ID A0A239MSK6_9ACTN Unreviewed; 1412 AA.
AC A0A239MSK6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 24.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05443665_103191 {ECO:0000313|EMBL:SNT45807.1};
OS Actinomadura meyerae.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Thermomonosporaceae; Actinomadura.
OX NCBI_TaxID=240840 {ECO:0000313|EMBL:SNT45807.1, ECO:0000313|Proteomes:UP000198318};
RN [1] {ECO:0000313|EMBL:SNT45807.1, ECO:0000313|Proteomes:UP000198318}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44715 {ECO:0000313|EMBL:SNT45807.1,
RC ECO:0000313|Proteomes:UP000198318};
RA Kim H.J., Triplett B.A.;
RL Submitted (JUN-2017) 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};
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DR EMBL; FZOR01000031; SNT45807.1; -; Genomic_DNA.
DR Proteomes; UP000198318; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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 CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 1.20.120.1530; -; 5.
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; 6.
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; 8.
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; 6.
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:SNT45807.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000198318};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 208..260
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 300..352
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 392..444
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 484..536
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 576..628
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 668..720
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 972..1204
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1289..1406
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..21
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1205..1275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 886..941
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1339
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1412 AA; 151717 MW; A1409A30690F9D70 CRC64;
MPRTASRARP GGYRDTTPRY SDADLEPLLK ALVAVRDGRA RSELDVPGEG AVAEAAAILE
EIRQNEQELA SGLSRVRREI GREGKLSGRL AAGGLRGSWA ASVEDANAII DKLTDLATGM
SRVVEAVAAG DLSQRVELRV RGRPMRGELL RMAKSANGMV ELLDQFTWEV TQFAREVGTE
GRLGGQAPAR GMTGRWRDVT ASVNVMAARL TSQVRDIAEV TTAVVKGDLT RKVTVEASGE
LQELKLTVNT MVDQLSAFAD EVTRVAREVG TEGQLGGQAN VRGVSGVWKD LTDNVNAMAN
NLTNQVRNIA QVTTAVADGD LGKKITVDAQ GEILQLKNTL NTMVDTLSAF ADEVTRVARE
VGTEGRLGGQ ARVPGVSGVW KDLTNNVNGM ASNLTYQVRN IAQVTTAVAE GDLGKKITVD
AQGEILELKD TVNGMVDTLS AFASEVTRVA REVGTEGRLG GQAIVPGAGG VWKDLTDNVN
AMANNLTNQV RGIAQVTTAV AQGDLTRKID VTAQGEILQL KDTLNTMVDT LSSFASEVSR
VAREVGTEGR LGGQAIVPGA GGMWKDLTDN VNGMASNLTY QVRNIAQVAT AVAHGDLTRR
IDVNAQGEIL ELKTTLNTMV DTLSSFASEV TRVAREVGSE GRLGGQAEVE GVSGTWKRLT
ESVNELAGNL TTQVRAIGEV ASAVATGDLT RTITVEARGE VAELSDNVNL MVATLRETTR
ANEEQDWLKT NLARIGGLMQ GHRDLLQVAE LIMRELTPTA SAQYGAFYLA EAAGEEVELV
LIAGYGTRRG RDGAVRFALG EGLVGQAAQE RRPLLIADAP ADYVKIGSGL GEASPVNIIV
LPIVFEDEVL GAIELASFGR FTDVHLAFFS QLIETIGVTL NAIRANARTE ALLGESQRLA
QELQERSDEL QRQQGELRHS NTELEEKAAL LAQQNRAIEI QNFQIEQARR TLEERAEQLA
ISSRYKSEFL ANMSHELRTP LNSLLVLAKL LSENQDGNLT DKQVEFARTI HESGTDLLEL
INDILDLAKV EAGKMEAHPQ RLAVSSLVDY VDATFRPLSV DKGLQFGVEV APDVPTTLNT
DEQRLQQVLR NLLSNAVKFT AEGEVRLLIE RAGDIDFTLP ALWNTPDVIA FRVIDTGIGV
SADKLQEIFE PFQQADGTTS RRYGGTGLGL SISRNIARLL GGEIHAESQP GRGSVFTLYL
PAQYSEREDR RRPEPSAEAA GGGPGREADF GAGAEQGNGA VVRPLPAGAA ETGPPAEQRP
PATEPEPALN GMVEEPPTDF LDTVLSGRKV LIVDDDVRNV FALTSVLEGY GMEVLYAEDG
QAGIDLLHRN PDVAVVLMDV MMPGLDGYAT TAAIREMPQF ADLPIIVITA KVMKGDREKS
LASGASDYVP KPVDVDHLLD VMRNWLQPSI VR
//
