ID A0A0C2FKN6_9ACTN Unreviewed; 516 AA.
AC A0A0C2FKN6;
DT 01-APR-2015, integrated into UniProtKB/TrEMBL.
DT 01-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 39.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=LP52_04510 {ECO:0000313|EMBL:KIH99889.1};
OS Streptomonospora alba.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Streptomonospora.
OX NCBI_TaxID=183763 {ECO:0000313|EMBL:KIH99889.1, ECO:0000313|Proteomes:UP000031675};
RN [1] {ECO:0000313|Proteomes:UP000031675}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YIM 90003 {ECO:0000313|Proteomes:UP000031675};
RX PubMed=25601074; DOI=10.1016/j.chembiol.2014.11.017;
RA Metelev M., Tietz J.I., Melby J.O., Blair P.M., Zhu L., Livnat I.,
RA Severinov K., Mitchell D.A.;
RT "Structure, bioactivity, and resistance mechanism of streptomonomicin, an
RT unusual lasso Peptide from an understudied halophilic actinomycete.";
RL Chem. Biol. 22:241-250(2015).
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:KIH99889.1}.
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DR EMBL; JROO01000007; KIH99889.1; -; Genomic_DNA.
DR RefSeq; WP_040271030.1; NZ_JROO01000007.1.
DR AlphaFoldDB; A0A0C2FKN6; -.
DR STRING; 183763.LP52_04510; -.
DR OrthoDB; 9767435at2; -.
DR Proteomes; UP000031675; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:InterPro.
DR Gene3D; 3.30.450.280; GAF domain; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 1.
DR InterPro; IPR038424; H_kinase_PdtaS_GAF_sf.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR022066; PdtaS_GAF.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR011495; Sig_transdc_His_kin_sub2_dim/P.
DR InterPro; IPR011102; Sig_transdc_His_kinase_HWE.
DR PANTHER; PTHR43065; SENSOR HISTIDINE KINASE; 1.
DR PANTHER; PTHR43065:SF23; SENSOR HISTIDINE KINASE PDTAS-RELATED; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF07568; HisKA_2; 1.
DR Pfam; PF12282; PdtaS_GAF; 1.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00911; HWE_HK; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Kinase {ECO:0000256|ARBA:ARBA00022777};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000031675};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 308..510
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
SQ SEQUENCE 516 AA; 56351 MW; 2D2AC281F36C4C87 CRC64;
MPHLSDLIRR YTALKTADLE WFHSLVSDWQ LLADLSFADL VLWVRLRDDS GWVAVSQMRP
TTGPTAFQDD LVETVLRDGA AEPPGDSAPS RLSGRHTLID RAWDEGRICR EGDPDWSGGV
PVREETIPVR RDGKLIGVIQ RSTNLSSART PSRLELTYLQ SASDLAQMIS EGAFPFNDQG
PLMVRSPRVG DGLLRLDQNG EVVYASPNAL SAYRRLGLTA DLVGARLDRT TLDLAALGDA
RDESLTWTAG GRVPQEAEVE GRGSTIQLRS IPLVVGGVRI GALVMVRDVT ELRRRERELM
TKNATIREIH HRVKNNLQTV AALLRLQSRR LGVPEGRAAL DEAVRRVGSI AIVHEMLSHT
PDEVVDFDDI ADRVIEMAAE ISSTEGPVMP RRTGQFGLLS ALVATPLSMV LAELVQNAVE
HGLRYGPGSI EVRAHRHDAP SGQEENGGRL VVEVTDDGGG LPPDFDVEST ASLGLQIVRT
LITSELGGSL EIKPQERGGT KVAIELPVER SFEPYA
//
