ID A0A132MTY7_9ACTN Unreviewed; 1118 AA.
AC A0A132MTY7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 34.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=LI90_2396 {ECO:0000313|EMBL:KWX01368.1};
OS Carbonactinospora thermoautotrophica.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Carbonactinosporaceae; Carbonactinospora.
OX NCBI_TaxID=1469144 {ECO:0000313|EMBL:KWX01368.1, ECO:0000313|Proteomes:UP000070188};
RN [1] {ECO:0000313|Proteomes:UP000070188}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H1 {ECO:0000313|Proteomes:UP000070188};
RA MacKellar D.C., Lieber L., Norman J., Bolger A., Tobin C., Murray J.W.,
RA Chang R., Ford T., Nguyen P.Q., Woodward J., Permingeat H., Joshi N.S.,
RA Silver P.A., Usadel B., Rutherford A.W., Friesen M., Prell J.;
RT "Physiological reanalysis, assessment of diazotrophy, and genome sequences
RT of multiple isolates of Streptomyces thermoautotrophicus.";
RL Submitted (APR-2015) 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:KWX01368.1}.
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DR EMBL; LAXD01000001; KWX01368.1; -; Genomic_DNA.
DR RefSeq; WP_066887811.1; NZ_LAXD01000001.1.
DR AlphaFoldDB; A0A132MTY7; -.
DR STRING; 1469144.LI90_2396; -.
DR PATRIC; fig|1469144.10.peg.2597; -.
DR OrthoDB; 4652229at2; -.
DR Proteomes; UP000070188; 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 InterPro; IPR013587; Nitrate/nitrite_sensing.
DR InterPro; IPR010910; Nitrate/nitrite_sensing_bac.
DR PANTHER; PTHR44936; SENSOR PROTEIN CREC; 1.
DR PANTHER; PTHR44936:SF12; SENSOR PROTEIN CREC; 1.
DR Pfam; PF00672; HAMP; 1.
DR Pfam; PF02518; HATPase_c; 1.
DR Pfam; PF08376; NIT; 1.
DR SMART; SM00304; HAMP; 1.
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.
DR PROSITE; PS50906; NIT; 1.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KWX01368.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000070188};
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 46..66
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 367..389
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 86..359
FT /note="NIT"
FT /evidence="ECO:0000259|PROSITE:PS50906"
FT DOMAIN 390..460
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 577..683
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 691..933
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 949..1021
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1033..1118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 693..713
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..808
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 823..837
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 890..918
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 988..1003
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1088..1102
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1118 AA; 120754 MW; EB6A8ED9FABB2F1E CRC64;
MFREATEAPG SQAAKSHERE ARQVSPRFER LRDRFLLRHQ RVHTRLLALI LLPLLVAVVS
SAVNVAHSWQ DRNRLAGVQK LTVLVRDIGI LVHHLEEERD HTAVYIAKGR RGDVDSVTKY
QEAADSAVDE VREAASEIDG SFDPSVRRVV QTVRDRLDNL PALREATVQS RMRTEDAVAM
YTSFIKDLLD TSVQLSESAT EASLGRSARA IAAFTRLKEL TSRERALLMD PAINHRFDPI
DYQNFLVVHA ERQSVRAEFL RSASPRQRQY LEDGVTGPEV DSAEGVIQQA TLSPVFLAPQ
QAAGDNAARQ QAAEDKTPAA VAPKIDADLL FRSLQTELRL MYSAEQRLVH DLEQEIAAKK
DAAQRNALLT IVIVLISLLL TIAATLYVAR SMAGPLLRLR RAAQEIANER LPNRVRELNE
SDPHKVDLTV EPIDITSRDE IGEVARAFDE VHREAVRLAS EQALLRSSVN AMFVNLSRRT
QSLVQRQLKL IDELERSERD PDQLANLFKL DHLATRMRRN GENLLILAGE EPGRRWNQPI
PLIDILRAAA SEVEQYERVQ VSNVPSVDVV GRAVNDLVHL IAELLENATS YSAPGTKVWV
SAQTLPGGGV MVEIEDNGIG MSPDELADAN RRLAEPPAID VSVSRRMGLF VVGRLAARNN
LRVRLRSSAG GGVTALVTIP AELIADPTRL TALGTPDTGS APVSDTSPVA EGPSASERLS
PRRAMPEASG ILIPRQVTAG ELGRRRPALP SGRATPPHSP PVGVDLSSIS GPRHASGRRS
VGPAQGADGR PGRSGSAQPT QDQPTPASGA ATPGDPRDQA GAPGWPVVPP PGAPFGYPIR
LADPGAADQR PGVPQPAEPA PVEGTRPAEQ PAGEADATPL AGLRPVPPGA PEDDARENTP
EDDARENTAV RLRPAPKEPD ILDPSTPLEG VRVERLPIFE AIESEWFRRR TGPKAIPAGE
NGVVPLPATP PAGSPTPDAG TRADQPQEAV AQVEQSTPAV SPPPVEEQES PPWRSAADEG
WKAAEMISKP IASGLTPAGL PKRIPKANLV PGSAGGPDQI KKVRANPAAR SPEAVRGRLA
SYHQGIRRGR LAGRELRERS RGTLPDLPAV SSDEQENS
//
