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Database: UniProt
Entry: F3N9K7_9ACTN
LinkDB: F3N9K7_9ACTN
Original site: F3N9K7_9ACTN 
ID   F3N9K7_9ACTN            Unreviewed;      1389 AA.
AC   F3N9K7;
DT   28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT   28-JUN-2011, sequence version 1.
DT   27-MAR-2024, entry version 64.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=SGM_0041 {ECO:0000313|EMBL:EGG49701.1};
OS   Streptomyces griseoaurantiacus M045.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces; Streptomyces aurantiacus group.
OX   NCBI_TaxID=996637 {ECO:0000313|EMBL:EGG49701.1, ECO:0000313|Proteomes:UP000003022};
RN   [1] {ECO:0000313|EMBL:EGG49701.1, ECO:0000313|Proteomes:UP000003022}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=M045 {ECO:0000313|EMBL:EGG49701.1,
RC   ECO:0000313|Proteomes:UP000003022};
RX   PubMed=21551298; DOI=10.1128/JB.05053-11;
RA   Li F., Jiang P., Zheng H., Wang S., Zhao G., Qin S., Liu Z.;
RT   "Draft genome sequence of the marine bacterium Streptomyces
RT   griseoaurantiacus M045, which produces novel manumycin-type antibiotics
RT   with a pABA core component.";
RL   J. Bacteriol. 193:3417-3418(2011).
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:EGG49701.1}.
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DR   EMBL; AEYX01000001; EGG49701.1; -; Genomic_DNA.
DR   STRING; 996637.SGM_0041; -.
DR   eggNOG; COG0745; Bacteria.
DR   eggNOG; COG2172; Bacteria.
DR   eggNOG; COG2205; Bacteria.
DR   eggNOG; COG2208; Bacteria.
DR   Proteomes; UP000003022; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000155; F:phosphorelay sensor kinase activity; IEA:InterPro.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd16936; HATPase_RsbW-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd00130; PAS; 1.
DR   CDD; cd17574; REC_OmpR; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 3.30.565.10; Histidine kinase-like ATPase, C-terminal domain; 2.
DR   Gene3D; 3.30.450.20; PAS domain; 2.
DR   Gene3D; 3.60.40.10; PPM-type phosphatase domain; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR029016; GAF-like_dom_sf.
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; IPR000014; PAS.
DR   InterPro; IPR035965; PAS-like_dom_sf.
DR   InterPro; IPR013656; PAS_4.
DR   InterPro; IPR036457; PPM-type-like_dom_sf.
DR   InterPro; IPR001932; PPM-type_phosphatase-like_dom.
DR   InterPro; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   NCBIfam; TIGR00229; sensory_box; 1.
DR   PANTHER; PTHR43547:SF2; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE C; 1.
DR   PANTHER; PTHR43547; TWO-COMPONENT HISTIDINE KINASE; 1.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF13581; HATPase_c_2; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF08448; PAS_4; 2.
DR   Pfam; PF00072; Response_reg; 1.
DR   Pfam; PF07228; SpoIIE; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00091; PAS; 1.
DR   SMART; SM00331; PP2C_SIG; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 2.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF55785; PYP-like sensor domain (PAS domain); 2.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50112; PAS; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   Kinase {ECO:0000313|EMBL:EGG49701.1};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000003022};
KW   Transferase {ECO:0000313|EMBL:EGG49701.1}.
FT   DOMAIN          360..577
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          641..757
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   DOMAIN          773..808
FT                   /note="PAS"
FT                   /evidence="ECO:0000259|PROSITE:PS50112"
FT   MOD_RES         690
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1389 AA;  149619 MW;  F9515E5310986A27 CRC64;
     MERSGRSVSR PRAVGDGGVF AACQEVGGDL AEVDWAATPL GPPQEWPQSL QTAVSILLSS
     RFPMWMAWGE ELTFFCNAAY RRDTLGRKYP WALGRPASEV WSEIWGDIGP RIEAVLGTGR
     ATWDEALLLF LERSGYTEET YHTFSYSPLR DDAGEVVGML CVVNEDTERV IGERRMATLR
     DLGSDPSVIR TEQEVLAFVH RQLTRNLKDL PFTLTYLFDG DEARLAGTTG VTPGTPVAPR
     SLPVGGPGGV WPVGELAEGE TRGIPLAEAS FGPLPVGDWP ESPLQALVVP LLQQGGAPYG
     FLVAALNRYR DLDDHYRGFV ELTAGHIASG IGSARSYQAQ QRRAEELAEL DRAKTTFFSN
     ISHELRTPLT LIMGPVEELR TRLSGAGEEV HAELDVIHRN GLRLGKLVNT LLDFSRLEAG
     RMQARYEPVE LAAVTAELAS VFRSAVERAG LTLDVDCPAL DEPVYVDRAM WEKVVLNLLS
     NALKFTFEGA VRVRVRRSGP DAVVVVADTG TGVPEAEMPR LFERFHRIEN ARARSHEGSG
     IGLALVRELV GLHGGTIDAE STEGVGTTFT LRIPFGTAHL PADSVVSEPD GGAAGATADP
     YVHEAFRWLP ASEPAPADDG GPREVGAAAV VPGAGPAYSA RVLVADDNAD MREYLARLLT
     AAGYQVTEVT DGVEALAAAR RRTPDLVVSD VMMPRLDGLE LVSRLRADPR TASVPVVLLS
     ARAGQEASIE GLRAGADDYL VKPFAAAELL ARVRANVELA RLRDHHLRWR TALIDSLQEA
     FFVCDESGTV VEINAAFTDI LGYGPEGLPY APVHPWWPHA PADPGAYEQV GDAFARLLES
     PRGSYTVPVT HRDGHRLWVA VNFNKAEDPN TGRGVTVGTF RDVTAEHYAV QRETALAALS
     TSLSRAADLP EALSAALHVL RSLWHARVVV AAVFGGGDTP ALTATDATLR WEDLPAARRE
     ALTALRDRPS LTVVAEDSGA GVRLEHPESP MVVWVDLEGH RPFGSEDQLL LSLLAGHLAQ
     GLGRAHQIDQ QRETAIALQR AILGPARLPE GFAVRYEPAT RPLEVGGDWY DTVTLPDGRI
     GIVVGDCVGR GLEAASVMGQ LRSACRALLL QDPSPARTLT ALDQFAAGVA GAICTTVFCG
     VLEPGSGELT YSSAGHPPGI LVHPDGSSRL LEEGRALPLA VRPGRARPEA TCSLPARATL
     LLYTDGLVER RRRPLSAGME QAGEAVKEGR EMPVEDLATA VMSRLAPAGG YDDDVALLLY
     RHPAPLEMIF PAESSQLAPV RRALRGWLDQ CDLPPTTVQN VLVAAGEACA NAIEHGHRHT
     PGEDVRLRAE ALVDTLRVTV ADSGRWRVPQ RGRNTHRGRG ISLMHALMQE VTVAPGPSGT
     TVDMQMRIA
//
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