ID A1JN96_YERE8 Unreviewed; 918 AA.
AC A1JN96;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 115.
DE RecName: Full=Copper-exporting P-type ATPase {ECO:0000256|ARBA:ARBA00015102};
DE EC=7.2.2.8 {ECO:0000256|ARBA:ARBA00012517};
DE AltName: Full=Copper-exporting P-type ATPase A {ECO:0000256|ARBA:ARBA00029719};
DE AltName: Full=Cu(+)-exporting ATPase {ECO:0000256|ARBA:ARBA00033239};
GN Name=ybaR {ECO:0000313|EMBL:CAL13097.1};
GN OrderedLocusNames=YE3061 {ECO:0000313|EMBL:CAL13097.1};
OS Yersinia enterocolitica serotype O:8 / biotype 1B (strain NCTC 13174 /
OS 8081).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Yersiniaceae; Yersinia.
OX NCBI_TaxID=393305 {ECO:0000313|EMBL:CAL13097.1, ECO:0000313|Proteomes:UP000000642};
RN [1] {ECO:0000313|EMBL:CAL13097.1, ECO:0000313|Proteomes:UP000000642}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 13174 / 8081 {ECO:0000313|Proteomes:UP000000642};
RX PubMed=17173484; DOI=10.1371/journal.pgen.0020206;
RA Thomson N.R., Howard S., Wren B.W., Holden M.T.G., Crossman L.,
RA Challis G.L., Churcher C., Mungall K., Brooks K., Chillingworth T.,
RA Feltwell T., Abdellah Z., Hauser H., Jagels K., Maddison M., Moule S.,
RA Sanders M., Whitehead S., Quail M.A., Dougan G., Parkhill J.,
RA Prentice M.B.;
RT "The complete genome sequence and comparative genome analysis of the high
RT pathogenicity Yersinia enterocolitica strain 8081.";
RL PLoS Genet. 2:2039-2051(2006).
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; AM286415; CAL13097.1; -; Genomic_DNA.
DR RefSeq; WP_011816861.1; NC_008800.1.
DR RefSeq; YP_001007244.1; NC_008800.1.
DR AlphaFoldDB; A1JN96; -.
DR KEGG; yen:YE3061; -.
DR PATRIC; fig|393305.7.peg.3257; -.
DR eggNOG; COG2217; Bacteria.
DR HOGENOM; CLU_001771_5_0_6; -.
DR OrthoDB; 9814270at2; -.
DR Proteomes; UP000000642; 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 CDD; cd00371; HMA; 3.
DR CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR Gene3D; 3.30.70.100; -; 3.
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 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; IPR017969; Heavy-metal-associated_CS.
DR InterPro; IPR006121; HMA_dom.
DR InterPro; IPR036163; HMA_dom_sf.
DR InterPro; IPR027256; P-typ_ATPase_IB.
DR InterPro; IPR001757; P_typ_ATPase.
DR InterPro; IPR044492; P_typ_ATPase_HD_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:SF6; COPPER-EXPORTING P-TYPE ATPASE; 1.
DR Pfam; PF00122; E1-E2_ATPase; 1.
DR Pfam; PF00403; HMA; 3.
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 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; SSF55008; HMA, heavy metal-associated domain; 3.
DR PROSITE; PS00154; ATPASE_E1_E2; 1.
DR PROSITE; PS01229; COF_2; 1.
DR PROSITE; PS01047; HMA_1; 2.
DR PROSITE; PS50846; HMA_2; 3.
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|ARBA:ARBA00022723,
KW 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 269..289
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 301..322
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 334..356
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 368..386
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 520..542
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 548..571
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 862..881
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT TRANSMEM 887..908
FT /note="Helical"
FT /evidence="ECO:0000256|RuleBase:RU362081"
FT DOMAIN 3..64
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 69..130
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT DOMAIN 183..246
FT /note="HMA"
FT /evidence="ECO:0000259|PROSITE:PS50846"
FT REGION 130..155
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 136..155
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 918 AA; 97244 MW; 7F9A1F1D199E155B CRC64;
MLQTTVLALH GLSCMNCAKR VKTALESRED VHHAEVNVHY AKVTGEAETT TLIDTVKQAG
YQAEEAQTPD IELQLSGLSC GHCTESTRKA LEAVPGVIAA DVSLDNAKVY GKVEAQTLID
AVEQAGYHAT LPGAQSPKTE PLTDSAPSSP EYLAAASSTI PAATTDIKNT QPSQPVAEPA
DNDSVQLLLT GMSCASCVSK VQNALQSVDG VEVARVNLAE RSALVTGHPS NEALIAAVKN
AGYGAEIIED ETERRERQQQ MSQASMKRFQ WQAALGLLLG IPLMGWGLFG GSMTLTPETQ
TPWLIVGIIT LLVMIFAGGH FYRNAWVSLK NGSATMDTLV ALGTGAAWIY SITVNIWPDV
FPMEARHLYY EASAMIIGLI NLGHAMEQRA RQRSSNALER LLDLAPPTAR LVTDEGEKLI
PLADVQLGMT LRLTTGDRVP VDGEIVQGEV WMDEAMLTGE PIPQQKSTGD VVHTGTQVQD
GTVLFRANAI GSQTTLARII KLVRQAQSSK PEIGKLADRI SAVFVPTVVA IAVIAGLIWY
FFGPQPQLIY TLVVATTVLI IACPCALGLA TPMSIISGVG RAAEFGVLVR DADALQQASN
LDTLVFDKTG TLTEGHPQVV AIHTFNGVSE QQALEWAAAL ETGSNHPLAR AILQRAEGLT
LATVNQFRTL RGLGVSGEVD GVALLLGNNR LLEEQQIDTS ELQSLIQQQA ESGTTPVILT
AQGKPAALLS IRDPLRSDSI SALQRLHQRG YNLVMLTGDN PITANAIAKE AGIDQVIAGV
LPDGKAEAIK QLQAAGHKVA MIGDGINDAP ALAQADVGIA MGGGSDIAIE TAAITLMRHS
LHGVADAVEL SKATLRNMKQ NLLGAFFYNA LGIPIAAGIL FPFTGTLLSP VVAGAAMALS
SITVVSNANR LLRFKPKQ
//
