ID A0A0N0H081_9ACTN Unreviewed; 1795 AA.
AC A0A0N0H081;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ADL29_15865 {ECO:0000313|EMBL:KPC63392.1};
OS Streptomyces chattanoogensis.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=66876 {ECO:0000313|EMBL:KPC63392.1, ECO:0000313|Proteomes:UP000037982};
RN [1] {ECO:0000313|Proteomes:UP000037982}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL ISP-5002 {ECO:0000313|Proteomes:UP000037982};
RA Ju K.-S., Doroghazi J.R., Metcalf W.W.;
RL Submitted (JUL-2015) 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:KPC63392.1}.
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; LGKG01000133; KPC63392.1; -; Genomic_DNA.
DR PATRIC; fig|66876.3.peg.3481; -.
DR Proteomes; UP000037982; 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; 9.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.120.1530; -; 7.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 1.
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; 10.
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; 11.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
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; 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; 7.
DR PROSITE; PS50885; HAMP; 11.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 1.
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:KPC63392.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000037982};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 77..140
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 180..232
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 272..324
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 364..416
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 456..508
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 548..600
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 640..692
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 732..784
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 824..876
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 916..968
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1008..1060
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1322..1563
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1675..1792
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1587..1664
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1243..1312
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1725
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1795 AA; 191951 MW; 18A127497DD5ADB4 CRC64;
MRDGNFRKRL TVNGEGVMSE IAAVFNEVAD RNLHLTGELA RVRRVVGREG KLTERLEVGA
AEGSWAAAID ASNALVDDLV RPVSEVGRVL SAVSEGDLEQ RMDLRSRSSD SSSEHPLRGE
FLKVGRTVNG LVDQLSAFTD EVTRVASEVG TEGKLGGQAR VRGMSGSWKD LTESVNTMAS
RLTAQVRDIA LVTTAVAKGD LSRKVTVHVA GEMLELKNTV NTMVDQLSSF ASEVTRVARE
VGTEGELGGQ AQVPGVAGVW KDLTDSVNLM AGNLTAQVRG IAQVTTAVAN GDLSQKVTVS
ARGEVAQLAD TINTMTETLR TFADEVTRVA NEVGAEGQLG GQAQVPGAAG TWKDLTDSVN
NAFRNLTGQV RDIAQVTTAV ANGDLSQKVT VDVAGEMLEL KNTVNTMVDQ LSAFGSEVTR
VAREIGVEGE LGGQAAVPGA AGTWKDLTDS VNTAFRNLTG QVRNIAQVTT AVANGDLSQK
VTVDVSGEML QLKNTVNTMV DQLSSFADQV TRMARDVGTE GRLGGQARVD GVSGTWKELT
DSVNFMAGNL TSQVRQIAQV TTAVARGDLS QKIDVDARGE ILELKSTINT MVDQLSAFAE
QVTRVAREVG TDGRLGGQAQ VPGVAGVWRD LTDSVNGMAG NLTAQVRNIA QVATAVARGD
LSQKIDVDAR GEILELKNTL NTMVDQLSSF AEQVTRVARE VGTEGILGGQ AEVQGVSGTW
KDLTQSVNFM ANNLTSQVRN IGEVTTAVAR GDLSKKITVD AKGEILELVT TVNTMVDQLS
LFAEQVTRVA REVGTEGQLG GQARVPGVTG IWKDLSDNVN LMANNLTIQV RNISQVSAAV
ANGDLTKKVT VEARGEVAQL ADTVNTMVTT LSSFADEVTR VAREVGTDGI LGGQARVPGV
AGTWKDLTES VNSMANNLTG QVRNIAMVTT AVAKGDLTKK IDVDARGEIL ALKTTINTMV
DQLSSFAEQV TRVAREVGTE GQLGGQAQVR GVAGTWKDLT ESVNEMAGNL TRQVRAIAAV
AAAVTLGDHN VRIDVDAAGE ILELQDNVNT MISTLRETTL ANEEQDWLKG NLARISGLMQ
GRRDLKDVAT LIMSELSPAV SAQHGAFFLA AQPETQEIGA DGGEPGAYEL RLMGSYGYSM
GGMPTTFKPG ETLIGTAAEE GRTILVENVP SGYLKIASGL GEAPPANVIV LPVLFEDKVL
GVIELASFQP FTQIQKDFLS QIAEMIATSV NTISVNTKTE VLLKQSQELT EQLRERSAEL
ESRQKALELS NSELEEKAEQ LRAQNRDIEV KNTEIEEARQ VLEERAEQLA VSMRYKSEFL
ANMSHELRTP LNSLLILAKL LADNAEGNLS PKQVEFAETI HGAGSDLLQL INDILDLSKV
EAGKMDVSPT RIALVQLVDY VEATFRPLTA EKGLDFSVRV SPELPATLHT DEQRLLQVLR
NLLSNAVKFT DTGAVELVIR PAGADVPVAI REQLLEHGSL RDPDADMIAF SVTDTGIGIA
SSKMRVIFEA FKQADGTTSR KYGGTGLGLS ISREIARLLG GEIHAQSEPN RGSTFTLYLP
HNPGGLPPQG YPQLVAGGLA MDAEAREVEV GRQPEPETLP EEGMASSLNR RRRRGISGGA
RRFALPGGQP VSTPPQQTPR QPAEPTTQQP AEEPWIGNGQ DLVEPGFGGG FHGEKVLIVD
DDIRNVFALT SVLEQNGLSV LYAENGREGI EVLEQHDDIV LVLMDIMMPE MDGYATTSAI
RRMPQFAGLP IIALTAKAMK GDREKSIDSG ASDYVTKPVD TDHLLSVMEQ WMRAR
//
