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Database: UniProt
Entry: A0A1C5IA16_9ACTN
LinkDB: A0A1C5IA16_9ACTN
Original site: A0A1C5IA16_9ACTN 
ID   A0A1C5IA16_9ACTN        Unreviewed;      1064 AA.
AC   A0A1C5IA16;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-MAR-2024, entry version 28.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=GA0070614_2478 {ECO:0000313|EMBL:SCG55240.1};
OS   Micromonospora coxensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=356852 {ECO:0000313|EMBL:SCG55240.1, ECO:0000313|Proteomes:UP000198215};
RN   [1] {ECO:0000313|EMBL:SCG55240.1, ECO:0000313|Proteomes:UP000198215}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45161 {ECO:0000313|EMBL:SCG55240.1,
RC   ECO:0000313|Proteomes:UP000198215};
RA   Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL   Submitted (JUN-2016) 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; LT607753; SCG55240.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1C5IA16; -.
DR   OrthoDB; 4349881at2; -.
DR   Proteomes; UP000198215; Chromosome i.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004673; F:protein histidine kinase activity; IEA:UniProtKB-EC.
DR   Gene3D; 6.10.340.10; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR013587; Nitrate/nitrite_sensing.
DR   PANTHER; PTHR44936; SENSOR PROTEIN CREC; 1.
DR   PANTHER; PTHR44936:SF12; SENSOR PROTEIN CREC; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF08376; NIT; 1.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:SCG55240.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Transferase {ECO:0000313|EMBL:SCG55240.1};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        35..55
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        335..355
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          548..653
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          662..762
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          895..1064
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        670..684
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        735..754
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        910..924
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        941..962
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        991..1005
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1020..1035
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1064 AA;  112121 MW;  E486050FCD169050 CRC64;
     MSTGPTTLPE IGDTADRDRG RRLPRLRDAR IRSKLALILV VPVAAVIALA TIRLVSTGEG
     AVDATRLRSL TALSTDVSAL TQDLHKERMA AALYLANPQQ RVDDYNLRVR ATDQRITEYR
     AERNGIGEVP DSVRDQLEVI DDHLETLNGT RQKVLDRRQM PVAEATLRYG IVLTDLVSYG
     DTLAQLPGQE SLADARRAVA AFSRAKAAVA EEEAVAFTAL SGGRVDEEQF SAFVTTLTSQ
     QEALVSFSLA AAPDQRDLVE GTVSGDAVGL ADRVAADITR SVGQQPLVTA GDAVASIGAV
     NDLMRWAEIE LQDRLLRQAE DARNDVIRQA VVESVLVLLT LIIAVSLAVV LARSLNHSLR
     RLREGALSVA NHDLPDAVKR LQNMGSVGDG GVEEIVRQVR DPIRLPNRDE VGQVALAFNV
     VHREAVRVAA EQAALRTSVS AMFLNLARRS QTLVDRMIGE LDAIERSEED PKRLAQLFEL
     DHLATRMRRN DENLLVLAGA DSAVPRRDDA LLVDVLRAAQ SEVELYNRIE FGTVDTDISV
     AAHAVNDVVR LVAELLDNAT RFSPPTTTVV ADGRRIRDYV LIQVEDRGLG LTDEQLDSLN
     RRLAAPPSVD VAAFRLMGLA VVSRLASRYG IRVELRRNVE GGTVAQVTLP NSAVVLPAHR
     GRDSSLPRQR QPLAVEQTPL SSAGLGESAV GGRSGAATLT DSWRTTPPAP APWRPPVDAR
     DAAPTVGFGA PVSAAPSSSV PTSAVPTSAV PTSAVPASAP PAEPSYGFSV GTPTVANPVL
     DPLPKRAPAA EPAPALPLGP VAGASADPFA GSSASFAAPA VPYAAAPAAP AAPAAPAVPF
     GGAPTPVAPA APYTPPAAAP AAPVVARPER PADSPIFREM EAVWFRSHGD DATAIFTRPD
     FDGAPPEARQ DEAAPPPRPK LPTRVPSAPT AAGTPSVAPA APQPAATPPP SYAPPSVPTA
     PPAPSATSSA GGADAWRTAA DEGWTRATKA AEPSTGGTTR SGLPKRVPQA QLVPGGIEPK
     SGRDRSRRTP DEVRGLLSAY HRGVQRGRSA GTDQNSTSTK ETRR
//
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