(data stored in ACNUC7421 zone)

SWISSPROT: C7QHG0_CATAD

ID   C7QHG0_CATAD            Unreviewed;      1119 AA.
AC   C7QHG0;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   08-MAY-2019, entry version 76.
DE   RecName: Full=Histidine kinase {ECO:0000256|SAAS:SAAS00924638};
DE            EC=2.7.13.3 {ECO:0000256|SAAS:SAAS00924638};
GN   OrderedLocusNames=Caci_0144 {ECO:0000313|EMBL:ACU69099.1};
OS   Catenulispora acidiphila (strain DSM 44928 / NRRL B-24433 / NBRC
OS   102108 / JCM 14897).
OC   Bacteria; Actinobacteria; Catenulisporales; Catenulisporaceae;
OC   Catenulispora.
OX   NCBI_TaxID=479433 {ECO:0000313|EMBL:ACU69099.1, ECO:0000313|Proteomes:UP000000851};
RN   [1] {ECO:0000313|EMBL:ACU69099.1, ECO:0000313|Proteomes:UP000000851}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44928 / NRRL B-24433 / NBRC 102108 / JCM 14897
RC   {ECO:0000313|Proteomes:UP000000851};
RX   PubMed=21304647;
RA   Copeland A., Lapidus A., Glavina Del Rio T., Nolan M., Lucas S.,
RA   Chen F., Tice H., Cheng J.F., Bruce D., Goodwin L., Pitluck S.,
RA   Mikhailova N., Pati A., Ivanova N., Mavromatis K., Chen A.,
RA   Palaniappan K., Chain P., Land M., Hauser L., Chang Y.J.,
RA   Jeffries C.D., Chertkov O., Brettin T., Detter J.C., Han C., Ali Z.,
RA   Tindall B.J., Goker M., Bristow J., Eisen J.A., Markowitz V.,
RA   Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Catenulispora acidiphila type strain (ID
RT   139908).";
RL   Stand. Genomic Sci. 1:119-125(2009).
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};
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; CP001700; ACU69099.1; -; Genomic_DNA.
DR   RefSeq; WP_012784394.1; NC_013131.1.
DR   STRING; 479433.Caci_0144; -.
DR   EnsemblBacteria; ACU69099; ACU69099; Caci_0144.
DR   KEGG; cai:Caci_0144; -.
DR   eggNOG; ENOG4105BZU; Bacteria.
DR   eggNOG; COG2203; LUCA.
DR   eggNOG; COG2770; LUCA.
DR   HOGENOM; HOG000183568; -.
DR   OMA; QFATTIH; -.
DR   OrthoDB; 1755994at2; -.
DR   BioCyc; CACI479433:G1GFP-144-MONOMER; -.
DR   Proteomes; UP000000851; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:InterPro.
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; 4.
DR   CDD; cd00075; HATPase_c; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00156; REC; 1.
DR   Gene3D; 2.60.120.260; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR008979; Galactose-bd-like_sf.
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   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF00672; HAMP; 4.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00304; HAMP; 5.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF52172; SSF52172; 1.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50885; HAMP; 5.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
DR   PRODOM; C7QHG0.
DR   SWISS-2DPAGE; C7QHG0.
KW   ATP-binding {ECO:0000256|SAAS:SAAS01002602};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000851};
KW   Kinase {ECO:0000256|SAAS:SAAS00924871, ECO:0000313|EMBL:ACU69099.1};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS01002785};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000851};
KW   Transferase {ECO:0000256|SAAS:SAAS00924820,
KW   ECO:0000313|EMBL:ACU69099.1};
KW   Two-component regulatory system {ECO:0000256|SAAS:SAAS00924981}.
FT   DOMAIN       11     66       HAMP. {ECO:0000259|PROSITE:PS50885}.
FT   DOMAIN      106    158       HAMP. {ECO:0000259|PROSITE:PS50885}.
FT   DOMAIN      198    250       HAMP. {ECO:0000259|PROSITE:PS50885}.
FT   DOMAIN      290    342       HAMP. {ECO:0000259|PROSITE:PS50885}.
FT   DOMAIN      382    434       HAMP. {ECO:0000259|PROSITE:PS50885}.
FT   DOMAIN      687    922       Histidine kinase. {ECO:0000259|PROSITE:
FT                                PS50109}.
FT   DOMAIN      987   1104       Response regulatory.
FT                                {ECO:0000259|PROSITE:PS50110}.
FT   COILED      415    435       {ECO:0000256|SAM:Coils}.
FT   COILED      608    677       {ECO:0000256|SAM:Coils}.
FT   MOD_RES    1037   1037       4-aspartylphosphate.
FT                                {ECO:0000256|PROSITE-ProRule:PRU00169}.
SQ   SEQUENCE   1119 AA;  120482 MW;  1A7F229F7ABE636D CRC64;
     MTLQSDARTD PELDRQLGAI LEVAQAVARG DLSRKIALSG DIVDGPVAEL ARTIDAMVGQ
     LSGFASEVIR VARELGTEGR LGGQATVEHA EGIWRDITDS VNSAARNLTA QVRDIAGVTT
     AVAQGDLTQK ITVEVAGEML ELKDTINTMV DQLSGFADEV TRVSLEVGTE GRLGGQARVP
     GVAGTWKDLT DSVNSMADNL TTQVRNIAQV ATAVASGDLT QSITVDARGE ILELKTTLNK
     MVDRLGTFAD EVTRVAREVG TEGKLGGQAT VRGVAGTWKD LTDNVNAMAN NLTSQVRNIA
     QVTTAVANGD LSKRIDVEAR GEILELKTTL NTMVDRLSAF ASEVTRVARE VGTEGKLGGQ
     ATVEDVSGTW QRLTESVNEL ASNLTTQVRA IAEVATAVTA GDLTRLITVE AKGEVADLKN
     NINQMIGNLR ETTRRNDQQD WLNTNLARMS GLMQGQRDLD AISALIMSEL TPLVNAQYGA
     FYLARKESGT KVLNLIASYG VDRESPDVTS RFRLGQGMVG QAAVERKPIM IQHAPVDYIR
     ISSGLGSAPP SSVAVLPVLF ENEVMAVIEL ASFHSFDEVH RALMESLMEM VGVTVNTITA
     NTRTEELLGE SRRLADELKA RTDELQMQQK ELRRSNAELE EKAELLARQN QDIEVKNSEI
     EQARQELEER ANQLTMSSRY KSEFLANMSH ELRTPLNSLL ILARLMSDNA EGNLTERQVE
     YAETIHGAGS DLLQLINDIL DLSKIEAGRM DVQPARIAVS QLVDYVEATF RPQTEQKGLE
     LRVRVAPSVP AHLFTDEQRL QQVLRNLLSN SVKFTETGHV ELVVDTVGDV VLGGPEDSNE
     VTLEPAVSFA VSDTGIGIVD DKIQTVFEAF QQEDGTTSRR YGGTGLGLSI SREIAKLLGG
     GIRAESQRGR GSTFTLFLPH AVGPDGAAVF GSTGSLGYGT SPGPTGAIAE PAPTLPMIPE
     QAPHPDLYLP STDLHAAGSD ITFDGEKILI VDDDIRNVFA LTSVLEQHGC AVLNAENGRA
     GLEALERADD VALVLMDVMM PEMDGYATMA AIREIDRYKN LPIIALTAKA MRGDREKSIE
     AGASDYVTKP VDTPHLLTVM RGWLDAETGA QPAPGGPAQ
//

If you have problems or comments...

PBIL Back to PBIL home page