGVN DAPALASADV GIAMGTGADV AVESAGITLV KGDLNGIVRA RTLAQATIGN
IRQNLFFAFL YNVLGVPVAA GVLYPLTGML LSPMLAAAAM SLSSVSVIAN ALRLRTLKL
//
