(data stored in SCRATCH zone)

SWISSPROT: Q13S82_PARXL

ID   Q13S82_PARXL            Unreviewed;       795 AA.
AC   Q13S82;
DT   22-AUG-2006, integrated into UniProtKB/TrEMBL.
DT   22-AUG-2006, sequence version 1.
DT   08-MAY-2019, entry version 117.
DE   SubName: Full=Copper-translocating P-type ATPase {ECO:0000313|EMBL:ABE33057.1};
DE            EC=3.6.1.- {ECO:0000313|EMBL:ABE33057.1};
GN   ORFNames=Bxe_B2938 {ECO:0000313|EMBL:ABE33057.1};
OS   Paraburkholderia xenovorans (strain LB400).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=266265 {ECO:0000313|EMBL:ABE33057.1, ECO:0000313|Proteomes:UP000001817};
RN   [1] {ECO:0000313|EMBL:ABE33057.1, ECO:0000313|Proteomes:UP000001817}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LB400 {ECO:0000313|EMBL:ABE33057.1,
RC   ECO:0000313|Proteomes:UP000001817};
RX   PubMed=17030797; DOI=10.1073/pnas.0606924103;
RA   Chain P.S., Denef V.J., Konstantinidis K.T., Vergez L.M., Agullo L.,
RA   Reyes V.L., Hauser L., Cordova M., Gomez L., Gonzalez M., Land M.,
RA   Lao V., Larimer F., LiPuma J.J., Mahenthiralingam E., Malfatti S.A.,
RA   Marx C.J., Parnell J.J., Ramette A., Richardson P., Seeger M.,
RA   Smith D., Spilker T., Sul W.J., Tsoi T.V., Ulrich L.E., Zhulin I.B.,
RA   Tiedje J.M.;
RT   "Burkholderia xenovorans LB400 harbors a multi-replicon, 9.73-Mbp
RT   genome shaped for versatility.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15280-15287(2006).
CC   -!- SUBCELLULAR LOCATION: Cell membrane
CC       {ECO:0000256|RuleBase:RU362081}.
CC   -!- SIMILARITY: Belongs to the cation transport ATPase (P-type)
CC       (TC 3.A.3) family. Type IB subfamily.
CC       {ECO:0000256|RuleBase:RU362081}.
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DR   EMBL; CP000271; ABE33057.1; -; Genomic_DNA.
DR   RefSeq; WP_011490445.1; NZ_CP008762.1.
DR   STRING; 266265.Bxe_B2938; -.
DR   EnsemblBacteria; ABE33057; ABE33057; Bxe_B2938.
DR   GeneID; 4006814; -.
DR   KEGG; bxe:Bxe_B2938; -.
DR   PATRIC; fig|266265.5.peg.4749; -.
DR   eggNOG; ENOG4105C59; Bacteria.
DR   eggNOG; COG2217; LUCA.
DR   HOGENOM; HOG000250397; -.
DR   KO; K17686; -.
DR   OMA; HWMLPAW; -.
DR   OrthoDB; 237367at2; -.
DR   BioCyc; BXEN266265:BXE_RS22515-MONOMER; -.
DR   Proteomes; UP000001817; Chromosome 2.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-UniRule.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0019829; F:cation-transporting ATPase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0030001; P:metal ion transport; IEA:InterPro.
DR   CDD; cd00371; HMA; 1.
DR   Gene3D; 3.40.1110.10; -; 1.
DR   Gene3D; 3.40.50.1000; -; 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   Pfam; PF00403; HMA; 1.
DR   PRINTS; PR00941; CDATPASE.
DR   SUPFAM; SSF55008; SSF55008; 1.
DR   SUPFAM; SSF56784; SSF56784; 1.
DR   SUPFAM; SSF81653; SSF81653; 1.
DR   SUPFAM; SSF81665; SSF81665; 1.
DR   TIGRFAMs; TIGR01525; ATPase-IB_hvy; 1.
DR   TIGRFAMs; TIGR01494; ATPase_P-type; 2.
DR   PROSITE; PS00154; ATPASE_E1_E2; 1.
DR   PROSITE; PS01047; HMA_1; 1.
DR   PROSITE; PS50846; HMA_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; Q13S82.
DR   SWISS-2DPAGE; Q13S82.
KW   ATP-binding {ECO:0000256|RuleBase:RU362081};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001817};
KW   Hydrolase {ECO:0000313|EMBL:ABE33057.1};
KW   Membrane {ECO:0000256|RuleBase:RU362081};
KW   Metal-binding {ECO:0000256|PROSITE-ProRule:PRU00280,
KW   ECO:0000256|RuleBase:RU362081};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001817};
KW   Transmembrane {ECO:0000256|RuleBase:RU362081};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    124    143       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    155    177       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    189    207       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    213    231       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    371    392       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    398    421       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    741    760       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    766    786       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   DOMAIN       31     97       HMA. {ECO:0000259|PROSITE:PS50846}.
FT   METAL        41     41       {ECO:0000256|PROSITE-ProRule:PRU00280}.
FT   METAL        44     44       {ECO:0000256|PROSITE-ProRule:PRU00280}.
SQ   SEQUENCE   795 AA;  82072 MW;  39FD6557838EDCD4 CRC64;
     MPPRALPAMT ELATAPRPAN TADAADISAH TAELDIGGMT CASCAMRVEK ALAKVPGVVS
     ASVNLATETA TVDLNGAAAG PDALIAAVRK AGYEAALVAP PDTPASANES APADRKRDQT
     RRELAAVLAS AVLTLPLIGP MVGEWFGFHA MLSPWLQFAL ASVVQFVFGA RFYRAAFRAV
     RAGAGNMDLL VALGTSAAYG ISVYELATHP GDMMHLYFEA SAVVITLVRF GKWLEARAKR
     QTTDAIRALN ALRPDRARIR VGAGERDVPL AQVRVGTIVI VRPGERVPVD GTVLEGRTHI
     DESLITGESL PVPKQVADAV TAGSINGEGA IAVTTTAIGA ETTLARIIRL VESAQAEKAP
     IQRLVDRVSE IFVPAILAIA ALTLAGWLIA GAAGETAILN AVAVLVIACP CALGLATPAA
     IMAGTGVAAR RGVLIKDAEA LETAHRVTIV AFDKTGTLTL GQPSVTAFEP IGGISRDEAL
     ALAAAVQRNS DHPLARAVVK AYEAEAAATA AAAEAADMPA AIGEAVASPT RTRALHASAA
     RAVAGRGVEA DVDGRTLALG SGRWLGELGI ELPPEFAARA RELEAAGNTV SWLMQRAPLA
     PVALALIAFG DTVKPTARAA VERLAQMGIT SVLVTGDNRG SAASVARALG IDEFHADVLP
     EDKARVIRDL KIRSAGIVAM AGDGINDAPA LAAADIGIAM ATGTDVAMHA AGITLMRGDP
     ALVADAIDIS RRTWRKIRQN LFWAFVYNLI GIPLAAFGLL NPMLAGAAMA FSSVSVVTNA
     LLLRTWRGAQ NGSGR
//

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