ID A0A0M8WX25_9ACTN Unreviewed; 1419 AA.
AC A0A0M8WX25;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 46.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=ADL04_28665 {ECO:0000313|EMBL:KOV92977.1};
OS Streptomyces sp. NRRL B-3648.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=1519493 {ECO:0000313|EMBL:KOV92977.1, ECO:0000313|Proteomes:UP000037702};
RN [1] {ECO:0000313|EMBL:KOV92977.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-3648 {ECO:0000313|EMBL:KOV92977.1};
RA Noorani M.;
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:KOV92977.1}.
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; LGDZ01000208; KOV92977.1; -; Genomic_DNA.
DR RefSeq; WP_053711073.1; NZ_LGDZ01000208.1.
DR PATRIC; fig|1519493.3.peg.6098; -.
DR Proteomes; UP000037702; 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; 7.
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; -; 4.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 1.10.287.950; Methyl-accepting chemotaxis protein; 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; 7.
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; 7.
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; 3.
DR PROSITE; PS50885; HAMP; 7.
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:KOV92977.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000037702};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 18..64
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 104..156
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 196..248
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 288..340
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 380..432
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 472..524
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 564..616
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 868..1099
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1300..1417
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1102..1138
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 789..858
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1350
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1419 AA; 151587 MW; 0231FACA56AB0681 CRC64;
MAGKATGTTD TVPGDHELRR LLAGLTAVRD GDFGTRLPDD ASGLMGDIAT VFNGMVDQLS
VFTSEVTRVA REVGTEGTLG GQAQVPGVSG TWADLTDSVN AMAGNLTTQV RDIAQVATAV
AKGDLSQKID VPARGEILQL KETVNTMVDQ LSAFADEVTR VAREVGTEGR LGGQAQVPGV
AGVWRDLTDS VNFMAGNLTA QVRNVAQVTT AVAQGDLSQK ITVDARGEIL ELKSTINTMV
DQLSAFADEV TRVAREVGTE GRLGGQADVK GVKGTWRDLT DSVNFMGGNL TAQVRNVAQV
ATAVAQGDLS QKITVDARGE ILELKNTINT MVDQLSAFAD EVTRVAREVG TEGRLGGQAQ
VRGVAGTWKD LTDNVNVMAS NLTGQVRSIA QVATAVAKGD LSQKITVEAK GEVAALADVI
NTMVDTLSAF ADEVTRVARE VGTEGRLGGQ AHVPHVAGTW KDLTDNVNSM ANNLTGQVRN
IALVTTAVAR GDLSKKIDVD ARGEILELKT TINTMVDQLS AFADEVTRVA REVGTEGRLG
GQAEVEGVSG TWKRLTENVN ELAGNLTRQV RAIADVASAV AEGDLTRSIT VDASGEVADL
KDNINSMVES LRETTRANQE QDWLKTNLAR ISGLMQGHRD LPVVAELIMD ELVPQVSAQY
GAFYLAEEGA SGPELRLVGS YGRPEEDTRP VRIPFGRSLV GQAARSRRTI AVDKLPAGYV
TISSGLGHIE PTALLLLPIV FEEQVLGVIE LASVSPFTTV QRDFLQQLVD TIGVNVNTIV
ANARTDELLE ESQRLTSELQ SRSAELQARQ EELQSSNAEL EEKASLLADQ NRDIEAKNLQ
IEQARQELEA RAQQLSLASK YKSEFLANMS HELRTPLNSL LILAQLLAQN PSRNLTPKQV
EYAGIIHSAG SDLLQLINDI LDLSKVEAGK MDVTPERVPL RQLIDYVEAT FRPMTSQKSL
EFAVTTAAGA PADLLTDDSR LRQILRNLLS NAVKFTEQGS VELRVEPAAD GEVPDSVVRG
SAIVAFRVKD TGIGIPEQQL ETIFGAFQQA DGTMSRKYGG TGLGLSITRE MAHLLGGAVT
VDSTPGKGST FTLFLPVARP DFGDHPRGAL PGPSADEERT DGTSAPALTE GRPAAGGRQR
ARRLLVVEER PRGLLTLVAE SVVKDLEHGR ADNVGMPVDI ITAVGAQEAA GALASEPCHC
VVVELGEPDG ESARFLEALH GDSALAGVPV LVHVSHRTEP LAEDIAGGSP EHLYSLDELR
ERIALHLAAE EPGEVLTLVR ADEPHLAAPQ PVDEHTRGRT VLVVDDDARN LFALSGILEL
HGFRVLHAEN GRKGIDTLLN NPDVELVLMD VMMPEMDGYT ATAEIRKLPQ YADLPIIAVT
AKAMQGDREK SLASGASDYV TKPVDTHALI ACVRRWLPV
//
