ID A0A239K630_9ACTN Unreviewed; 1096 AA.
AC A0A239K630;
DT 25-OCT-2017, integrated into UniProtKB/TrEMBL.
DT 25-OCT-2017, sequence version 1.
DT 24-JAN-2024, entry version 19.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=SAMN06264365_14311 {ECO:0000313|EMBL:SNT13410.1};
OS Actinoplanes regularis.
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=52697 {ECO:0000313|EMBL:SNT13410.1, ECO:0000313|Proteomes:UP000198415};
RN [1] {ECO:0000313|EMBL:SNT13410.1, ECO:0000313|Proteomes:UP000198415}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 43151 {ECO:0000313|EMBL:SNT13410.1,
RC ECO:0000313|Proteomes:UP000198415};
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};
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-
CC pass membrane protein {ECO:0000256|ARBA:ARBA00004141}.
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DR EMBL; FZNR01000043; SNT13410.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A239K630; -.
DR Proteomes; UP000198415; Unassembled WGS sequence.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-KW.
DR GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR CDD; cd00082; HisKA; 1.
DR CDD; cd00130; PAS; 2.
DR CDD; cd00156; REC; 1.
DR CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR Gene3D; 1.10.287.130; -; 1.
DR Gene3D; 3.40.50.2300; -; 2.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR Gene3D; 3.30.450.20; PAS domain; 2.
DR InterPro; IPR011006; CheY-like_superfamily.
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; IPR007895; MASE1.
DR InterPro; IPR001610; PAC.
DR InterPro; IPR000014; PAS.
DR InterPro; IPR000700; PAS-assoc_C.
DR InterPro; IPR035965; PAS-like_dom_sf.
DR InterPro; IPR013656; PAS_4.
DR InterPro; IPR013655; PAS_fold_3.
DR InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR NCBIfam; TIGR00229; sensory_box; 2.
DR PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF00512; HisKA; 1.
DR Pfam; PF05231; MASE1; 1.
DR Pfam; PF08447; PAS_3; 1.
DR Pfam; PF08448; PAS_4; 1.
DR Pfam; PF00072; Response_reg; 2.
DR PRINTS; PR00344; BCTRLSENSOR.
DR SMART; SM00387; HATPase_c; 1.
DR SMART; SM00388; HisKA; 1.
DR SMART; SM00086; PAC; 2.
DR SMART; SM00091; PAS; 2.
DR SMART; SM00448; REC; 2.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR SUPFAM; SSF52172; CheY-like; 2.
DR SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR PROSITE; PS50109; HIS_KIN; 1.
DR PROSITE; PS50113; PAC; 1.
DR PROSITE; PS50112; PAS; 2.
DR PROSITE; PS50110; RESPONSE_REGULATORY; 2.
PE 4: Predicted;
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000198415};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW ECO:0000256|SAM:Phobius}.
FT TRANSMEM 20..46
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 53..72
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 78..96
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 117..139
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 151..171
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 183..205
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 217..234
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 239..259
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 299..369
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 371..423
FT /note="PAC"
FT /evidence="ECO:0000259|PROSITE:PS50113"
FT DOMAIN 417..487
FT /note="PAS"
FT /evidence="ECO:0000259|PROSITE:PS50112"
FT DOMAIN 557..782
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 799..919
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT DOMAIN 936..1052
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1054..1096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1096
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 853
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
FT MOD_RES 985
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1096 AA; 118205 MW; AD44D161FFC01392 CRC64;
MKTVVTVSLF LVGYVVLQQI GLWLVVSAVE LAVFWPVLGF AMAVLARVPV RMWPVYVGLL
SVATLVGNIL NGNTVPGSVI YALANALQVV GGAVLVRRAR ANGEECGFGT TSWITRALLP
AALLPPAAAA LVATTTVMID SGVAASAGLF WWLWFSSGAL GVLAMLPVVE ACSGIGWQHR
WSALRLVEGL LVVVVEAALL VKVFAAEGDG PYQTWQWPFV LLPAVLWAAV RFGLRFTTVF
AAALTTAVVG GTAGGYGPFA QQASMNDRML SVQGFCVVMF LSSQVIAHAI ATRETAERTL
RERSEAMSLA VEGIAFIDPQ GRYVRVNPAY AASLGNIPEQ LVGQSWESTV HPDDVPALRA
AYETMLREGK ATVTARGVRR DGTIFFQEIT MITQSDADGR PTGHHCFVRD ITQRQSAEQR
VSQFFALSQD LLCMLGSDGY FKRVNPAWTE TLGYTEHELL SRTYTDFIHP DDREATLAQL
AKTVSNAATN PLFDNRYRCK DGSYRWLRWT SSIDEVDKML YGVARDVTEA KETERAMALA
RDQALETARM KTQFVATMSH EIRTPMNGVI GLADLLERTT LTEKQRRYVD GIRTAGSGLL
DIINDILDYS KIESGKIVLE ESDFDLARLI GDTAALLGDS ARRKNLYLNV EVDPALPSGL
HGDPGRLRQI LLNLIGNAIK FTERGGVTVR AEAVAQPAGV APGQFMLAMS VRDTGIGMDK
ATQSRIFEPF RQADASTTRV YGGTGLGLAI TRQLAHAMGG DVTVDSGPGL GATFTVTVLL
TTAAGDTAHV DPLARSALRI LVVDDNEINQ FILNDNLEQW GMRSESVSSA HEALALLRDE
AANGRRFDLA IIDMHMPMMD GLQLSMAISQ HAEIPATPII LFTSGDQITK DEAARAGIRA
SLTKPVDHST LLDTLIGITG SPQSISAPLD KHGAGRILLV EDNDINQIVA ADLLDQLGYD
VDIAADGIEA IAKATENDYN AILMDCQMPR MDGYTATAGL RAQASTAAIP IIAMTADAFE
EGRERCIAAG MNDYLSKPIH ADELERTLTR WVHDEGAGEP ESPLPHDRHP GSTSTSTSTS
TSASVESRAS GKRSSN
//
