ID A0A2M9K1Y3_9ACTN Unreviewed; 1837 AA.
AC A0A2M9K1Y3;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=CG723_00025 {ECO:0000313|EMBL:PJN13037.1};
OS Streptomyces sp. CB01635.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=2020326 {ECO:0000313|EMBL:PJN13037.1, ECO:0000313|Proteomes:UP000232157};
RN [1] {ECO:0000313|Proteomes:UP000232157}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CB01635 {ECO:0000313|Proteomes:UP000232157};
RA Pan G., Xu Z., Guo Z., Ma M., Yang D., Zhou H., Gansemans Y., Zhu X.,
RA Zhao L.-X., Jiang Y., Cheng J., van Nieuwerburgh F., Suh J.W., Duan Y.,
RA Shen B.;
RT "Discovery of the Leinamycin Family of Natural Products by Mining
RT Actinobacterial Genomes.";
RL Proc. Natl. Acad. Sci. U.S.A. 114:0-0(2017).
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:PJN13037.1}.
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DR EMBL; NNBL01000001; PJN13037.1; -; Genomic_DNA.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000232157; 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; 10.
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; -; 8.
DR Gene3D; 3.30.450.40; -; 1.
DR Gene3D; 3.40.50.2300; -; 1.
DR Gene3D; 1.10.8.500; HAMP domain in histidine kinase; 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; 10.
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; 12.
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; 5.
DR PROSITE; PS50885; HAMP; 12.
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:PJN13037.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000232157};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 35..84
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 124..186
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 226..278
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 318..370
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 410..462
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 502..554
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 594..646
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 686..738
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 778..830
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 870..922
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 962..1014
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1054..1106
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 1366..1607
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1717..1834
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1662..1708
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 1287..1356
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1682..1700
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1767
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1837 AA; 197085 MW; 894DB5BE4FA5C12E CRC64;
MESGAASRGT NTRAKGGQSL AKQRKPRNGT TAVDTAALNR LLAGLVAMRD GNFRKRLTVS
GDGLMTEIAA VFNEVADRNL HLTGELSRVR RMVGREGKLT ERLETGACEG SWAAAINASN
ALVDDLVRPV SEVGRVLTAV AEGDLSPRME LRSQVPDGNG HPLRGEFLKV GRTVNNLVDQ
LSTFTDEVTR VASEVGTEGK LGGQARVRGM SGSWKDLTDS VNTMAYRLTA QVRDIALVTT
AVAKGDLSRK VTVHVAGEML ELKNTVNTMV DQLSSFSSEV TRVAREVGTE GELGGQAQVP
GVAGVWKDLT DSVNLMAGNL TAQVRGIAQV TTAVANGDLS QKVTVSARGE VAQLAETINQ
MTETLRTFAD EVTRVANEVG AEGQLGGQAN VPGAAGTWKD LTDSVNTVFR NLTTQVRDIA
TVTTAVANGD LSQKVTVDVA GEMLELKNTV NTMVDQLSAF GSEVTRVARE IGVEGELGGQ
AHVQGAAGTW KDLTDSVNTA FRNLTGQVRN IAQVTTAVAN GDLSQKVTVD VSGEMLQLKN
TVNTMVDQLS SFADQVTRMA RDVGTEGRLG GQARVDGVSG TWKELTDSVN FMAGNLTSQV
RQIAQVTTAV ARGDLSQKID VDARGEILEL KNTINTMVDQ LSAFADQVTR VAREVGTEGR
LGGQAQVPGV AGVWRDLTDS VNGMAGNLTA QVRNIAQVAT AVARGDLSQK IDVDARGEIL
ELKNTLNTMV DQLSNFAEQV TRVSREVGTE GILGGQAEVQ GVSGTWKDLT QSVNGMANNL
TLQVRNIAEV TTAVARGDLS KKITVDAKGE ILELVTTVNT MVDQLSSFAE QVTRVAREVG
TEGQLGGQAR VRGVTGIWKD LSDNVNLMAN NLTSQVRNIS QVATAVANGD LTKKVTVEAR
GEVAQLADTV NTMVTTLSSF ADQVTRVARE VGTDGILGGQ ARVPGVSGTW KDLTESVNGM
ASNLTGQVRN IAMVTTAIAK GDLTKKIDID ARGEILELKT TINTMVDQLS SFAEQVTRVA
REVGTEGQLG GQARVRDVDG TWRDLTESVN EMAGNLTRQV RAIAAVATAV TRGDLNLKID
VDAAGEIQVL QDNINKMISN LRDTTIANEE QDWLKGNLAR ISGLMQGRRD LEDVASLIMS
ELTPVVSAQH GAFFLALPTD EAEAGGAPED AYELRMLGSY GYSMGSMPTS FRPGETLIGT
AAQERRAILV ENVPQGYLKI ASGLGEAPPA HVIVLPVLFE GTVLGVIELA TFQPFTQIQK
DFLNQIAEMI ATSVNTISVN TKTEVLLKQS QELTEQLRER SAELENRQKA LQASNAELEE
KAELLAQQNR DIEVKNTEIE EARQVLEERA EQLAVSMRYK SEFLANMSHE LRTPLNSLLI
LAKLLADNAD SNLTPKQVEF AETIHGAGSD LLQLINDILD LSKVEAGKMD VSPTRIALVQ
LVDYVEATFR PLTAEKGLDF SVRVSPELPA TLHTDEQRLL QVLRNLLSNA VKFTDSGAVE
LVIRPAGADV PNAIREQLLE AGSLREADGD LIAFSVTDTG IGIAASKMRV IFEAFKQADG
TTSRKYGGTG LGLSISREIA RLLGGEIHAQ SEPGRGSTFT LYMPLHASEL PPQGYPQLAP
SIEPGMYAVP MEGAMPTEAS MPPEVRSYQD TQHGPAALFR RRRKQVAAPE QRPALPGQPE
QQAPVAPSQD RAQEQWAGTG QEGAPQERRT FLFGGEKVLI VDDDIRNVFA LTSVLEQHGL
SVLYAENGRE GIEVLEQHDD VTVVLMDIMM PEMDGYATTT AIRRMPQFAG LPIIALTAKA
MKGDREKAIE SGASDYVTKP VDPDHLLTVM EQWMRGE
//
