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Database: UniProt
Entry: A0A0K2GCH3_NITMO
LinkDB: A0A0K2GCH3_NITMO
Original site: A0A0K2GCH3_NITMO 
ID   A0A0K2GCH3_NITMO        Unreviewed;       509 AA.
AC   A0A0K2GCH3;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   08-MAY-2019, entry version 21.
DE   SubName: Full=Putative Sensor histidine kinase {ECO:0000313|EMBL:ALA58648.1};
DE            EC=2.7.13.3 {ECO:0000313|EMBL:ALA58648.1};
GN   ORFNames=NITMOv2_2232 {ECO:0000313|EMBL:ALA58648.1};
OS   Nitrospira moscoviensis.
OC   Bacteria; Nitrospirae; Nitrospirales; Nitrospiraceae; Nitrospira.
OX   NCBI_TaxID=42253 {ECO:0000313|EMBL:ALA58648.1, ECO:0000313|Proteomes:UP000069205};
RN   [1] {ECO:0000313|EMBL:ALA58648.1, ECO:0000313|Proteomes:UP000069205}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NSP M-1 {ECO:0000313|EMBL:ALA58648.1,
RC   ECO:0000313|Proteomes:UP000069205};
RX   PubMed=26305944; DOI=10.1073/pnas.1506533112;
RA   Koch H., Lucker S., Albertsen M., Kitzinger K., Herbold C., Spieck E.,
RA   Nielsen P.H., Wagner M., Daims H.;
RT   "Expanded metabolic versatility of ubiquitous nitrite-oxidizing
RT   bacteria from the genus Nitrospira.";
RL   Proc. Natl. Acad. Sci. U.S.A. 112:11371-11376(2015).
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; CP011801; ALA58648.1; -; Genomic_DNA.
DR   EnsemblBacteria; ALA58648; ALA58648; NITMOv2_2232.
DR   KEGG; nmv:NITMOv2_2232; -.
DR   PATRIC; fig|42253.5.peg.2198; -.
DR   KO; K07711; -.
DR   OMA; NARQRAP; -.
DR   Proteomes; UP000069205; 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; cd06225; HAMP; 1.
DR   CDD; cd00075; HATPase_c; 1.
DR   CDD; cd00082; HisKA; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR007891; CHASE3.
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; PF05227; CHASE3; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
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;
KW   ATP-binding {ECO:0000256|SAAS:SAAS00925949};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000069205};
KW   Kinase {ECO:0000256|SAAS:SAAS01003914, ECO:0000313|EMBL:ALA58648.1};
KW   Membrane {ECO:0000256|SAAS:SAAS00925724, ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS00925310};
KW   Reference proteome {ECO:0000313|Proteomes:UP000069205};
KW   Transferase {ECO:0000256|SAAS:SAAS01003669,
KW   ECO:0000313|EMBL:ALA58648.1};
KW   Transmembrane {ECO:0000256|SAAS:SAAS00926038,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAAS:SAAS00926160,
KW   ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|SAAS:SAAS00924981}.
FT   TRANSMEM     22     46       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    204    224       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      221    273       HAMP. {ECO:0000259|PROSITE:PS50885}.
FT   DOMAIN      281    502       Histidine kinase. {ECO:0000259|PROSITE:
FT                                PS50109}.
FT   COILED       95    115       {ECO:0000256|SAM:Coils}.
SQ   SEQUENCE   509 AA;  56349 MW;  A50EDE230ED8DC4E CRC64;
     MALPTLLVSI AGSRDISVRL SIFWRLVLTS LVIIAVMGGV NLYALFQLRQ LTAMSTEMAS
     YHYPAVESAK RLLGSLYAQL NSEKKYMATK DNAFLTNFNE EVEEFQRSLQ HLRSQETSPQ
     GLRLLQETGR LLQERLVLFH DEFQLVNDKT RAPVPGYDNR RDALMDRMSS TIQSYVDLHE
     ARISVGVSES RASAAQAEAV TEQLVLVALV FGLGLAGIAS YTILRPLRQL QSHIKQIGQG
     NFGVPLQITA PAELKQLVDT VNWMGTKLQE LDDMKAEFLA HVSHELRTPM ASIQEGTHLL
     LDEIPGPLLQ EQRTTLRIMA DSSRRLIHLI STILDLSKME AGMMEYRIVP VDLRRVADIS
     VNKVRLLADS KHVQLVLEHP GERIWVKADA PRIEQVIDNL LSNALKFSPE GGIVKMQMKP
     DLKAGVLEVA VSDAGPGIAP EDLPHIFERF YQGKTRAKQT SAGSGLGLAL AKKVVEAHGG
     RIWIESEMGK GTTVRFILRL TKPGGAGSA
//
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