ID G8SCF1_ACTS5 Unreviewed; 1136 AA.
AC G8SCF1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=ACPL_8149 {ECO:0000313|EMBL:AEV89027.1};
OS Actinoplanes sp. (strain ATCC 31044 / CBS 674.73 / SE50/110).
OC Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC Micromonosporaceae; Actinoplanes.
OX NCBI_TaxID=134676 {ECO:0000313|EMBL:AEV89027.1, ECO:0000313|Proteomes:UP000005440};
RN [1] {ECO:0000313|Proteomes:UP000005440}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 31044 / CBS 674.73 / SE50/110
RC {ECO:0000313|Proteomes:UP000005440};
RA Schwientek P., Szczepanowski R., Kalinowski J., Klein A., Selber K.,
RA Wehmeier U.F., Stoye J., Puehler A.;
RT "The complete genome sequence of the acarbose producer Actinoplanes sp.
RT SE50/110.";
RL Submitted (DEC-2011) 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; CP003170; AEV89027.1; -; Genomic_DNA.
DR RefSeq; WP_014695082.1; NZ_LT827010.1.
DR AlphaFoldDB; G8SCF1; -.
DR STRING; 134676.ACPL_8149; -.
DR KEGG; ase:ACPL_8149; -.
DR PATRIC; fig|134676.3.peg.8080; -.
DR eggNOG; COG2205; Bacteria.
DR HOGENOM; CLU_008825_0_0_11; -.
DR OrthoDB; 4349881at2; -.
DR Proteomes; UP000005440; Chromosome.
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; IPR013587; Nitrate/nitrite_sensing.
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.
PE 4: Predicted;
KW Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:AEV89027.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Reference proteome {ECO:0000313|Proteomes:UP000005440};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:AEV89027.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius};
KW Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT TRANSMEM 309..331
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 332..403
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT REGION 787..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 813..839
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 840..854
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 906..920
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1003..1032
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1038..1054
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1056..1071
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1136 AA; 120698 MW; 3750D875E1DB7EC1 CRC64;
MLFGKFRILG KLALLVLVPL LGVLALTVPI IYNRVQAANE AQDTSDSVQL ATAVSSAVLE
LQEERLLSVG YTLHLVDEPT LVVQSAEAGE KVAELLDSKD RVLPADLRRA VLLATKLNST
RQNVLNGQTN ATSIVTDFTS VITPMIDGLG LSNHSDLTTK TGQQVFALER SMRSDDLISQ
ASCYLAYAAV LNQAPNRKLR SFAPQVLTLF NNSFAQIQSV ITQSKGYFTD AQYKLYLNTQ
DAFQSRVGSG FVDGLATNPA QALNKLPSIT SLFPSLQSVM VLGGFVEKRV AKDVDVAVTA
SRNSAIQQAL YVGGGAFVLL ILVVTLSIFM ARAVARPLRR LTASADRIAR AAEAELERVA
DDESEAQVRP IRLDPVDVEA QDEIGDLARA FDRVQTTAAR LVERQVLGRR NVAQMFGHVG
RRTQNLVGRQ LSLIDGLERR ETDSDRLREL YRLDHMSSRL RRNASALVVL SGGAGANEHM
APLPLSDVVR LALGEIEDYT RVEVDVPEEI VVVPAILADL TLLLAELLEN ATTFSPPHTS
VTVSADELRG GARLAIIDHG LGLQPERLAE ENARLTRRER LDLAPTEVLG LFVVGRLARR
HGIEVTLTDT PDGGVTAWID LSPQHLIARV ENLAAPGIPA PAAVPQIPMQ REPVAQQSYP
QQPFEQQYGQ PEYAVPVSGA LRGNTAEVAI ASTAIRTVPG SQQPFDPNKL SRATQTLESV
PSWNAFGGSV PAQPAVEDPY AGQPVYDAEP VYSPGVAYQE PSAPYRQVEA SQGYNSGIPV
AGRNPAALPE LPAAGQPAWG SDPALPAGPS WSGTPAPSET SWSVPESPAS GWNTPAPASP
SPAWNTPAPA SPAPAWNTPA AASAEPAWNT PAPAETHWNS PQQPAEPAWN TPAPAVEAPM
APASNSGHPA PAPEPTAPEP VVSSPAGGLK PLRRRVPGSQ LPMDSGPKQH AAAPSQDDAL
AARAAFDAFE QGVSRAHETS TSLPAPEFAG GQWAMPASLP EMPAPQWNVP APAPEAAPQW
STPAPAPEAA PQWSTPAPVQ EAAPQWNTPE PAQQWNAPAP AAPPAPAAPA PPLGGGGLTR
RVPGATLPRD EPHQPILPPA PTLMDPEQAR ALMDQFEYGV ALALNETQPQ PEGQPR
//
