ID A0A370I7F6_9NOCA Unreviewed; 1093 AA.
AC A0A370I7F6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-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=DFR76_104416 {ECO:0000313|EMBL:RDI66666.1};
OS Nocardia pseudobrasiliensis.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Nocardia.
OX NCBI_TaxID=45979 {ECO:0000313|EMBL:RDI66666.1, ECO:0000313|Proteomes:UP000254869};
RN [1] {ECO:0000313|EMBL:RDI66666.1, ECO:0000313|Proteomes:UP000254869}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44290 {ECO:0000313|EMBL:RDI66666.1,
RC ECO:0000313|Proteomes:UP000254869};
RA Goeker M.;
RT "Genomic Encyclopedia of Type Strains, Phase IV (KMG-IV): sequencing the
RT most valuable type-strain genomes for metagenomic binning, comparative
RT biology and taxonomic classification.";
RL Submitted (JUL-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:RDI66666.1}.
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DR EMBL; QQBC01000004; RDI66666.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370I7F6; -.
DR STRING; 1210086.GCA_001613105_01613; -.
DR Proteomes; UP000254869; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0007165; P:signal transduction; IEA:InterPro.
DR CDD; cd06225; HAMP; 1.
DR Gene3D; 6.10.340.10; -; 1.
DR Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR InterPro; IPR003660; HAMP_dom.
DR InterPro; IPR003594; HATPase_C.
DR InterPro; IPR036890; HATPase_C_sf.
DR InterPro; IPR005467; His_kinase_dom.
DR PANTHER; PTHR44936; SENSOR PROTEIN CREC; 1.
DR PANTHER; PTHR44936:SF12; SENSOR PROTEIN CREC; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR SMART; SM00304; HAMP; 2.
DR SMART; SM00387; HATPase_c; 1.
DR SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR PROSITE; PS50885; HAMP; 1.
DR PROSITE; PS50109; HIS_KIN; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:RDI66666.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000254869};
KW Transferase {ECO:0000256|ARBA:ARBA00022679};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 20..38
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 292..314
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 315..382
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 499..609
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 650..694
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 709..986
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1002..1093
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 723..737
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 767..792
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..854
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 866..885
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 940..954
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 970..986
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1093 AA; 117149 MW; 3483DD9E4B5B8E0C CRC64;
MGTAPRPWQR SLSNLSVTSK VGIVLLLPVL LASTFAVLRI KDELGRIAQL DTASEQARII
RPTLAFAGAA DQLAVVASGD RVTDSALDQA ATRFDQAAAE LQSTLKVTDG EQRALAELNQ
ALEAGRTLRN NPRANTAIGQ QADEVSRHVS TALTALPTPQ DATIEHYFDQ LGAVTAARRQ
FIQQQLLITG AEIGNNPSTL ARVLTAAGAE QTMINQYVQV APDTAVKPEA LLGALQTRLG
ALSQNAIEPI AVPGVADSMR ISADAYTQAT DQLAAQIDSG LSRRSIDART NVLRDVALVV
VTLLIGLALA LAVARSLVVP VRRLRRDALQ VAHTDLPAEL AVVREGGATP DIVPVDVDTT
EEIGQLARAV DDMHRQALHL AAEQARLRLQ IGNMFETLSR RSQSLVEQQL GLIEDLERDE
DDSERLQSLF RLDHLATRMR RNGDNLLVLA GTALRRGMLP PTPLSDMLWS AVSQVEDYQR
VEIGTVPDGI VAGEPAVDIE HLLAELIDNS LRYSPPNTPV AVSVTRAVDG GYLIEITDRG
LGMSSEDLRA INERLASGGE VTVETARRMG LFVVGRLAKR HTVTVSLRRT ASAGQQAGIT
ASVHLPSALV SPLPESTTGP QPIIAPFPSP IGPAPLSVVP DAEATGLFAR PQLELPQRRP
GEAADFGPPI PADDLFTPYA QDDAPQPSLT DGLFTHRSTG ELFTHRESAH PDATVGHLNL
PPDEFPADDE DRATTGADHF TAWDSPDDSA DDAPAQPDPR WPQNPPAEDE SAQQEWQPSE
DPPPQDSDPS ESAAQRGEWP RTDGLPQRVS HPSDNAAPHS EWPRTDGLPQ RVSHSSADAA
PHSEWRRTDD PPQRVSHPSD NAAPHGEWPR TDDLPDSDRT DDTRGEWAGA SAGFSDRDSG
ALEDGYAREW SSADDSLPQR DPNPDEDRYT YAEPVYTQDD TRFGRGDSEP DAPHDSGQPV
DIWAETAVYP SQQPEESAAS ATAPVPQGTP IYQRMVSEWL VEPSSSGPAN GWSSPADAGW
AAAAEASSPT SARQTEGGLP IRRPGAQLVP GGLTATTRSG APDPEEIRTN LSRHLSGVRS
GRADAQHYDG GSA
//
