ID A0A066Z182_9ACTN Unreviewed; 1300 AA.
AC A0A066Z182;
DT 03-SEP-2014, integrated into UniProtKB/TrEMBL.
DT 03-SEP-2014, sequence version 1.
DT 27-MAR-2024, entry version 58.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=KCH_06530 {ECO:0000313|EMBL:KDN87543.1};
OS Kitasatospora cheerisanensis KCTC 2395.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Kitasatospora.
OX NCBI_TaxID=1348663 {ECO:0000313|EMBL:KDN87543.1, ECO:0000313|Proteomes:UP000027178};
RN [1] {ECO:0000313|EMBL:KDN87543.1, ECO:0000313|Proteomes:UP000027178}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KCTC 2395 {ECO:0000313|EMBL:KDN87543.1,
RC ECO:0000313|Proteomes:UP000027178};
RA Nam D.H.;
RT "Draft Genome Sequence of Kitasatospora cheerisanensis KCTC 2395.";
RL Submitted (MAY-2014) 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; Evidence={ECO:0000256|ARBA:ARBA00000085};
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KDN87543.1}.
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DR EMBL; JNBY01000028; KDN87543.1; -; Genomic_DNA.
DR PATRIC; fig|1348663.4.peg.621; -.
DR eggNOG; COG0784; Bacteria.
DR eggNOG; COG1511; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR HOGENOM; CLU_000445_3_0_11; -.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000027178; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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; 5.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.120.1530; -; 4.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
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 PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF13185; GAF_2; 1.
DR Pfam; PF00672; HAMP; 5.
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; 6.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF55781; GAF domain-like; 1.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 3.
DR PROSITE; PS50885; HAMP; 6.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KDN87543.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000027178};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KDN87543.1}.
FT DOMAIN 26..72
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 112..164
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 204..256
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 296..348
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 388..440
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 480..532
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 804..1034
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1048..1157
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 1181..1298
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 586..614
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1154..1174
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 746..794
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1..18
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1099
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 1231
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1300 AA; 138133 MW; 27086C952C83088B CRC64;
MDSTPDPKAP EPERPAQQHA EPDGVALRRL LAGLTAVRDG DLSLRLPDAP GVLGEISGVY
NDMAERLSRL NAEVTRVARE VGTEGMLGGQ AEVPQAVGAW RELADSVNAM AGNLTAQVRN
IAQVTTAVAR GDLTRTIAVD AQGEILELKN TVNTMVEQLS SFAAEVTRVA REVGTEGILG
GQADVRGVSG TWRDLTDSVN FMAGNLTAQV RSIAQVATAV ARGDLTRKTD VVARGEILEL
KSTVNTMVEQ LSSFAGEVTR VAREVGTEGA LGGQADVRGV SGTWRDLTDN VNVMAANLTG
QVRSMAQVAT AVARGDLSRR VTVEAAGEVA ELVGALNAMV DTLSAFAAEV TRVAREVGTD
GTLGGQARLP NVAGTWKDLT DSVNFMAHNL TSQVRNIAQV TTAVARGDLT RKIDVDARGE
ILELKNTVNT MVEQLSSFAA EVTRVAREVG TEGRLGGQAE VEGVSGTWKR LTENVNELAG
NLTRQVRAIG EVTSAVTAGD LTRSVTVDAS GEVADLKDNV NVMVESLRET TRANREQDWL
KTHLARLTGM IQGRREPAAV AELLMDELCP LLGAQYGTCY LAESGPAENR PGGGPAEQPD
DGGGDGPDRP ALVRAAGYGH PEAGAPRRFG LGESLIGQAG RSRRPIAITE LPPGYAEIRS
GLGSGPPREL LIQPIAMEDR LLGVVEVATL HHFTDLHRDF LERLAQDIGT TLATLLANAR
TDELLQESQR LTAELQARSE QLVDGQEELR RSNAELGEKA ELLAAQNRDI EAKNLQIEQA
RRELEERARQ LTSASMYKSE FLANMSHELR TPLNSLLILA QLLAQNPEGN LTGKQVEYAE
VIRSAGSDLL QLINDILDLS KVEAGKLDVT VEPFPLRELL DYVDTTFRPL AAEKNLEFRI
GTAPGAPEEL RTDQARLRQI LRNLLSNAVK FTDRGFVELT VEAARPGELP TGQRESAAVA
FRVQDSGIGI GADHLESIFG AFQQADGTTS RKYGGTGLGL SISRELARLL GGAVSAESVP
GEGSCFTLLL PAPAPAEAAE PAEAAERRIL VVEPDPPGLL TVLARSAVAD RDTTVDSAAD
PDSALAALDR RPPRLIVLDL ALPQDGARTL LAALERRPAP VPVIGHTTTP DAPLPDGDRL
EITTGLDELR ERVGKAAGPP ADEPAPAAAP SDRAGRLAGR TVLVVDDDSR NVYALSAALE
REGATALHAA NGRTGLALLR AHPETDLVLM DLMMPELDGY AATAAIRESA EHANVPIIAV
TAKALPDDRA RSLAAGADDH LTKPVDTTHL ITTVLHWLES
//
