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Database: UniProt
Entry: A0A261SG29_9BORD
LinkDB: A0A261SG29_9BORD
Original site: A0A261SG29_9BORD 
ID   A0A261SG29_9BORD        Unreviewed;       845 AA.
AC   A0A261SG29;
DT   20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT   20-DEC-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Copper-translocating P-type ATPase {ECO:0000313|EMBL:OZI36379.1};
GN   ORFNames=CEG14_15375 {ECO:0000313|EMBL:OZI36379.1};
OS   Bordetella genomosp. 1.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=1395607 {ECO:0000313|EMBL:OZI36379.1, ECO:0000313|Proteomes:UP000217005};
RN   [1] {ECO:0000313|EMBL:OZI36379.1, ECO:0000313|Proteomes:UP000217005}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AU17610 {ECO:0000313|EMBL:OZI36379.1,
RC   ECO:0000313|Proteomes:UP000217005};
RA   Spilker T., LiPuma J.;
RT   "Complete and WGS of Bordetella genogroups.";
RL   Submitted (MAY-2017) to the EMBL/GenBank/DDBJ databases.
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}.
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:OZI36379.1}.
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DR   EMBL; NEVL01000003; OZI36379.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A261SG29; -.
DR   OrthoDB; 8552908at2; -.
DR   Proteomes; UP000217005; Unassembled WGS sequence.
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:0005507; F:copper ion binding; IEA:InterPro.
DR   GO; GO:0015662; F:P-type ion transporter activity; IEA:UniProt.
DR   CDD; cd00371; HMA; 2.
DR   CDD; cd02094; P-type_ATPase_Cu-like; 1.
DR   Gene3D; 3.30.70.100; -; 2.
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; IPR006122; HMA_Cu_ion-bd.
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   NCBIfam; TIGR00003; copper ion binding protein; 2.
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; PF00403; HMA; 2.
DR   Pfam; PF00702; Hydrolase; 1.
DR   PRINTS; PR00119; CATATPASE.
DR   PRINTS; PR00943; CUATPASE.
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; 2.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01047; HMA_1; 2.
DR   PROSITE; PS50846; HMA_2; 2.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|RuleBase:RU362081};
KW   Cell membrane {ECO:0000256|RuleBase:RU362081};
KW   Copper {ECO:0000256|ARBA:ARBA00023008};
KW   Copper transport {ECO:0000256|ARBA:ARBA00022796};
KW   Ion transport {ECO:0000256|ARBA:ARBA00022796};
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   Repeat {ECO:0000256|ARBA:ARBA00022737};
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}; Transport {ECO:0000256|ARBA:ARBA00022796}.
FT   TRANSMEM        179..201
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        213..232
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        248..271
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        277..296
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        430..452
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        458..481
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        774..793
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   TRANSMEM        799..821
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|RuleBase:RU362081"
FT   DOMAIN          18..83
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
FT   DOMAIN          85..151
FT                   /note="HMA"
FT                   /evidence="ECO:0000259|PROSITE:PS50846"
SQ   SEQUENCE   845 AA;  87871 MW;  70EEA6E5B998200D CRC64;
     MGRSSPPQAP SAAASLPVAH QLAVEGMTCA SCVRRVEKAV AAVPGVARAS VNLATERVDV
     EFAGTPDFGP VQAAIADAGY AVREDTVELA IEGMTCASCV ARIERALRAV PGVLEATVNL
     ATERATVRRM SGAADDAALR QAVADAGYEA RIATEGDTPD QASAARDAEI RKLGRSLSIA
     AVLTLPVFIV EMGSHLIPAF HRWVMATMSG WNWQAQFVLT TLVLFGPGWR FFRRGIPALL
     KGAPDMNALV ALGSGAAWTY SLVATFLPGL LPAGTANVYY EAAAVIVTLI LLGRYLEARA
     KGRTGEAIKK LMGLQAKTAR VLRDGVAHEV PLGEVRAGDL VQVRPGERIA VDGEVTEGGS
     YVDEAMITGE PIPVEKRAGD DVVGGTLNKT GSFTFRATKV GSATLLAQII RMVEQAQGAK
     LPIQAMVDKV TAWFVPAVIA AAVLTFLVWL FVGPDPALVF ALVNGVAVLI IACPCAMGLA
     TPTSIMVGTG RAAELGVLFR KGDALQTLRD ASVIAIDKTG TLTEGRPELT DFLVLEGFDE
     RTVLQQVAAV EARSEHPVAE AIARAAEQRG LALLAAADFE AIPGFGVRAT VSEQRVDVGA
     DRYMRQLGLD IGVFGATAAR LADQGRTPLY AAVGGRLAAI IAVADPIKAS TPAAIAAFHA
     LGLKVAMVTG DNTRTAQAIA RELGIDLVMA EVLPDGKVEA VRQLAMGGAR VAFVGDGIND
     APALAAADVG IAIGTGTDIA IESADVVLMS GELTGVANAI ALSRATLRNI RQNLFWAFAY
     NVALIPVAAG VLYPVNGTLL SPMLAAGAMA FSSVFVLSNA LRLKRFSAPI QPGQPAVPAR
     LATAR
//
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