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
//