(data stored in SCRATCH zone)

SWISSPROT: A0A0E1NNQ7_YERPA

ID   A0A0E1NNQ7_YERPA        Unreviewed;       782 AA.
AC   A0A0E1NNQ7;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   08-MAY-2019, entry version 27.
DE   SubName: Full=Putative P-type cation-translocating membrane ATPase {ECO:0000313|EMBL:ABG12171.1};
GN   OrderedLocusNames=YPA_0202 {ECO:0000313|EMBL:ABG12171.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12171.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12171.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12171.1,
RC   ECO:0000313|Proteomes:UP000001971};
RX   PubMed=16740952; DOI=10.1128/JB.00124-06;
RA   Chain P.S., Hu P., Malfatti S.A., Radnedge L., Larimer F.,
RA   Vergez L.M., Worsham P., Chu M.C., Andersen G.L.;
RT   "Complete genome sequence of Yersinia pestis strains Antiqua and
RT   Nepal516: evidence of gene reduction in an emerging pathogen.";
RL   J. Bacteriol. 188:4453-4463(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; CP000308; ABG12171.1; -; Genomic_DNA.
DR   RefSeq; WP_002220867.1; NZ_CP009906.1.
DR   EnsemblBacteria; ABG12171; ABG12171; YPA_0202.
DR   EnsemblBacteria; AJJ78584; AJJ78584; CH58_3047.
DR   KEGG; ypa:YPA_0202; -.
DR   PATRIC; fig|360102.15.peg.3199; -.
DR   KO; K01534; -.
DR   OMA; WLPWIYK; -.
DR   Proteomes; UP000001971; Chromosome.
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; A0A0E1NNQ7.
DR   SWISS-2DPAGE; A0A0E1NNQ7.
KW   ATP-binding {ECO:0000256|RuleBase:RU362081};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Membrane {ECO:0000256|RuleBase:RU362081};
KW   Metal-binding {ECO:0000256|RuleBase:RU362081};
KW   Nucleotide-binding {ECO:0000256|RuleBase:RU362081};
KW   Transmembrane {ECO:0000256|RuleBase:RU362081};
KW   Transmembrane helix {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    166    183       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    189    207       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    391    412       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    418    442       Helical. {ECO:0000256|RuleBase:RU362081}.
FT   TRANSMEM    734    752       Helical. {ECO:0000256|RuleBase:RU362081}.
SQ   SEQUENCE   782 AA;  83079 MW;  0B38972E03FEC4A8 CRC64;
     MHSHSEHQKS VETNSNCGCG HTHDKHQTGC SNLATAANSD AISHDSVSEH SHHDGESCSH
     THADEADEES DRLDTTIVSG TQRFSWQVKG MDCPSCARKI ENAISGLDGV EKVKVLFTTE
     KLVVDARADV RSLVQKAVIA TGFSLVNTQT TAGQKNVATE SRLREYLPLA LLSTLMLISW
     GLSFFNTELS QTAFTITTIV GLIPFVIKSW KLIRSGTPFA IETLMSVAAI GAVFIGATAE
     AAMVLLLFMV GELLESYAVN RARRGVTALM ALVPEEALLL KDGKRTLVPV ADLRPGDIIE
     IPPGGRLPAD AELQASFASF DESALTGESI PVERQQGEKV AAGCLSVDRA VEMCVVSEPG
     NNAIDRILQL IELAEERRAP IERFIDRFSR IYTPIIILFS ILVILVPPLV FAAPWEPWIY
     RGLTLLLIGC PCALVISTPA AITSALAAAT RRGALIKGGA ALEQLGRSQI IAFDKTGTLT
     EGKPKVTDVL PISGISETRL LTLAAAVEAG SHHPLAIAII QCTQQNQRAQ QNTPMLPLAE
     ERRALAGVGI EGVVDGLMVR VSAPSKLSPA LLTDEWQAQI DQLESSGKTA VVVLEDEKFI
     GLLALRDTLR TDAKQAIDAL KKLGIQGVML TGDNPRAAAA IAGELGIDYR AGLLPADKVQ
     AVMALNALQP TVMVGDGIND APAMKASSIG VAMGSGTDVA LETADTALTH NRLTGLAEII
     LLSRAANANI RQNITIALGL KAIFLVTTLL GLTGLWLAVL ADSGATALVT ANALRLLRKR
     DV
//

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