ID A0A2W2FPE6_9ACTN Unreviewed; 1429 AA.
AC A0A2W2FPE6;
DT 12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT 12-SEP-2018, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN ORFNames=C1J01_00445 {ECO:0000313|EMBL:PZG23727.1};
OS Nonomuraea aridisoli.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Streptosporangiaceae; Nonomuraea.
OX NCBI_TaxID=2070368 {ECO:0000313|EMBL:PZG23727.1, ECO:0000313|Proteomes:UP000249304};
RN [1] {ECO:0000313|EMBL:PZG23727.1, ECO:0000313|Proteomes:UP000249304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KC333 {ECO:0000313|EMBL:PZG23727.1,
RC ECO:0000313|Proteomes:UP000249304};
RA Sahin N., Saygin H., Ay H.;
RT "Draft genome sequence of Nonomuraea sp. KC333.";
RL Submitted (JAN-2018) 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:PZG23727.1}.
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DR EMBL; POUD01000001; PZG23727.1; -; Genomic_DNA.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000249304; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:InterPro.
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; 7.
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; 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; 7.
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; 7.
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; 7.
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:PZG23727.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000249304};
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 390..442
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 482..534
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 574..626
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 878..1109
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1310..1427
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1..24
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 795..868
FT /evidence="ECO:0000256|SAM:Coils"
FT MOD_RES 1360
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1429 AA; 153321 MW; 2A66E8E93E19D693 CRC64;
MGETAGGTRS AARDTTGRGA GDAMEPELRQ LLAGLTAVRD GDFGTRLPDD ASGLLGEIAQ
VFNGMVDQLS LFTSEVTRVA REVGTEGRLG GQAEVPGVSG TWKDLTESVN AMAGNLTSQV
RSIAEVTTAV AKGDLSQKIT VDARGEILEL KNTVNTMVDQ LSSFADEVTR VAREVGTDGR
LGGQADVKGV AGTWRDLTDS VNYMAGNLTA QVRNISQVAT AVARGDLSQK ITVSARGEIL
ELKNTLNTMV DQLSSFADEV TRVAREVGTD GRLGGQADVK GVSGTWKALT ESVNVMADNL
TAQVRSIAEV TTAVARGDLT QKIRVDARGE ILELKETINT MVDQLSAFAD EVTRVAREVG
TEGQLGGQAT VRGVSGTWKD LTDNVNFMAS NLTGQVRSIA QVATAVAKGD LSQKINVEAK
GEVAALAQTI NTMVDTLSAF ADEVTRVARE VGTEGQLGGQ ARVPNVAGTW KDLTDNVNSM
ADNLTNQVRS IAQVTTAVAR GDLTRKIDVD ARGEILELKE TINTMVDQLS AFAAEVTRVA
REVGSEGRLG GQAEVEGVSG TWKRLTENVN ELAGNLTRQV RAIAEVTSAV TSGDLTRSIT
VDAEGELADL KDNINSMVGS LRETTRANQE QDWLKSNLAR ISGLMQGHRD LSAVAELVMN
ELAPLVSAQY GAFFLAEEAP GGVELHLISA YGYADDAERP TRFKLGQSLV GQAATTRRTI
AMDGVPADYI KISSALGHTA PASVIVLPIV VEEQVLGVIE LGSVYAFTPV HRSFLEQLME
AIGVNVNTII ANARTDELLQ RSQRLTQELQ ERSDELQRQQ EELQRSNAEL EEKAALLASQ
NRDIETKNLE IEQARQELET RARELALASK YKSEFLANMS HELRTPLNSL LILAQLLAQN
HTRNLTPKQV EYASIIHSAG SDLLQLINDI LDLSKVEAGK MDISPERVPL RQLLDDIEAT
FRPMTMQKSL DFAVTTAAGV PVDVLTDDSR LRQILRNLLS NAVKFTETGS VELHIEPVAP
GEVPTSVREH GAAIAFRIKD TGIGIAEQQL EVIFGAFQQA DGTTSRKYGG TGLGLSISRE
IAHLLGGAIT AESAPGKGSV FTLYLPVARP DFEESPGHAA VRSERPAHAD GVAAIPPPAP
PPQQQRRLLV VEERDRGLLS LVAESAVADL SNNRDLGDPR GPIEVVTAVG VQEAAAALAA
QAYHCIVLEL DMADGAALRF LENMDGDSAL RGVPVLAYNN WRLDPRQESN LQARTGTQPL
ELLSSLDELR ERIALHLSAD GPGDVLPLVR HEEMPRSVAQ KVDDTFAGRT VLVVDDDARN
LYALTGMLEI HGMQVLHAEN GRKGIEVLTA HPEIDIVLMD VMMPDMDGYA ATAAIRQMPQ
YAEMPIITVT AKAMPGDQEK SLASGASDYV TKPVDADELL GKIQRWLAS
//
