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Database: UniProt
Entry: A0A1I0S9W9_9BACT
LinkDB: A0A1I0S9W9_9BACT
Original site: A0A1I0S9W9_9BACT 
ID   A0A1I0S9W9_9BACT        Unreviewed;      1190 AA.
AC   A0A1I0S9W9;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   13-FEB-2019, entry version 9.
DE   RecName: Full=Histidine kinase {ECO:0000256|SAAS:SAAS00924638};
DE            EC=2.7.13.3 {ECO:0000256|SAAS:SAAS00924638};
GN   ORFNames=SAMN04488122_5312 {ECO:0000313|EMBL:SEW53043.1};
OS   Chitinophaga arvensicola.
OC   Bacteria; Bacteroidetes; Chitinophagia; Chitinophagales;
OC   Chitinophagaceae; Chitinophaga.
OX   NCBI_TaxID=29529 {ECO:0000313|EMBL:SEW53043.1, ECO:0000313|Proteomes:UP000199310};
RN   [1] {ECO:0000313|EMBL:SEW53043.1, ECO:0000313|Proteomes:UP000199310}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 3695 {ECO:0000313|EMBL:SEW53043.1,
RC   ECO:0000313|Proteomes:UP000199310};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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; FOJG01000002; SEW53043.1; -; Genomic_DNA.
DR   BioCyc; GCF_900110835:BMW79_RS26255-MONOMER; -.
DR   Proteomes; UP000199310; Unassembled WGS sequence.
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   CDD; cd00156; REC; 3.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.30.565.10; -; 1.
DR   InterPro; IPR007891; CHASE3.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_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; PF05227; CHASE3; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF00672; HAMP; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 3.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00304; HAMP; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 3.
DR   SUPFAM; SSF47384; SSF47384; 1.
DR   SUPFAM; SSF52172; SSF52172; 3.
DR   SUPFAM; SSF55874; SSF55874; 1.
DR   PROSITE; PS50885; HAMP; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 3.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|SAAS:SAAS01002602};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Complete proteome {ECO:0000313|Proteomes:UP000199310};
KW   Kinase {ECO:0000256|SAAS:SAAS00924871, ECO:0000313|EMBL:SEW53043.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Nucleotide-binding {ECO:0000256|SAAS:SAAS01002785};
KW   Phosphoprotein {ECO:0000256|PROSITE-ProRule:PRU00169};
KW   Transferase {ECO:0000256|SAAS:SAAS00924820};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|SAAS:SAAS00924981}.
FT   TRANSMEM     12     31       Helical. {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM    175    199       Helical. {ECO:0000256|SAM:Phobius}.
FT   DOMAIN      220    272       HAMP. {ECO:0000259|PROSITE:PS50885}.
FT   DOMAIN      534    753       Histidine kinase. {ECO:0000259|PROSITE:
FT                                PS50109}.
FT   DOMAIN      803    916       Response regulatory.
FT                                {ECO:0000259|PROSITE:PS50110}.
FT   DOMAIN      925   1041       Response regulatory.
FT                                {ECO:0000259|PROSITE:PS50110}.
FT   DOMAIN     1071   1188       Response regulatory.
FT                                {ECO:0000259|PROSITE:PS50110}.
FT   COILED      434    506       {ECO:0000256|SAM:Coils}.
FT   MOD_RES     852    852       4-aspartylphosphate.
FT                                {ECO:0000256|PROSITE-ProRule:PRU00169}.
FT   MOD_RES     974    974       4-aspartylphosphate.
FT                                {ECO:0000256|PROSITE-ProRule:PRU00169}.
FT   MOD_RES    1121   1121       4-aspartylphosphate.
FT                                {ECO:0000256|PROSITE-ProRule:PRU00169}.
SQ   SEQUENCE   1190 AA;  132718 MW;  071056423267424C CRC64;
     MNHSFKRNLL VSYGTSLFLL IVSSIASFIS IRNLLDSQQW VNHTNTVITK LENVMSVMKD
     GETGERGFLL TGEAEFLEPY SGTAEKINRL LEEIRELTID NPAQTQTVEQ LREASNKRLA
     DFQHMIDQKK AGVAASSEIL RQGKVKMDEC RRLVQQMQNR EQALLVSRTG TVSQFASYTS
     ILILLASLLA ILVTIVSFVR VNSDFNKRVQ LQLELQQKDE ETTQRLNIIQ QIADRISSGN
     YQTRVGDEGK DVLGALSGSL NKMAESLEYS FTSLSEKEWL QAGIAALNEK MIGEKALTKL
     TYQVIEYLAA YTDAQVGAFY LLEGENTLSL SASIGLNTKD ARSEILLGEG LAGQSGLSGA
     PIQLRDIADA EMLIDYSGGS IKPHSIIALP VFHERMLKGV IEIASLKPFS NIAIEFLKAA
     MFNTGIAVNS AQDHQRLQVL LEETQAQSEE LQSQHNELES INAELEAQSQ RLQASEEELR
     VQQEELQEAN QELEGRSRLL QESNELILER NFEIQHKAEE LALSTKYKSE FLANMSHELR
     TPLNSILLLS RLLAENHPAN LEKEQIEYAE VIQSSGNGLL TLIDEILDLS KIESGKMELE
     YGYVALDEIS DEMTSLFEPI AHDKGITFTV EASEDLPKMI ETDHLRLQQV LRNLISNALK
     FTAAGSVVLQ IKKDLPGISF AVKDTGIGIP QNKQHTVFEA FQQADGSTRR KYGGTGLGLS
     ISRELARLLG GDIYLESEEN KGSTFTLKIP LHKETALPET TVVASADTPA YKPTPPREQR
     YIAEHIPAAI PDDRNEIGPG DKVILIVEDD TPFARSLLEY TRRSGFKGIV AVRGDEGVEL
     AKQYRPLGIL LDIELPVKSG WEVMEELKTN ASTRAIPVHI MSSHEVKHRS LSRGAVDFIN
     KPLAVEKLGE VFQKIEMALS KHPKKVLIVE ENQKHAQGLA YFLESFNIST EIRNNIGEGL
     KALNRTEVDC VILDMGIPTQ GSYDVLEEVK KTPGYENLPI IIFTGKNLSH VEEFRIKQYA
     DSIVIKTAHS YQRILDEVSL FLHLVEENKK DPGTYQYKKL NELSEILKGK TVLVADDDVR
     NIFSLTKSLE SYGLKVLSAI DGKEALTQLQ EGPKVDLVLM DMMMPEMDGY ESTARIRQIP
     AYKNLPVIAV TAKAMTGDRE KCINAGASDY ITKPVDVDQL ISLLRVWLYD
//
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