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Database: UniProt
Entry: A0A010ZVN6_9ACTN
LinkDB: A0A010ZVN6_9ACTN
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ID   A0A010ZVN6_9ACTN        Unreviewed;       545 AA.
AC   A0A010ZVN6;
DT   11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT   11-JUN-2014, sequence version 1.
DT   27-MAR-2024, entry version 46.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=CryarDRAFT_2356 {ECO:0000313|EMBL:EXG81247.1};
OS   Cryptosporangium arvum DSM 44712.
OC   Bacteria; Actinomycetota; Actinomycetes; Cryptosporangiales;
OC   Cryptosporangiaceae; Cryptosporangium.
OX   NCBI_TaxID=927661 {ECO:0000313|EMBL:EXG81247.1, ECO:0000313|Proteomes:UP000021053};
RN   [1] {ECO:0000313|EMBL:EXG81247.1, ECO:0000313|Proteomes:UP000021053}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44712 {ECO:0000313|EMBL:EXG81247.1,
RC   ECO:0000313|Proteomes:UP000021053};
RG   DOE Joint Genome Institute;
RA   Eisen J., Huntemann M., Han J., Chen A., Kyrpides N., Mavromatis K.,
RA   Markowitz V., Palaniappan K., Ivanova N., Schaumberg A., Pati A.,
RA   Liolios K., Nordberg H.P., Cantor M.N., Hua S.X., Woyke T.;
RL   Submitted (JUL-2013) 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:EXG81247.1}.
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DR   EMBL; JFBT01000001; EXG81247.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A010ZVN6; -.
DR   PATRIC; fig|927661.3.peg.2320; -.
DR   HOGENOM; CLU_020211_11_1_11; -.
DR   OrthoDB; 9792686at2; -.
DR   Proteomes; UP000021053; 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   Gene3D; 1.10.287.130; -; 1.
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; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR033463; sCache_3.
DR   InterPro; IPR029151; Sensor-like_sf.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR016120; Sig_transdc_His_kin_SpoOB.
DR   InterPro; IPR039506; SPOB_a.
DR   PANTHER; PTHR45436:SF5; SENSOR HISTIDINE KINASE TRCS; 1.
DR   PANTHER; PTHR45436; SENSOR HISTIDINE KINASE YKOH; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF17203; sCache_3_2; 1.
DR   Pfam; PF14689; SPOB_a; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 1.
DR   SUPFAM; SSF103190; Sensory domain-like; 1.
DR   SUPFAM; SSF55890; Sporulation response regulatory protein Spo0B; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:EXG81247.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000021053};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius};
KW   Two-component regulatory system {ECO:0000256|ARBA:ARBA00023012}.
FT   TRANSMEM        179..198
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          336..532
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
SQ   SEQUENCE   545 AA;  57857 MW;  E4F11B062AAA6CF4 CRC64;
     MVVTSRRSTL AGQLLALQLV VIVVVLVAIA ALSVAQSAAT FDRVEGRRVA ALAEQLADNP
     LVRTQLGEPA PGETLAPLVQ TIRTQSGVTS VTIADADGIV VSSTDPLLTR GRLPLGSAGV
     ADGRSWSGEL RLNGSLELVA QVPVLGAEPQ NLGRQLGVVV IGEASPTLQQ RALDASSHLA
     IYLGLASVVG LLGSWLLARR IKRQTLGLEP REIAGLAEHR EAMLYGIAEG VIALDPHDRV
     TLVNAVGLRL LDLPEECVGA TLTELGVEGR LGEVLTGGAR DEVVLRRGRV LVLNRMSVTK
     DGRRLGSVTT LRDRTELAQL EREMGSFRSS TELLRAQAHE FANQLHTISG LIQIGEYDEV
     VQYVEALADH RESLDLTLTS RIHDTAVAAL LMAKSAQAAE RRVRLRVSER TGLGRLEAED
     AADIATVVGN LVDNALDAAA VADAGDDAWV EVELRHDTST VEIVVRDSGP GIAPELAQEV
     FTRGFTTKAA EGGERGIGLA LTRLVCKRHG GEVSVANTPD GAMFVARLTV GRPMEPVDAR
     ERVDA
//
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