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Database: UniProt
Entry: W0RW81_9BACT
LinkDB: W0RW81_9BACT
Original site: W0RW81_9BACT 
ID   W0RW81_9BACT            Unreviewed;      1009 AA.
AC   W0RW81;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 41.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=J421_6298 {ECO:0000313|EMBL:AHG93833.1};
OS   Gemmatirosa kalamazoonensis.
OG   Plasmid 2 {ECO:0000313|EMBL:AHG93833.1, ECO:0000313|Proteomes:UP000019151}.
OC   Bacteria; Gemmatimonadota; Gemmatimonadetes; Gemmatimonadales;
OC   Gemmatimonadaceae; Gemmatirosa.
OX   NCBI_TaxID=861299 {ECO:0000313|EMBL:AHG93833.1, ECO:0000313|Proteomes:UP000019151};
RN   [1] {ECO:0000313|EMBL:AHG93833.1, ECO:0000313|Proteomes:UP000019151}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=KBS708 {ECO:0000313|EMBL:AHG93833.1,
RC   ECO:0000313|Proteomes:UP000019151};
RC   PLASMID=Plasmid 2 {ECO:0000313|Proteomes:UP000019151};
RX   PubMed=24699952;
RA   Debruyn J.M., Radosevich M., Wommack K.E., Polson S.W., Hauser L.J.,
RA   Fawaz M.N., Korlach J., Tsai Y.C.;
RT   "Genome Sequence and Methylome of Soil Bacterium Gemmatirosa
RT   kalamazoonensis KBS708T, a Member of the Rarely Cultivated Gemmatimonadetes
RT   Phylum.";
RL   Genome Announc. 2:e00226-14(2014).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + protein L-histidine = ADP + protein N-phospho-L-
CC         histidine.; EC=2.7.13.3; Evidence={ECO:0000256|ARBA:ARBA00000085};
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DR   EMBL; CP007130; AHG93833.1; -; Genomic_DNA.
DR   AlphaFoldDB; W0RW81; -.
DR   KEGG; gba:J421_6298; -.
DR   PATRIC; fig|861299.3.peg.6368; -.
DR   eggNOG; COG4191; Bacteria.
DR   HOGENOM; CLU_000445_114_51_0; -.
DR   InParanoid; W0RW81; -.
DR   OrthoDB; 5287556at2; -.
DR   Proteomes; UP000019151; Plasmid 2.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 3.
DR   CDD; cd00156; REC; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.30.450.20; PAS domain; 5.
DR   InterPro; IPR011006; CheY-like_superfamily.
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; IPR001610; PAC.
DR   InterPro; IPR000014; PAS.
DR   InterPro; IPR000700; PAS-assoc_C.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR013655; PAS_fold_3.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 4.
DR   PANTHER; PTHR43065:SF10; PEROXIDE STRESS-ACTIVATED HISTIDINE KINASE MAK3; 1.
DR   PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08447; PAS_3; 1.
DR   Pfam; PF08448; PAS_4; 4.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00086; PAC; 4.
DR   SMART; SM00091; PAS; 5.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 4.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50113; PAC; 4.
DR   PROSITE; PS50112; PAS; 3.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Plasmid {ECO:0000313|EMBL:AHG93833.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000019151}.
FT   DOMAIN          186..238
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          239..309
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          313..365
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          366..427
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          439..491
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          499..535
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   DOMAIN          577..629
FT                   /note="PAC"
FT                   /evidence="ECO:0000259|PROSITE:PS50113"
FT   DOMAIN          642..872
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          892..1003
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   MOD_RES         943
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1009 AA;  107696 MW;  CCE64592EE5945A8 CRC64;
     MTASPVRVSP SAEPHAPAAP AFLVLDRSGR CTHATHDAAA LLGLGDVALV GRSLADVLPA
     ADVLHDAIAA AVATQRATTV SEPVPGRVVP SPEGALLLLD GEPWSDAAAG VEGTRYLHAV
     LDTVPECIKV VARDGTLLDM NGAGLAMLEA PSRDAVIGCP VEQIVVPRHR GALRRVLASV
     FGGTAARAEL EIVTLGGHTR RVETRAAPLR DDAGNVVAAL SVTHDVSDRH ADAERLRESE
     TRFRTLAAAA PAGIALLDAT GNALYRNERF AEILGIDLEQ ITDATWRAAM HPADLAAAER
     DAHAFLAGEA DETTSEYRLR RADGTVRWVH STLRRQRDAD GRPTGMIAIV ADVTAEKHAE
     AERRANDARF RQLAAAAPVG IFLGDADGRV LYANPRYEEI WELRGEAALG NGWLTRMTPE
     EASRLRRDGI AAFAAGAQFS SEYQIVLPDG RTRWIRGHMV LLRNAAGEPE SSLGTVEDIT
     ARREAEEAEA RARSAADVER ARLEAVLEAL PAGVIFADAD GRIVRATRQA RALWGGDVTA
     EHVDGYGRYR ARLRGSNRPL TDDERALTRA LRGESTPPRE LELERLDGGS ATVLSAAEPV
     RDAEGRIVGG VVVLIDVSER VRLEAQLRQA QKMEAVGQLA GGVAHDFNNL LTVINGNLEF
     ARNDIDPDHQ AQEDLAQVAQ AAERARALVR QLLAFSRKQV VQSEEIDVND VVRGAEALLR
     RVLGEEIAFA TTLAERPAVV RADRGQLEQV LLNLAVNARD AMLTTAHGRA GTGGTLTLVT
     DVVRLSPREA QGWTPGPGRY VRLTVSDTGH GMDATTRAHI FEPFFTTKAV GAGTGLGLAT
     VYGIVTQAGG AVHVDSEPGA GATFTILLPY QGGRVAAAER GGGTSLPRGR GTVLVVEDEA
     SVRLTTRRVL ERHGFAVLEA RHGADALLVW REHGADIVCC VTDLRMPEMG GRELVAQIRA
     DRPALPVVYL SGYVDRGAVE PADGFVEKPF TGEALLQAVT SVLRAPRDA
//
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