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Database: UniProt
Entry: A0A124H3B8_9ACTN
LinkDB: A0A124H3B8_9ACTN
Original site: A0A124H3B8_9ACTN 
ID   A0A124H3B8_9ACTN        Unreviewed;       857 AA.
AC   A0A124H3B8;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   24-JAN-2024, entry version 37.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=AQI70_14210 {ECO:0000313|EMBL:KUM77086.1};
OS   Streptomyces curacoi.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=146536 {ECO:0000313|EMBL:KUM77086.1, ECO:0000313|Proteomes:UP000054024};
RN   [1] {ECO:0000313|EMBL:KUM77086.1, ECO:0000313|Proteomes:UP000054024}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 40107 {ECO:0000313|EMBL:KUM77086.1,
RC   ECO:0000313|Proteomes:UP000054024};
RA   Ruckert C., Winkler A., Kalinowski J., Kampfer P., Glaeser S.;
RT   "Draft genome sequence of Streptomyces curacoi DSM 40107, type strain for
RT   the species Streptomyces curacoi.";
RL   Submitted (OCT-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   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}.
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:KUM77086.1}.
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DR   EMBL; LMWJ01000008; KUM77086.1; -; Genomic_DNA.
DR   RefSeq; WP_062148681.1; NZ_KQ947987.1.
DR   AlphaFoldDB; A0A124H3B8; -.
DR   STRING; 146536.AQI70_14210; -.
DR   OrthoDB; 9806130at2; -.
DR   Proteomes; UP000054024; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd00075; HATPase; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd01987; USP_OKCHK; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 1.20.120.620; Backbone structure of the membrane domain of e. Coli histidine kinase receptor kdpd; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR   InterPro; IPR003594; HATPase_C.
DR   InterPro; IPR036890; HATPase_C_sf.
DR   InterPro; IPR005467; His_kinase_dom.
DR   InterPro; IPR003661; HisK_dim/P.
DR   InterPro; IPR036097; HisK_dim/P_sf.
DR   InterPro; IPR038318; KdpD_sf.
DR   InterPro; IPR025201; KdpD_TM.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR003852; Sig_transdc_His_kinase_KdpD_N.
DR   InterPro; IPR006016; UspA.
DR   PANTHER; PTHR45569; SENSOR PROTEIN KDPD; 1.
DR   PANTHER; PTHR45569:SF1; SENSOR PROTEIN KDPD; 1.
DR   Pfam; PF13493; DUF4118; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF02702; KdpD; 1.
DR   Pfam; PF00582; Usp; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SUPFAM; SSF52402; Adenine nucleotide alpha hydrolases-like; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   PROSITE; PS50109; HIS_KIN; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:KUM77086.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054024};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        379..398
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        430..453
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        459..480
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          622..833
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          832..857
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   857 AA;  92076 MW;  8FCE71C7E6877460 CRC64;
     MGRGKLRIYL GAAPGVGKTY AMLSEAHRRV ERGTDCVVAF VEHHGRPRTE VMLHGLEQIR
     RKELEYRGAF FTEMDVDAVL ARRPQVALVD ELAHTNVPGS RNAKRWQDVA ELLAAGIDVI
     STVNIQHLES LGDVVESITG VRQRETVPDE VVRRADQVEL VDMSPQALRR RMAHGNIYEP
     DKVDAALSNY FRPGNLTALR ELALLWVADR VDEYLKQYRS DHRVSTIWGS RERIVVGLTG
     GPEGRTLIRR AARLAEKGAG GEVLAVYIAR SDGLTSASPK ELAVQRTLVE DLGGTFHHVL
     GDDIPAALLA FARGANATQI VLGSSRRKSW QYVFGPGVGA TVARDSGPDL DVHIVTHEEA
     AKGRGLPVAR GARLGRSRIL WGWLTGVGGP LLLTLLLTHT AVDLGLANDM LLFLTLTVAA
     ALLGGRYPAL ASAAVGSMLL NWYFTAPVHH ITIADPKNLL ALVIFVFVAV AVASVVDLAA
     RRTHQAARLR AESEILSFLA GNVLRGETGL EELLERVRET FGMQSAALLE RESDLDPWTC
     AGRVGTGHAP ARPEDADVDV PVGDHMALAL TGRVLPAEDR RVLAAFAAQS AVVLDRQRLQ
     READQAKELA EGNRIRTALL AAVSHDLRTP LAGIKAAVSS LRSDDVAWSE EDEAELLEGI
     EEGADRLDHL VGNLLDMSRL QTGTVTPLIR EIDLDEVVPM ALGGVPEGSV ELDVPESLPM
     VAVDPGLLER SVANLVENAV KYGPGDSAVL VSASAIADRV EVRVVDRGRG VPDEAKERIF
     EPFQRYGDAP RGAGVGLGLA VARGFAEAMG GTLNAEDTPG GGLTMVLTLR AAGPGPELQE
     GAASTDRPVE PERQVTP
//
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