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Database: UniProt
Entry: A0A0D0V0T8_9ACTN
LinkDB: A0A0D0V0T8_9ACTN
Original site: A0A0D0V0T8_9ACTN 
ID   A0A0D0V0T8_9ACTN        Unreviewed;      1455 AA.
AC   A0A0D0V0T8;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   24-JAN-2024, entry version 46.
DE   RecName: Full=histidine kinase {ECO:0000256|ARBA:ARBA00012438};
DE            EC=2.7.13.3 {ECO:0000256|ARBA:ARBA00012438};
GN   ORFNames=TK50_03105 {ECO:0000313|EMBL:KIR64637.1};
OS   Micromonospora haikouensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Micromonosporales;
OC   Micromonosporaceae; Micromonospora.
OX   NCBI_TaxID=686309 {ECO:0000313|EMBL:KIR64637.1, ECO:0000313|Proteomes:UP000032254};
RN   [1] {ECO:0000313|EMBL:KIR64637.1, ECO:0000313|Proteomes:UP000032254}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JXNU-1 {ECO:0000313|EMBL:KIR64637.1,
RC   ECO:0000313|Proteomes:UP000032254};
RA   Long Z., Huang Y., Jiang Y.;
RT   "Sequencing and annotation of Micromonospora carbonacea strain JXNU-1
RT   genome.";
RL   Submitted (JAN-2015) 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:KIR64637.1}.
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DR   EMBL; JXSX01000001; KIR64637.1; -; Genomic_DNA.
DR   RefSeq; WP_043961316.1; NZ_JXSX01000001.1.
DR   PATRIC; fig|47853.6.peg.665; -.
DR   OrthoDB; 9810730at2; -.
DR   Proteomes; UP000032254; 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; 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; -; 7.
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; PF18947; HAMP_2; 1.
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; 9.
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; 9.
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:KIR64637.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW   Phosphoprotein {ECO:0000256|ARBA:ARBA00022553, ECO:0000256|PROSITE-
KW   ProRule:PRU00169}; Reference proteome {ECO:0000313|Proteomes:UP000032254};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          21..66
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          106..163
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          203..255
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          295..347
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          387..439
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          479..531
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          571..623
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          663..715
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          755..807
FT                   /note="HAMP"
FT                   /evidence="ECO:0000259|PROSITE:PS50885"
FT   DOMAIN          1051..1284
FT                   /note="Histidine kinase"
FT                   /evidence="ECO:0000259|PROSITE:PS50109"
FT   DOMAIN          1329..1446
FT                   /note="Response regulatory"
FT                   /evidence="ECO:0000259|PROSITE:PS50110"
FT   COILED          972..1041
FT                   /evidence="ECO:0000256|SAM:Coils"
FT   MOD_RES         1379
FT                   /note="4-aspartylphosphate"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00169"
SQ   SEQUENCE   1455 AA;  156077 MW;  203DC88DAC54DFB0 CRC64;
     MTTAKHPVAA DPSAPDQAAL LGELAEALRR VRGGDLKVRL RPRAGAAGEV ADAFNEVVAL
     QERQHRDLLR ISRVVGRDGR LNERLEEEGL EGSWAEDQRA VNSLIDGLGR PTTEIARVIV
     AVADGDLSQH MALEIDGRPL RGEYLRIGRT VNTMVDQLSS FSNEVTRVAR EVGTEGKLGG
     QADVRGVAGT WKDLTDSVNT MASNLTGQVR SISQVATAVA RGDLSQKITV GARGEVAELA
     DTMNSLTDTL RLFAEQVTRV AREVGTEGKL GGQADVPNVA GTWKDLTDSV NSMASNLTAQ
     VRNIAQVSTA VARGDLSQKI TVAAQGEILE LKDTVNTMVD QLSSFADEVT RVAREVGSEG
     KLGGQAQVRG VSGTWRDLTE NVNQLAGNLT SQVRNISQVS TAVAKGDLSQ KITVDAQGEI
     LELKNTVNTM VDQLSSFADE VTRVAREVGT EGKLGGQAQV RGVAGTWRDL TDNVNSMASN
     LTAQVRNIAS VTTAVAKGDL SQKITVDARG EILELKSTVN TMVDQLSSFA DEVTRVAREV
     GTEGKLGGQA QVKGVLGTWR DLTDNVNSMA SNLTSQVRNI ASVTTAVAKG DLSQKITVDA
     RGEILELKST VNTMVDQLSS FADEVTRVAR EVGTEGKLGG QAQVKGVSGT WRDLTDNVNS
     MGSNLTSQVR NIASVTTAVA KGDLSQKITV DAQGEILELK NTVNTMVDQL RSFADEVTRV
     GREVGIEGKL GAQAQVKGVS GTWRDLTENV NQLASTLTTQ LRAIAEVSTS VTRGDLTQRI
     AVEAQGEVAD LKDNINQMIV TLRETTKKNA EQGWLDSNLA RIGGLLQGQR DLGEVCRMIM
     MEVTPLVDAQ LGAFFLADTS DGSMRLRLTA SYGYVARGHD VTFGPGEGLV GQAALSRRTI
     RVSASPDGRL TLRSGLANTP PADLVVLPVL FEGELLGVIE FAGVAAFPDL HLTFLERLVL
     TIGVAVNTIQ ANRRTEELLA QSQRLAHELQ EQSAELQRTN AELEDKAQLL SEQKANIETQ
     NREIELARLG LEDKAQQLTR ASAYKSEFLA NMSHELRTPL NSLLLLARLL VENSEQNLTP
     KQIEFARTIH GSGSDLLRLI DDILDLSKIE AGRMDVEPTE VQFTEIRGFV EQAFAPQAEE
     KGLDFQVRLA KELPPALVTD AQRLQQILRN LLSNAVKFTD NGAVTLRIAP APENVVFDVP
     ALTNARQVIA FTVIDTGIGI SDDKLSLIFE AFQQADGTTS RRYGGTGLGL SISRDLARLL
     GGSITVSSAP GEGSTFTLYV PEVLAPDAVV APAPPSPARA GLPSSLLMPP LELPEPAEAP
     GTRRLEGVTV LIIDDDVRNV FALTSALELH GMTVLYSDNG ADGVRLLAEH PEVDIVLMDA
     MMPDQDGYET TRQIRRNHHF ADLPIVFLTA KAMPGDRESA LAAGGSDYIT KPVDLDELIE
     LMSSWVSGSR GEESS
//
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