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Database: UniProt
Entry: A0A0F7CQ87_9ACTN
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ID   A0A0F7CQ87_9ACTN        Unreviewed;       869 AA.
AC   A0A0F7CQ87;
DT   22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT   22-JUL-2015, sequence version 1.
DT   24-JAN-2024, entry version 42.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SXIM_45970 {ECO:0000313|EMBL:AKG45981.1};
OS   Streptomyces xiamenensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=408015 {ECO:0000313|EMBL:AKG45981.1, ECO:0000313|Proteomes:UP000034034};
RN   [1] {ECO:0000313|Proteomes:UP000034034}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCCC 1A01550 {ECO:0000313|Proteomes:UP000034034};
RA   Xu J.;
RT   "Complete genome sequence of a mangrove-derived Streptomyces xiamenensis.";
RL   Submitted (FEB-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}.
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DR   EMBL; CP009922; AKG45981.1; -; Genomic_DNA.
DR   RefSeq; WP_046725002.1; NZ_CP009922.3.
DR   AlphaFoldDB; A0A0F7CQ87; -.
DR   STRING; 408015.SXIM_45970; -.
DR   KEGG; sxi:SXIM_45970; -.
DR   PATRIC; fig|408015.6.peg.4652; -.
DR   HOGENOM; CLU_000445_113_1_11; -.
DR   Proteomes; UP000034034; Chromosome.
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:AKG45981.1};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
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        410..439
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        459..480
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          626..837
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   REGION          836..869
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   869 AA;  92985 MW;  AF2513DED30B3C72 CRC64;
     MARRGTLRIY LGAAPGVGKT YAMLSEAHRR AERGTDIVVG FVETHDRPRT EALLRGLETV
     PRRPPPGAGR GEMDTEAVLR RAPAVACVDE LAHSNAPGSR HDKRWRDIDT LLDAGIDVIS
     TVNIQHLESL ADVVAAITGV RQRETVPDAV VRRADQIELV DMTPEALRRR MAHGNIYAPD
     KVDAALSHYF RPGNLTALRE LALLWTADRV DAYLQRYRTE QGIRSTWYAR ERIVVALTGG
     PEGSTLIRRA ARMAAKSSGG EILAVHVSRA DRLTAVSPRE LASQRTLVEQ LGGTFHHVIG
     DDISSALLDF ARGVNANQIV LGSSRRKTWQ YAFGPGVGAS VARDSGPDLD VHIVTHAEVA
     RGRGLPNARG ARLGRSRTVA GWLIGLAGPP LLTVLLAAPP RPLAEFASDV LLFLSVTVLA
     ALVGGFYPGL VSAALATLLL DYFFTEPLRE WGVGSGHDVI TVVIFFAIAL AVASVVDMSA
     QRTQQAARLR AESETLTVLA GSVLRGEDTL RALLGRARET FGMDCAALLE RDHDGGRWRC
     VGSVSAIADN PRPLLRPQDA DVDVPVGEHT MLVLSGRVLP AEDRRVLSAF AAQAATILDR
     QRLLTEAARA HKLAEGNRIR TALLAAVSHD LRTPLAAIKA SVSSLRSDDV EWSPQDRAGL
     LESIEDGADR LDQLVGNLLD MSRLHTGTVR PLIRRTGLDE VVLRALAGVP VDVVDLDVPE
     SLPWVAADPG LLERSVANIV ENAVKYRPPD TRVLVRGSAL GNQVELRVVD RGPGVPDADK
     GRIFEPFQRH GDIPRGNGVG LGLAVARGFT EAMGGTLDAE DTPGGGMTMV LTLPTDIPAP
     AAAGAGAPAE RESEQGEQGG AHAPGTRGR
//
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