ID A4Z1A1_BRASO Unreviewed; 764 AA.
AC A4Z1A1;
DT 29-MAY-2007, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2007, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE SubName: Full=Putative Cation-transporting ATPase {ECO:0000313|EMBL:CAL79927.1};
DE EC=3.6.3.- {ECO:0000313|EMBL:CAL79927.1};
GN OrderedLocusNames=BRADO6289 {ECO:0000313|EMBL:CAL79927.1};
OS Bradyrhizobium sp. (strain ORS 278).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=114615 {ECO:0000313|EMBL:CAL79927.1, ECO:0000313|Proteomes:UP000001994};
RN [1] {ECO:0000313|EMBL:CAL79927.1, ECO:0000313|Proteomes:UP000001994}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ORS 278 {ECO:0000313|Proteomes:UP000001994};
RX PubMed=17540897; DOI=10.1126/science.1139548;
RA Giraud E., Moulin L., Vallenet D., Barbe V., Cytryn E., Avarre J.C.,
RA Jaubert M., Simon D., Cartieaux F., Prin Y., Bena G., Hannibal L.,
RA Fardoux J., Kojadinovic M., Vuillet L., Lajus A., Cruveiller S., Rouy Z.,
RA Mangenot S., Segurens B., Dossat C., Franck W.L., Chang W.S., Saunders E.,
RA Bruce D., Richardson P., Normand P., Dreyfus B., Pignol D., Stacey G.,
RA Emerich D., Vermeglio A., Medigue C., Sadowsky M.;
RT "Legumes symbioses: absence of nod genes in photosynthetic bradyrhizobia.";
RL Science 316:1307-1312(2007).
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; CU234118; CAL79927.1; -; Genomic_DNA.
DR RefSeq; WP_012029812.1; NC_009445.1.
DR AlphaFoldDB; A4Z1A1; -.
DR STRING; 114615.BRADO6289; -.
DR KEGG; bra:BRADO6289; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_6_3_5; -.
DR OrthoDB; 391538at2; -.
DR Proteomes; UP000001994; 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:0015662; F:P-type ion transporter activity; IEA:UniProt.
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; 1.20.120.520; nmb1532 protein domain like; 1.
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; IPR012312; Hemerythrin-like.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_dom.
DR NCBIfam; TIGR01525; ATPase-IB_hvy; 1.
DR NCBIfam; TIGR01494; ATPase_P-type; 2.
DR PANTHER; PTHR48085; CADMIUM/ZINC-TRANSPORTING ATPASE HMA2-RELATED; 1.
DR PANTHER; PTHR48085:SF5; CADMIUM_ZINC-TRANSPORTING ATPASE HMA2; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF01814; Hemerythrin; 1.
DR Pfam; PF00702; Hydrolase; 1.
DR PRINTS; PR00119; CATATPASE.
DR SFLD; SFLDS00003; Haloacid_Dehalogenase; 1.
DR SFLD; SFLDF00027; p-type_atpase; 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 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 Hydrolase {ECO:0000313|EMBL:CAL79927.1};
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 Reference proteome {ECO:0000313|Proteomes:UP000001994};
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 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 32..53
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 65..90
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 230..249
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 255..280
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 565..584
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 627..755
FT /note="Hemerythrin-like"
FT /evidence="ECO:0000259|Pfam:PF01814"
SQ SEQUENCE 764 AA; 79761 MW; CA0168401648E491 CRC64;
MFERILRWTL VAIAVAGLAA GGLAYAVGRS ELAGIAFTAS TVPVIAGLIV SIVRDVLAGR
VGVDAIALVS MSAAIVLGEP LAGAVVALMY SGGNVLEDIA VARAEHDLRA LVDRAPRLAH
RWRDDRIEDV EVADVAVGDR LMVRAGEIVP VDGVVETVLA VIDESALTGE PIPVSKTRGM
AILSGSLNTG ETFELSVTAT AGESTYAGIV KLVTAAQTAK APFVRLADRY ALIFLPVSLA
IAAAAWFASG DLIRALAVMV AATPCPLILA APVAFIAGVA QAARSGILVK GGGKLEALAR
AHTVLFDKTG TLTVGGARLL SVEAAPGEDA DSVLLLGASL EQASHHVLAH AIVEAGQARG
LKLKVPERVR EAMGSGLEGV IDGRRISAGS PDLILGNHAP PPWAGRAIRR ASWRSALIVL
VAVDGKPIGA LLLADELRAD TPRAIRWLRE AGIARMVMVT GDRAAAAQAI GAALDLDAVL
ADRVPSDKVD AVRSEQRLHP TIMVGDGIND APALASADVG IALGARGASA SSEAADVVIL
ADRLDRVGEA IVIAQRARRI ALESIIAGMA LSFIAMGAAA FGLLQPVPAA LVQEAIDVAV
ILNALRALLP AGRARTGRIT VEDGQGLRHD HQALLRGLDR LRAIVDTLDE APPERAVSLI
VEANAVVQDQ VVAHERDDEG SVYPRLARLL QDSHGLSAMS RAHREILHLA RLLGRVVEDL
PSEKVDRYLI RDAQRVIEAI ETLVRMHTAQ EDDIYEAVAA RSAA
//
