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Database: UniProt
Entry: A0A1H6E6Q1_9ACTN
LinkDB: A0A1H6E6Q1_9ACTN
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ID   A0A1H6E6Q1_9ACTN        Unreviewed;       823 AA.
AC   A0A1H6E6Q1;
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=SAMN04489712_13452 {ECO:0000313|EMBL:SEG92624.1};
OS   Thermomonospora echinospora.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Thermomonosporaceae; Thermomonospora.
OX   NCBI_TaxID=1992 {ECO:0000313|EMBL:SEG92624.1, ECO:0000313|Proteomes:UP000236723};
RN   [1] {ECO:0000313|Proteomes:UP000236723}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 43163 {ECO:0000313|Proteomes:UP000236723};
RA   Varghese N., Submissions S.;
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; FNVO01000034; SEG92624.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1H6E6Q1; -.
DR   Proteomes; UP000236723; 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; 2.
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; -; 2.
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; 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; 2.
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; 1.
DR   PROSITE; PS50885; HAMP; 2.
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:SEG92624.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000236723};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          20..72
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          112..164
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          416..649
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          700..817
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          649..673
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          330..385
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   COMPBIAS        651..665
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         750
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   823 AA;  89042 MW;  8DBB92FED6958727 CRC64;
     MRGVSGVWKD LTNNVNGMAS NLTYQVRNIA QVTTAVAHGD LTKKIDVDAR GEILELKTTI
     NTMVDTLSAF SSEVTRVARE VGSEGRLGGQ AKVEGVYGTW KRLTENVNEL ASNLTTQVRA
     IAEVTSAVAS GDLSREITVE AAGEVAELKD NVNLMVATLR ETTHANQEQD WLKSNLARIG
     GLLQGHRDMT QMAQLIMSEL TPTASADYGA FYLARPNGDG ETELALIAGY GVRPTPDGTS
     FRLGEGLVGQ AALERRMILI DNAPPGYVTI RSGLGQASAT HVIVLPVLFE DQVLGAIELA
     SFGGFTATHL AFFDQFAETL GVTINAISAN SRTEALLTES QRLAQELQER SDELQRQQAE
     LRRSNAELED KAALLAKQNR AIEIQNFQIE QARRTLEERA EQLALSSRYK SEFLANMSHE
     LRTPLNSLLV LAKLLSENPE GNLSAKQVEF ARTIHDSGTD LLQLINDILD LSKVEAGKME
     VHPQPLAFTK LVDYVDATFR PMAVDKGLAF GIEVAPDVPG LLYADEQRLQ QVLRNLLSNA
     VKFTSEGEVK LTIAPAGNDE EFSAPGLREA PLVIGFEVSD TGIGISEDKL QVIFEAFQQA
     DGTTSRRYGG TGLGLSISRN IAHLLGGEIH ARSQLGRGSR FTLYLPAQYQ GAGSPPPPAE
     VEPPVSSGRP APEAAAGPAL AEFLEEPPAD HLDAVLSGRK VLIVDDDVRN VFALTSVLEG
     YGMDVLYAED GQAGIDLLQR NPDVALVLMD VMMPGLDGYA TTEAIRGMPQ FTDLPIIVIT
     AKVMKGDREK SLASGASDYV PKPVDVDHLL DLMRTWLQRA TVR
//
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