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Database: UniProt
Entry: A0A428XMM8_9ACTN
LinkDB: A0A428XMM8_9ACTN
Original site: A0A428XMM8_9ACTN 
ID   A0A428XMM8_9ACTN        Unreviewed;       738 AA.
AC   A0A428XMM8;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   28-JUN-2023, entry version 15.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
DE   Flags: Fragment;
GN   ORFNames=DMB66_33910 {ECO:0000313|EMBL:RSM56565.1};
OS   Actinoplanes sp. ATCC 53533.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Actinoplanes.
OX   NCBI_TaxID=1288362 {ECO:0000313|EMBL:RSM56565.1, ECO:0000313|Proteomes:UP000287606};
RN   [1] {ECO:0000313|EMBL:RSM56565.1, ECO:0000313|Proteomes:UP000287606}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 53533 {ECO:0000313|EMBL:RSM56565.1,
RC   ECO:0000313|Proteomes:UP000287606};
RA   Waglechner N., Wright G.D.;
RT   "Evolution of GPA BGCs.";
RL   Submitted (MAY-2018) 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:RSM56565.1}.
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DR   EMBL; QHHV01000117; RSM56565.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A428XMM8; -.
DR   OrthoDB; 9810730at2; -.
DR   Proteomes; UP000287606; 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; 1.
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; -; 1.
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; PF18947; HAMP_2; 1.
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; 1.
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   PROSITE; PS50885; HAMP; 1.
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:RSM56565.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000287606};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          22..74
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          318..551
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          607..724
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          48..75
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COILED          239..308
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         657
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:RSM56565.1"
SQ   SEQUENCE   738 AA;  79890 MW;  DF38C41BD93808D7 CRC64;
     AEVKGVSGTW RDLTDNVNQL ASTLTTQLRA IAEVSTSVTR GDLTQSVAVE AQGEVAELKD
     NINQMIVTLR ETTKANAEQG WLDSNLARIG GLLQGQRDLG EVCRMIMTEV TPLVDAQLGA
     FFMVDHEEAV MRLRLAASYG YVARNHEVTF GPGEALVGQA AVSRRTIRVR AAHDGALTMR
     SGLMSMPPSD LVVLPVLFEG EMLGVIEFAS VAAFSGLHLT FLERLVAAIG VALNTIQANR
     RTEELLAQSQ RLAREMQDQS AELQRTNAEL EDKAQLLSEQ KGNIETKNRE IELARLGLEE
     KAQQLSRASA YKTEFLANMS HELRTPLNSL LLLARLLADN SEHNLTEKQI EFARTIHSAG
     SDLLSLIDDI LDLSKIEAGR MDVEPDQVDF DGVRSYVEQA FTPQADEKGL EFRVEVSDDL
     PESIVTDAQR LQQILRNLLS NAVKFTDNGS VTLRIHPAPP EADFGIPALA AARQVVAFAV
     SDTGIGISDE KLSLIFEAFQ QADGTTSRKY GGTGLGLSIS REFAALLGGT ILVSSSPGAG
     STFTLYMPDA LVGDAIPVPS MPQLPASHSA GEPRRALSSL DLPLITARPE LETHTVSPAS
     RQLDGATVLI VDDDVRNVFA LTSALEMHGL NVLYSDNGVD GVRLLAEHPE VDIVLMDAMM
     PEQDGYETTR GIRRNQRFAD LPVVFLTAKA MPGDRESALA AGASDYITKP VDLDELIELM
     ARWVNASDNS GTESQNGG
//
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