ID A0A1H5TMZ5_9ACTN Unreviewed; 1345 AA.
AC A0A1H5TMZ5;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN05444920_101270 {ECO:0000313|EMBL:SEF64232.1};
OS Nonomuraea solani.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=1144553 {ECO:0000313|EMBL:SEF64232.1, ECO:0000313|Proteomes:UP000236732};
RN [1] {ECO:0000313|EMBL:SEF64232.1, ECO:0000313|Proteomes:UP000236732}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.7037 {ECO:0000313|EMBL:SEF64232.1,
RC ECO:0000313|Proteomes:UP000236732};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FNVT01000001; SEF64232.1; -; Genomic_DNA.
DR Proteomes; UP000236732; 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; -; 6.
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 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; 8.
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:SEF64232.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000236732};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 22..65
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 105..162
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 202..254
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 294..346
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 386..438
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 478..530
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 570..622
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 662..714
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 934..1158
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1220..1337
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT COILED 883..917
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1270
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1345 AA; 145068 MW; 9D8B2DF7D210FA3B CRC64;
MVAQLESPYT PGSLHPADLR PLLVALQGLR DGNFRTRLEM PGDPVLAELA ITFNQVIDRN
EHLSNELTRL RGEVARHGRL DERLSPSPGT GSWAVNIAAV NTLVDALVIP AAKATRVLNA
VADGDLSKRV DLQEDNRPLR GGLRLMGKAV NRMVDQLALF SGEVTRVARE VGTEGRLGGR
AKVQGMSGSW RDVTEAVNAM AGRLTAQVRD IAVVTTAVAR GDLTRQVTVE ATGELLELKL
TVNTMVDQLS SFASEVTRVA REVGTEGQLG GRAEVKGVLG TWKDLTDNVN FMASNLTTQV
RSIAQVTTAV ANGDLSKKIT VDARGEILQL KDTINTMVGQ LSAFADEVTR VAREVGTEGR
LGGQAQVRGV SGVWKDLTDN VNFMASNLTE QVRDIAQVAT AVAQGDLSRK ISVDVKGEIL
QLKDTVNTMV GQLSAFADEV TRVAREVGTE GRLGGQAQVR GVSGVWKDLT DNVNFMASNL
TSQVRNIAKV TTAIANGDLY KKINVDARGE ILQLKDTINA TVDKLSAFAD EVTRVAREVG
TEGRLGGQAQ VRGVSGVWKD LTDNVNFMAS NLTSQVRNIA QVATAVANGD LYKKIDVDAR
GEILELKTTI NTMVDTLSSF SSEVTRVARE VGSEGRLGGQ AEVEGVYGTW ERLTKNVNEL
AGNLTTQVRA IAEVASAVAQ GDLSRSISVE AKGEVAELKN NVNLMVANLR ETTRAKDWLE
SNLARIAGLM QGHRDLVEVA DLILRELTPL VSAQYGAFFL ADADSPDGSL AFIAGYGAAH
DVLPGPGTPG PGLIRQAALE RKRILFEDVP PGYIKVHSGL GEAAPASVVV LPIVYEDKVL
GVIELASFSR FSDVHLAFFD QFVVTIGVAI NTIIANARTE ALLSESQRLA QQLQGRSDEL
QRQQAELRKS NAALEEKAHL LATSSRYKSE FLANMSHELR TPLNSLLILA RLLADNPEGN
LSEQEVEFAT TIHNAGSDLL QLINDILDLS KIEAGRMDVR PEKLPLSKLL DYVDATFRPL
TVDRGLTFEI EVRPGTPREL YNDERRLQQI LRNLLSNAVK FTSAGEVRLE VRVEREAADG
DVIAFAVSDT GIGIAADKLP AIFGAFQQAD GTTSRKYGGT GLGLSISSEI ARLLGGEIHA
SSRPDSGSTF TLFVPARCPV AGHAGEPERE AEPALEAVET RAAPPHDEWP SAEGDDLWLR
GSTLTRLNDD PLGAVFGGRR VLIVDDDIRN VYALTHVLGR LGMEIVYAEN GREGIEALER
EEDIALVLMD VMMPEMDGYE TLVAVRQMPR FADLPIVALT AKAMPGDREK TIACGASDYV
PKPVDLDQLL EVMRGWLAGD REDGG
//
