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Database: UniProt
Entry: A0A1E5PL50_9ACTN
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ID   A0A1E5PL50_9ACTN        Unreviewed;      1522 AA.
AC   A0A1E5PL50;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 39.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=BGK67_01800 {ECO:0000313|EMBL:OEJ30260.1};
OS   Streptomyces subrutilus.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=36818 {ECO:0000313|EMBL:OEJ30260.1, ECO:0000313|Proteomes:UP000095705};
RN   [1] {ECO:0000313|EMBL:OEJ30260.1, ECO:0000313|Proteomes:UP000095705}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=10-1-1 {ECO:0000313|EMBL:OEJ30260.1,
RC   ECO:0000313|Proteomes:UP000095705};
RA   Chen X.;
RT   "The complete genome of Streptomyces subrutilus 10-1-1.";
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:OEJ30260.1}.
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DR   EMBL; MEHK01000001; OEJ30260.1; -; Genomic_DNA.
DR   RefSeq; WP_069918404.1; NZ_MEHK01000001.1.
DR   STRING; 36818.BGK67_01800; -.
DR   OrthoDB; 9810730at2; -.
DR   Proteomes; UP000095705; 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; 8.
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; -; 5.
DR   Gene3D; 3.30.450.40; -; 1.
DR   Gene3D; 3.40.50.2300; -; 1.
DR   Gene3D; 6.10.340.10; -; 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; 8.
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; 8.
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; SSF47384; Homodimeric domain of signal transducing histidine kinase; 1.
DR   SUPFAM; SSF58104; Methyl-accepting chemotaxis protein (MCP) signaling domain; 3.
DR   PROSITE; PS50885; HAMP; 8.
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:OEJ30260.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000095705};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          16..68
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          108..160
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          200..252
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          292..344
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          384..436
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          476..528
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          568..620
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          660..712
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          963..1194
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1394..1511
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   REGION          1199..1230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          894..953
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         1444
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1522 AA;  161776 MW;  059F0586151CA76F CRC64;
     MVKPTDVVTS AQASGAVGEQ QLRQLLAGLT SVRDGDFGTR LPDEAEGLLG EIATVFNGMV
     DQLSLFTSEV TRVAREVGTE GTLGGQAVVP GVSGTWADLT DSVNAMAGNL TTQVRDIAQV
     ATAVARGDLS QKIDVAARGE ILELKDTVNT MVDQLSSFAD EVTRVAREVG SEGRLGGQAE
     VPGVAGVWRD LTDSVNFMAG NLTDQVRNIA QVTTAVAKGD LSQKIAVDAR GEILELKNTI
     NTMVDQLSAF ADEVTRMARE VGTDGRLGGQ ADVKGVSGTW RDLTDSVNFM AGNLTAQVRS
     IAEVATAVAQ GDLSQKIRVD ARGEILELKT TINTMVDQLS AFADEVTRVA REVGTDGRLG
     GQADVKGVSG TWRDLTDSVN FMADNLTAQV RSIAEVTTAV AQGDLTQKIR VDARGEILEL
     KETINTMVDQ LSAFADEVTR VAREVGTEGN LGGQATVRGV SGTWKDLTDN VNVMASNLTG
     QVRSIAQVAT AVARGDLSQK IVVEAKGEVA ALAGVINTMV DTLSAFADEV TRVAREVGTE
     GRLGGQAQVP NVAGTWKDLT DNVNSMANNL TGQVRNIALV TTAVANGDLS KKIDVDARGE
     ILELKTTINT MVDQLSAFAA EVTRVAREVG SEGRLGGQAE VEGVSGTWKR LTENVNELAG
     NLTRQVRAIA EVASAVAEGD LTRSITVDAS GEVAELKDNI NSMVGSLRET TRANQEQDWL
     KSNLAQISGL MQGHRDLEVV AELVMDELVP LVEASYGAFY LAEEADGETW LALIGSFGRP
     IDSPAAQRVR NGETLVGQAV RSRRILSTDN VPAGYLISSG LGAAAPANLI VLPIIVEDQV
     LGVIELASFQ PFTPVHRDFL SRLMETVGVN VSTIVANART DELLGESQRL TGELQARSEQ
     LQVQQDELQR SNAELEEKAA LLATQNRDIE TKNLEIEQAR QELEDRAQQL SLASKYKSEF
     LANMSHELRT PLNSLLILAQ LLAQNPGRNL TPKQVEYAGI IHSAGSDLLQ LINDILDLSK
     VEAGKMDVNL ERVSLKKLLD YVEASFRPLT TQKGLDFDIT TSPGVPVDLL TDDARLQQIL
     RNLLSNAVKF TERGRVQVRI EPANAAELPE ELARSGSVVA FKVDDTGIGI AEEQLEVIFA
     AFQQADGTTS RKFGGTGLGL SITREIARLL GGIVTATSTP GVGSTFTLYL PVTGAGSSDH
     GAGAPALEGS TDGDEKSDGG SADPAADSHP RRLLVIEERA NGLLSLVAES AASDVTAGRA
     ASDLAEQVEV VTALTSGDAA TMLAQSPFHC VVLELDAKGE ALRFLRALSG DTALASLPVL
     AHANRRMAAD VHEEVARLAN GHHLEVLSSL DELRERIALH LSVERLRDVL PLVRPEGDQV
     ADHPHVDASL ADKSVLVVDD DPRNLYAISG ILELHGIRVL HAENGRKGIE TLTSTPGIDL
     ILMDVMMPEL DGYAATEEIR GMPEYAGLPI ISVTAKAMPG DREKSIASGS SDYITKPVDA
     NDLVALLRQW LLPKDAAGAS RV
//
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