ID D7B8S4_NOCDD Unreviewed; 1478 AA.
AC D7B8S4;
DT 10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT 10-AUG-2010, sequence version 1.
DT 27-MAR-2024, entry version 81.
DE RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN OrderedLocusNames=Ndas_5202 {ECO:0000313|EMBL:ADH70582.1};
OS Nocardiopsis dassonvillei (strain ATCC 23218 / DSM 43111 / CIP 107115 / JCM
OS 7437 / KCTC 9190 / NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509)
OS (Actinomadura dassonvillei).
OG Plasmid pNDAS01 {ECO:0000313|Proteomes:UP000002219}.
OC Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC Nocardiopsaceae; Nocardiopsis.
OX NCBI_TaxID=446468 {ECO:0000313|EMBL:ADH70582.1, ECO:0000313|Proteomes:UP000002219};
RN [1] {ECO:0000313|EMBL:ADH70582.1, ECO:0000313|Proteomes:UP000002219}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 23218 / DSM 43111 / CIP 107115 / JCM 7437 / KCTC 9190 /
RC NBRC 14626 / NCTC 10488 / NRRL B-5397 / IMRU 509
RC {ECO:0000313|Proteomes:UP000002219};
RC PLASMID=Chromosome 2 {ECO:0000313|Proteomes:UP000002219};
RX PubMed=21304737; DOI=10.4056/sigs.1363462;
RA Sun H., Lapidus A., Nolan M., Lucas S., Del Rio T.G., Tice H., Cheng J.F.,
RA Tapia R., Han C., Goodwin L., Pitluck S., Pagani I., Ivanova N.,
RA Mavromatis K., Mikhailova N., Pati A., Chen A., Palaniappan K., Land M.,
RA Hauser L., Chang Y.J., Jeffries C.D., Djao O.D., Rohde M., Sikorski J.,
RA Goker M., Woyke T., Bristow J., Eisen J.A., Markowitz V., Hugenholtz P.,
RA Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Nocardiopsis dassonvillei type strain (IMRU
RT 509).";
RL Stand. Genomic Sci. 3:325-336(2010).
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};
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DR EMBL; CP002041; ADH70582.1; -; Genomic_DNA.
DR RefSeq; WP_013156189.1; NC_014211.1.
DR STRING; 446468.Ndas_5202; -.
DR KEGG; nda:Ndas_5202; -.
DR eggNOG; COG0745; Bacteria.
DR eggNOG; COG1511; Bacteria.
DR eggNOG; COG2203; Bacteria.
DR eggNOG; COG4251; Bacteria.
DR HOGENOM; CLU_000445_3_2_11; -.
DR OrthoDB; 9810730at2; -.
DR Proteomes; UP000002219; Chromosome 2.
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; 6.
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; -; 4.
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; PF18947; HAMP_2; 2.
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:ADH70582.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000002219};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 13..60
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 100..157
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 197..249
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 289..341
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 381..433
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 473..525
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 565..617
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 657..709
FT /note="HAMP"
FT /evidence="ECO:0000259|PROSITE:PS50885"
FT DOMAIN 960..1193
FT /note="Histidine kinase"
FT /evidence="ECO:0000259|PROSITE:PS50109"
FT DOMAIN 1305..1422
FT /note="Response regulatory"
FT /evidence="ECO:0000259|PROSITE:PS50110"
FT REGION 1198..1234
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1274..1298
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1432..1478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 874..950
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 1464..1478
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1355
FT /note="4-aspartylphosphate"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ SEQUENCE 1478 AA; 160113 MW; F999085B13E106CF CRC64;
MPEAVKELAA DDQLDEILRA LYRMRDGDFS VRLRKRGGGT MREIASVFNE VVDHSEQLSD
ELQRVGDVVR NEGRLNERVN VNPARGAWGE SAQALNLLLD EVAEPVTDVA GVLDSVAEGQ
LSRRASTEGR RGELKGDLLR LATTVNRMAD QMSGFAGEVT RVAREVGTEG KLGGTAQVEG
VSGAWREVTE SVNQMSSRLT DQMRDISEVT TAVARGDLSR KITVDVQGEM LDLKDTVNTM
VDQLSTFADE VTRVAREVGT EGKLGGRANV RGVRGIWKDL TENVNSMADN LTNQVRDISQ
VTTSVARGDL TQKVQVDVQG EMLALKNTVN TMVDQLDSFA DEVTRVAREV GTEGKLGGRA
NVKGVSGIWK DLTDNVNSMA NSLTYQVRNI SQVTTAVATG DLTKKITVDA QGEMLDLKDT
INKMVDQLDS FAGEVTRVAR EVGTEGKLAG QAHVRDVSGV WKDLTDNVNS MANNLTYQVR
QISMVTRAVA AGDLTKKVTV NAKGEILELK DTINVMVDQL SAFADEVTRV AREVGTEGKL
GGRADVKGVS GIWNDLTENV NSMSHNLTTQ VRNISEVTTA VAAGDLNKKI DVNAQGEILE
LKTTVNTMVD QLSAFATEVT RVAHEVGSQG QLGGQAKVEG VTGTWKQLTD SVNGLAGNLT
TQVRAIAEVA NAVAKGDLTR NIQVDARGEM EQLKHNINLM VSNLRETTAT QRDADWLKSN
VARISGHIQG HRDLKELARL IMTEVTPLIG AQHGACYLPE DQDDQENFLF YAGFGFDPDE
DRRRVRAGIG LVGEALAQQV EQQISNIPPD YVKVRSGLGE ASPRNLYILP IVSEGRSLGA
IEFASYDDFR ESHKNFLRQL VSLLGTTINT ILANNRTEDL LEQSQQLTSQ LRERSNELQR
QQEELRGKNA ELRQKATQLA NQNRAIELQN QQIQRSRNAL EERAHQLQVS SKYKSEFLAN
MSHELRTPLN SLLILARLLA DNAEQNLSAK QVEFAQTIHK AGSDLLLLID EILDLSKVEA
GRAEVQPSEV SIAQLVDYVE ATFRPVTGDQ GLAFAVDVSP DIPGTLWTDE QRLQQILRNL
LSNAVKFTPQ GEVRLLIEPA WALEDADLEM FVENEEVIAF TVADTGIGIA EDKLQVIFEA
FHQGDGGTSR RFGGTGLGLS ISRNFARLLG GEIRVQSVPN QGSTFTLLLP VRLPDDAGER
AEEAGSPIRG LSGMDSAPML DSGRGADTGG FGSSPLDDGF SMPDEDFDAA LAALTDISDE
PLPTVPVLKA PETHAAAAEG EAPEQPAESE PRTDPERRAV LSGQRVLIVD DDVRNVFALT
SALEAQGLEV LYADNGHAGI AKLEANEDIA LVLMDVMMPE LDGNQTTQRI REMPQFAGLP
IISLTAKAMQ GDRERSLAAG ATDYVTKPVD LDHLLDVMRR WLTAGREETI AGAAADGGGG
AVPDGHSRAT SGPEEAGAGH DNDPNGETGT STPSEDLE
//
