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Database: UniProt
Entry: A0A1E7NF46_KITAU
LinkDB: A0A1E7NF46_KITAU
Original site: A0A1E7NF46_KITAU 
ID   A0A1E7NF46_KITAU        Unreviewed;      1151 AA.
AC   A0A1E7NF46;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-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=HS99_0001050 {ECO:0000313|EMBL:OEV39331.1};
OS   Kitasatospora aureofaciens (Streptomyces aureofaciens).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Kitasatospora.
OX   NCBI_TaxID=1894 {ECO:0000313|EMBL:OEV39331.1, ECO:0000313|Proteomes:UP000037395};
RN   [1] {ECO:0000313|EMBL:OEV39331.1, ECO:0000313|Proteomes:UP000037395}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10762 / DSM 40127 / CCM 3239 / JCM 4008 / LMG 5968 / NBRC
RC   12843 / NCIMB 8234 / A-377 {ECO:0000313|Proteomes:UP000037395};
RA   Zhang J.E., Yang H., Guo J., Deng Z., Luo H., Luo M., Zhao B.;
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000037395}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10762 / DSM 40127 / CCM 3239 / JCM 4008 / LMG 5968 / NBRC
RC   12843 / NCIMB 8234 / A-377 {ECO:0000313|Proteomes:UP000037395};
RA   Gradnigo J.S., Johnson N., Somerville G.A.;
RT   "Sequencing, assembly and comparative genomics of S. aureofaciens ATCC
RT   10762.";
RL   Submitted (AUG-2016) 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:OEV39331.1}.
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DR   EMBL; JPRF03000001; OEV39331.1; -; Genomic_DNA.
DR   RefSeq; WP_050367010.1; NZ_JPRF03000001.1.
DR   AlphaFoldDB; A0A1E7NF46; -.
DR   Proteomes; UP000037395; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma 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; cd06225; HAMP; 4.
DR   CDD; cd16922; HATPase_EvgS-ArcB-TorS-like; 1.
DR   CDD; cd00082; HisKA; 1.
DR   CDD; cd17546; REC_hyHK_CKI1_RcsC-like; 1.
DR   Gene3D; 1.10.287.130; -; 1.
DR   Gene3D; 1.20.120.1530; -; 3.
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; 1.
DR   InterPro; IPR011006; CheY-like_superfamily.
DR   InterPro; IPR003018; GAF.
DR   InterPro; IPR029016; GAF-like_dom_sf.
DR   InterPro; IPR003660; HAMP_dom.
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; IPR004358; Sig_transdc_His_kin-like_C.
DR   InterPro; IPR001789; Sig_transdc_resp-reg_receiver.
DR   PANTHER; PTHR45339; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   PANTHER; PTHR45339:SF1; HYBRID SIGNAL TRANSDUCTION HISTIDINE KINASE J; 1.
DR   Pfam; PF13185; GAF_2; 1.
DR   Pfam; PF00672; HAMP; 4.
DR   Pfam; PF02518; HATPase_c; 1.
DR   Pfam; PF00512; HisKA; 1.
DR   Pfam; PF00072; Response_reg; 1.
DR   PRINTS; PR00344; BCTRLSENSOR.
DR   SMART; SM00065; GAF; 1.
DR   SMART; SM00304; HAMP; 4.
DR   SMART; SM00387; HATPase_c; 1.
DR   SMART; SM00388; HisKA; 1.
DR   SMART; SM00448; REC; 1.
DR   SUPFAM; SSF55874; ATPase domain of HSP90 chaperone/DNA topoisomerase II/histidine kinase; 1.
DR   SUPFAM; SSF52172; CheY-like; 1.
DR   SUPFAM; SSF55781; GAF domain-like; 1.
DR   SUPFAM; SSF158472; HAMP domain-like; 1.
DR   SUPFAM; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 1.
DR   PROSITE; PS50885; HAMP; 4.
DR   PROSITE; PS50109; HIS_KIN; 1.
DR   PROSITE; PS50110; RESPONSE_REGULATORY; 1.
PE   4: Predicted;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW   Coiled coil {ECO:0000256|SAM:Coils};
KW   Kinase {ECO:0000256|ARBA:ARBA00022777, ECO:0000313|EMBL:OEV39331.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000037395};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          28..74
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          114..166
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          206..258
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          298..350
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          601..832
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1032..1149
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          845..869
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          522..591
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         1082
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1151 AA;  122418 MW;  131621EC150278AC CRC64;
     MAGPTTSNGS QHRPAIGPDA ALGNEPELRQ LLAGLTAVRD GDFSTKLPDD AHGLLGEIAS
     VFNGMVDQLS HFTSEVTRVA REVGTEGRLG GQAQVPGVSG TWADLTDSVN AMAGNLTWQV
     RGIAQVTTAV ARGDLTQKIE VDARGEILEL KNTVNTMVDQ LSSFAGEVTR VAREVGTEGI
     LGGQARVVGV SGTWRDLTDS VNSMAGNLTG QVRAIAQVAT AVAEGDLSQK ITVTARGEIL
     ELKETINTMV DQLSSFADEV TRVAREVGTE GRLGGQAKVE GVSGTWKRLT ENVNELAGNL
     TRQVRAIAEV TSAVAAGDLT RSITVDASGE VADLKDNVNF MVESLRETTR ANEEQDWLKT
     NLARFSALMQ GRRDLGVVAE SVMDELAPLV EAQCGAFYLA EDSPEGTVLQ LVGSYAFPDG
     ERPTRFRLGE SFVGQAARSR RTIAVDALPA GYLPASSGLG RTDSLSLLVL PIVVEDQVLG
     VIELASVQPF TQVHRDFLNQ LMETIGVNVN TIIANARTDE LLGESQRLAA ELQARSEELQ
     ARQEELQFSN AELEDKAELL AAQNRDIETK NLEIEQARQE LEERAHQLSL ASKYKSEFLA
     NMSHELRTPL NSLLILAQLL AQNPTRNLTA KQVEYAGIIH SAGSDLLQLI NDILDLSKVE
     AGKMDLNVDA VPLHALLDYV EATFRPLTGQ KNLAFAVRTA PGVPGELLTD DYRLRQVLRN
     LLSNAVKFTE HGRVELRIEP ATDAELPDGV RRGGPVLAFR VTDTGIGIAP QHLETVFGAF
     QQADGTTSRK YGGTGLGLSI SREIAFLLGG AITVESTLGR GTVFTLYLPV EHSVVAGSEL
     PPAAGAPAGA AAGPAPEQPV DPADHPTTER PRRLLVVEGR PNGLLTLVAE NAVADLARYS
     AGHRQVEIVT AVGAQDAATA LATAPCHCVV LELDLPDGTA GALLADMEGD PALHTVPVLA
     HNNRGVTGER AGSVSRPGER PLELIASLDE LRGRIALHMS ADRPGGALPP GRGADLVPSW
     SPDAEPALAG RTALVVDDDD RNLYAITSIL ELHGMRVLQA ENGRAALESL TVHPGIDVIL
     MDVMMPEMDG YTATAAIRAM PEHAGLPIIA VTAKAMIGDR EKSLAAGASD YITKPVDADE
     VISRITHHLT R
//
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