(data stored in SCRATCH zone)

SWISSPROT: A0A0E1NN64_YERPA

ID   A0A0E1NN64_YERPA        Unreviewed;       355 AA.
AC   A0A0E1NN64;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   16-JAN-2019, entry version 24.
DE   SubName: Full=Two-component system sensor protein {ECO:0000313|EMBL:ABG12027.1};
DE   Flags: Precursor;
GN   OrderedLocusNames=YPA_0058 {ECO:0000313|EMBL:ABG12027.1};
OS   Yersinia pestis bv. Antiqua (strain Antiqua).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Yersiniaceae; Yersinia.
OX   NCBI_TaxID=360102 {ECO:0000313|EMBL:ABG12027.1, ECO:0000313|Proteomes:UP000001971};
RN   [1] {ECO:0000313|EMBL:ABG12027.1, ECO:0000313|Proteomes:UP000001971}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Antiqua {ECO:0000313|EMBL:ABG12027.1,
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   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3;
CC         Evidence={ECO:0000256|SAAS:SAAS01126420};
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DR   EMBL; CP000308; ABG12027.1; -; Genomic_DNA.
DR   RefSeq; WP_002210182.1; NZ_CP009906.1.
DR   EnsemblBacteria; ABG12027; ABG12027; YPA_0058.
DR   EnsemblBacteria; AJJ78306; AJJ78306; CH58_2894.
DR   KEGG; ypa:YPA_0058; -.
DR   PATRIC; fig|360102.15.peg.3048; -.
DR   KO; K07643; -.
DR   OMA; NAYRYSP; -.
DR   BioCyc; YPES360102:GHZU-66-MONOMER; -.
DR   Proteomes; UP000001971; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00075; HATPase_c; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR003660; HAMP_dom.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
DR   PRODOM; A0A0E1NN64.
DR   SWISS-2DPAGE; A0A0E1NN64.
KW   ATP-binding {ECO:0000256|SAAS:SAAS00925949};
KW   Complete proteome {ECO:0000313|Proteomes:UP000001971};
KW   Kinase {ECO:0000256|SAAS:SAAS01003914};
KW   Membrane {ECO:0000256|SAAS:SAAS00925724};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00925310};
KW   Transferase {ECO:0000256|SAAS:SAAS01003669};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00926038};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00926160};
KW   Two-component regulatory system {ECO:0000256|SAAS:SAAS00924981}.
SQ   SEQUENCE   355 AA;  40223 MW;  D98342ADBA0FA166 CRC64;
     MISMRRRLLL MLALILLVTQ LISAFWLWHE SQEQISFLVD ETLSAKARNE QVDKEIAEAI
     ASLLAPSLIM MTITLLLSFW AISWIIRPLD QLQQKLAERS ADNLSPLVVN SEMQEIVSVT
     STLNQLLLRL SNTIQQERLF TADAAHELRT PLAGIRLHLE LMEKQGIAES KSLINRIDLL
     MHTIEQLLML SRAGQNFASG HYQTLDWVND VVPPLQEELA EMCELRRQTI QWELPPHAKM
     EGDATLLRLM LRNLVENAHR YSPVGSQIIV TLSTENQGVL LQVTDEGPGI KQNQAGELTQ
     AFRRMDQRYG GSGLGLNIVI RIAQLHQGKL TLENRLDRTG LKAQCWLPAT TYSQK
//

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